Flavonoid hydroxylase from Catharanthus roseus: cDNA, heterologous expression, enzyme properties and cell-type specific expression in plants
We investigated the P450 dependent flavonoid hydroxylase from the ornamental plant Catharanthus roseus. cDNAs were obtained by heterologous screening with the CYP75 Hf1 cDNA from Petunia hybrida. The C. roseus protein shared 68-78% identity with other CYP75s, and genomic blots suggested one or two g...
Saved in:
Published in | The Plant journal : for cell and molecular biology Vol. 19; no. 2; pp. 183 - 193 |
---|---|
Main Authors | , , , , |
Format | Journal Article |
Language | English |
Published |
Oxford, UK
Blackwell Science Ltd
01.07.1999
Blackwell Science |
Subjects | |
Online Access | Get full text |
Cover
Loading…
Abstract | We investigated the P450 dependent flavonoid hydroxylase from the ornamental plant Catharanthus roseus. cDNAs were obtained by heterologous screening with the CYP75 Hf1 cDNA from Petunia hybrida. The C. roseus protein shared 68-78% identity with other CYP75s, and genomic blots suggested one or two genes. The protein was expressed in Escherichia coli as translational fusion with the P450 reductase from C. roseus. Enzyme assays showed that it was a flavonoid 3',5'-hydroxylase, but 3'-hydroxylated products were also detected. The substrate specificity was investigated with the C. roseus enzyme and a fusion protein of the Petunia hybrida CYP75 with the C. roseus P450 reductase. Both enzymes accepted flavanones as well as flavones, dihydroflavonols and flavonols, and both performed 3'- as well as 3'5'-hydroxylation. Kinetics with C. roseus cultures on the level of enzyme activity, protein and RNA showed that the F3'5'H was present in dark-grown cells and was induced by irradiation. The same results were obtained for cinnamic acid 4-hydroxylase and flavanone 3beta-hydroxylase. In contrast, CHS expression was strictly dependent on light, although CHS is necessary in the synthesis of the F3'5'H substrates. Immunohistochemical localization of F3'5'H had not been performed before. A comparison of CHS and F3'5'H in cotyledons and flower buds from C. roseus identified CHS expression preferentially in the epidermis, while F3'5'H was only detected in the phloem. The cell-type specific expression suggests that intercellular transport may play an important role in the compartmentation of the pathways to the different flavonoids. |
---|---|
AbstractList | We investigated the P450 dependent flavonoid hydroxylase from the ornamental plant Catharanthus roseus. cDNAs were obtained by heterologous screening with the CYP75 Hf1 cDNA from Petunia hybrida. The C. roseus protein shared 68-78% identity with other CYP75s, and genomic blots suggested one or two genes. The protein was expressed in Escherichia coli as translational fusion with the P450 reductase from C. roseus. Enzyme assays showed that it was a flavonoid 3', 5'-hydroxylase, but 3'-hydroxylated products were also detected. The substrate specificity was investigated with the C. roseus enzyme and a fusion protein of the Petunia hybrida CYP75 with the C. roseus P450 reductase. Both enzymes accepted flavanones as well as flavones, dihydroflavonols and flavonols, and both performed 3'- as well as 3'5'-hydroxylation. Kinetics with C. roseus cultures on the level of enzyme activity, protein and RNA showed that the F3'5'H was present in dark-grown cells and was induced by irradiation. The same results were obtained for cinnamic acid 4-hydroxylase and flavanone 3beta-hydroxylase. In contrast, CHS expression was strictly dependent on light, although CHS is necessary in the synthesis of the F3'5'H substrates. Immunohistochemical localization of F3'5'H had not been performed before. A comparison of CHS and F3'5'H in cotyledons and flower buds from C. roseus identified CHS expression preferentially in the epidermis, while F3'5'H was only detected in the phloem. The cell-type specific expression suggests that intercellular transport may play an important role in the compartmentation of the pathways to the different flavonoids. We investigated the P450 dependent flavonoid hydroxylase from the ornamental plant Catharanthus roseus. cDNAs were obtained by heterologous screening with the CYP75 Hf1 cDNA from Petunia hybrida. The C. roseus protein shared 68-78% identity with other CYP75s, and genomic blots suggested one or two genes. The protein was expressed in Escherichia coli as translational fusion with the P450 reductase from C. roseus. Enzyme assays showed that it was a flavonoid 3',5'-hydroxylase, but 3'-hydroxylated products were also detected. The substrate specificity was investigated with the C. roseus enzyme and a fusion protein of the Petunia hybrida CYP75 with the C. roseus P450 reductase. Both enzymes accepted flavanones as well as flavones, dihydroflavonols and flavonols, and both performed 3'- as well as 3'5'-hydroxylation. Kinetics with C. roseus cultures on the level of enzyme activity, protein and RNA showed that the F3'5'H was present in dark-grown cells and was induced by irradiation. The same results were obtained for cinnamic acid 4-hydroxylase and flavanone 3 beta -hydroxylase. In contrast, CHS expression was strictly dependent on light, although CHS is necessary in the synthesis of the F3'5'H substrates. Immunohistochemical localization of F3'5'H had not been performed before. A comparison of CHS and F3'5'H in cotyledons and flower buds from C. roseus identified CHS expression preferentially in the epidermis, while F3'5'H was only detected in the phloem. The cell-type specific expression suggests that intercellular transport may play an important role in the compartmentation of the pathways to the different flavonoids. Summary We investigated the P450 dependent flavonoid hydroxylase from the ornamental plant Catharanthus roseus. cDNAs were obtained by heterologous screening with the CYP75 Hf1 cDNA from Petunia hybrida. The C. roseus protein shared 68–78% identity with other CYP75s, and genomic blots suggested one or two genes. The protein was expressed in Escherichia coli as translational fusion with the P450 reductase from C. roseus. Enzyme assays showed that it was a flavonoid 3′,5′‐hydroxylase, but 3′‐hydroxylated products were also detected. The substrate specificity was investigated with the C. roseus enzyme and a fusion protein of the Petunia hybrida CYP75 with the C. roseus P450 reductase. Both enzymes accepted flavanones as well as flavones, dihydroflavonols and flavonols, and both performed 3′‐ as well as 3′5′‐hydroxylation. Kinetics with C. roseus cultures on the level of enzyme activity, protein and RNA showed that the F3′5′H was present in dark‐grown cells and was induced by irradiation. The same results were obtained for cinnamic acid 4‐hydroxylase and flavanone 3β‐hydroxylase. In contrast, CHS expression was strictly dependent on light, although CHS is necessary in the synthesis of the F3′5′H substrates. Immunohistochemical localization of F3′5′H had not been performed before. A comparison of CHS and F3′5′H in cotyledons and flower buds from C. roseus identified CHS expression preferentially in the epidermis, while F3′5′H was only detected in the phloem. The cell‐type specific expression suggests that intercellular transport may play an important role in the compartmentation of the pathways to the different flavonoids. Summary We investigated the P450 dependent flavonoid hydroxylase from the ornamental plant Catharanthus roseus . cDNAs were obtained by heterologous screening with the CYP75 Hf1 cDNA from Petunia hybrida . The C. roseus protein shared 68–78% identity with other CYP75s, and genomic blots suggested one or two genes. The protein was expressed in Escherichia coli as translational fusion with the P450 reductase from C. roseus . Enzyme assays showed that it was a flavonoid 3′,5′‐hydroxylase, but 3′‐hydroxylated products were also detected. The substrate specificity was investigated with the C. roseus enzyme and a fusion protein of the Petunia hybrida CYP75 with the C. roseus P450 reductase. Both enzymes accepted flavanones as well as flavones, dihydroflavonols and flavonols, and both performed 3′‐ as well as 3′5′‐hydroxylation. Kinetics with C. roseus cultures on the level of enzyme activity, protein and RNA showed that the F3′5′H was present in dark‐grown cells and was induced by irradiation. The same results were obtained for cinnamic acid 4‐hydroxylase and flavanone 3β‐hydroxylase. In contrast, CHS expression was strictly dependent on light, although CHS is necessary in the synthesis of the F3′5′H substrates. Immunohistochemical localization of F3′5′H had not been performed before. A comparison of CHS and F3′5′H in cotyledons and flower buds from C. roseus identified CHS expression preferentially in the epidermis, while F3′5′H was only detected in the phloem. The cell‐type specific expression suggests that intercellular transport may play an important role in the compartmentation of the pathways to the different flavonoids. |
Author | Lutz, V Schroder, J Schmelzer, E Kaltenbach, M Schroder, G |
Author_xml | – sequence: 1 fullname: Kaltenbach, M – sequence: 2 fullname: Schroder, G – sequence: 3 fullname: Schmelzer, E – sequence: 4 fullname: Lutz, V – sequence: 5 fullname: Schroder, J |
BackLink | http://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=1905648$$DView record in Pascal Francis https://www.ncbi.nlm.nih.gov/pubmed/10476065$$D View this record in MEDLINE/PubMed |
BookMark | eNqNUU1v1DAUtFAR3Rb-AviAODXBjmM7Rr1US8uHKkBikbhZrvPS9SobBztLN_wGfjQOWUFvcLKlN_Nm3swJOup8BwhhSnJKSvFyk1MmeMYo-5pTpVROCC_KfP8ALf4MjtCCKEEyWdLiGJ3EuCGESibKR-g4LZGCCL5AP69a89133tV4PdbB78fWRMBN8Fu8NMPaBNMN613EwUfYxVfYvv5wcYbXMEDwrb_1aQT7PkCMzndnGLof4xZwH3wPYXAQselqbKFts2HsAccerGucvUfCrsN9m2TiY_SwMW2EJ4f3FK2uLlfLt9n1xzfvlhfXmeWiLDPeNI2QFYeyVkwWjAoplU2XGatsIQkYpmpieVUJJrm8sdLKshKllIYwStkpejGvTS6_7SAOeuviZNF0kO7RMgXFiaz-CUxxJgFeJGA1A22KKQZodB_c1oRRU6KnxvRGT8XoqRg9NaZ_N6b3ifr0oLG72UJ9jzhXlADPDwATrWmbVIh18S9OkRTK5PV8ht25Fsb_1terT-_TJ9GfzfTGeG1uQ1L48rkglJFCsUJWJfsFkZq-mA |
CitedBy_id | crossref_primary_10_1007_s11101_013_9280_x crossref_primary_10_3389_fpls_2014_00442 crossref_primary_10_1134_S1022795410040071 crossref_primary_10_1146_annurev_arplant_54_031902_134840 crossref_primary_10_1016_j_ymben_2015_07_002 crossref_primary_10_1007_s10529_005_5718_6 crossref_primary_10_1016_j_febslet_2007_06_045 crossref_primary_10_1016_S0031_9422_01_00421_6 crossref_primary_10_1104_pp_108_117457 crossref_primary_10_1186_s12870_014_0347_7 crossref_primary_10_1016_S0163_7258_02_00298_X crossref_primary_10_1186_1471_2164_11_562 crossref_primary_10_1186_1471_2229_10_21 crossref_primary_10_1104_pp_109_142059 crossref_primary_10_1111_j_1399_3054_2004_00407_x crossref_primary_10_1074_jbc_M111_225383 crossref_primary_10_1007_s00425_008_0730_4 crossref_primary_10_3390_ijms140714950 crossref_primary_10_1007_s11101_006_9007_3 crossref_primary_10_1016_j_foodchem_2024_138454 crossref_primary_10_1111_j_1469_8137_2004_01217_x crossref_primary_10_1177_1934578X1000501211 crossref_primary_10_1016_j_bbrc_2009_06_134 crossref_primary_10_1371_journal_pone_0207278 crossref_primary_10_3390_molecules28073205 crossref_primary_10_1104_pp_105_073262 crossref_primary_10_12677_BR_2014_33012 crossref_primary_10_1002_evl3_212 crossref_primary_10_1111_tpj_12330 crossref_primary_10_1016_j_phytochem_2014_02_009 crossref_primary_10_1111_ppl_12034 crossref_primary_10_1002_cbic_201200572 crossref_primary_10_1071_FP06181 crossref_primary_10_1515_BC_2000_090 crossref_primary_10_1007_s10535_011_0216_2 crossref_primary_10_1007_s11101_006_9052_y crossref_primary_10_1016_S1016_8478_23_17587_X crossref_primary_10_1021_jf200259n crossref_primary_10_3390_ijms232113317 crossref_primary_10_1016_j_pmpp_2004_11_007 crossref_primary_10_1046_j_1365_313x_2000_00922_x crossref_primary_10_1007_s00425_015_2293_5 crossref_primary_10_1186_s12870_016_0850_0 crossref_primary_10_1016_j_foodchem_2014_08_010 crossref_primary_10_1016_S0003_9861_02_00613_6 crossref_primary_10_1016_j_envexpbot_2011_12_006 crossref_primary_10_1016_j_phytochem_2005_09_041 crossref_primary_10_1021_jf205192q crossref_primary_10_1002_pca_2937 crossref_primary_10_1016_j_phytochem_2005_01_008 crossref_primary_10_1016_j_febslet_2006_07_020 crossref_primary_10_1007_s00425_005_0167_y crossref_primary_10_1016_j_plantsci_2011_04_012 crossref_primary_10_1007_s11032_005_2520_z crossref_primary_10_1128_AEM_71_12_8241_8248_2005 crossref_primary_10_1016_j_procbio_2008_02_001 crossref_primary_10_1074_jbc_M411870200 crossref_primary_10_3389_fpls_2019_00010 crossref_primary_10_1007_s00709_010_0160_6 crossref_primary_10_1007_s00425_012_1590_5 crossref_primary_10_1093_pcp_pce169 crossref_primary_10_1007_s11103_006_0012_0 crossref_primary_10_3390_genes14101920 crossref_primary_10_1111_j_1365_313X_2005_02557_x crossref_primary_10_1111_j_1365_313X_2004_02030_x crossref_primary_10_1093_femsyr_foy046 crossref_primary_10_1186_s12864_015_2151_7 crossref_primary_10_1186_s12934_016_0533_4 crossref_primary_10_1007_s00438_011_0652_x crossref_primary_10_1016_j_indcrop_2019_111547 crossref_primary_10_3390_ijms23031265 crossref_primary_10_1016_j_plantsci_2010_04_002 crossref_primary_10_1093_pcp_pcu121 crossref_primary_10_1007_s11515_017_1472_0 |
Cites_doi | 10.1016/S0168-9452(97)00236-7 10.1006/anbo.1996.0052 10.1515/znc-1982-1-205 10.1146/annurev.bi.56.070187.004501 10.1016/0031-9422(93)85102-W 10.1073/pnas.85.9.2989 10.1016/S0981-9428(98)80098-3 10.1007/BF00201341 10.1515/znc-1980-9-1004 10.1104/pp.80.2.483 10.1038/366276a0 10.1016/S0168-9452(97)00175-1 10.1111/j.1438-8677.1997.tb00660.x 10.1074/jbc.271.43.26684 10.1016/S0031-9422(00)86854-5 10.1083/jcb.93.1.97 10.1104/pp.118.1.69 10.1097/00008571-199602000-00002 10.1104/pp.106.2.633 10.1074/jbc.270.14.7922 10.1016/1360-1385(96)10040-6 10.1093/oxfordjournals.pcp.a029004 10.1146/annurev.pp.43.060192.001325 10.1016/0014-5793(95)01141-Z 10.1073/pnas.94.26.14954 10.3109/10520299509108308 10.1016/0378-1119(88)90170-9 10.1073/pnas.88.13.5597 10.1111/j.1438-8677.1996.tb00568.x 10.1007/s004250050192 10.1016/0168-9452(93)90013-P 10.1104/pp.100.2.998 10.1007/BF00958968 10.1007/BF00391415 10.1104/pp.70.3.745 10.1111/j.1432-1033.1983.tb07601.x 10.1006/abio.1994.1031 10.2307/3870058 10.1016/0003-9861(90)90731-D 10.1111/j.1432-1033.1976.tb10719.x 10.1016/0031-9422(82)83146-4 10.1007/978-3-662-02387-7_6 10.1016/S1360-1385(98)01242-4 10.1016/S0031-9422(00)89636-3 10.1007/BF00021810 |
ContentType | Journal Article |
Copyright | 1999 INIST-CNRS |
Copyright_xml | – notice: 1999 INIST-CNRS |
DBID | FBQ IQODW CGR CUY CVF ECM EIF NPM AAYXX CITATION 7TM 8FD FR3 P64 RC3 7X8 |
DOI | 10.1046/j.1365-313X.1999.00524.x |
DatabaseName | AGRIS Pascal-Francis Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed CrossRef Nucleic Acids Abstracts Technology Research Database Engineering Research Database Biotechnology and BioEngineering Abstracts Genetics Abstracts MEDLINE - Academic |
DatabaseTitle | MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) CrossRef Genetics Abstracts Engineering Research Database Technology Research Database Nucleic Acids Abstracts Biotechnology and BioEngineering Abstracts MEDLINE - Academic |
DatabaseTitleList | MEDLINE Genetics Abstracts CrossRef |
Database_xml | – sequence: 1 dbid: NPM name: PubMed url: https://proxy.k.utb.cz/login?url=http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed sourceTypes: Index Database – sequence: 2 dbid: EIF name: MEDLINE url: https://proxy.k.utb.cz/login?url=https://www.webofscience.com/wos/medline/basic-search sourceTypes: Index Database – sequence: 3 dbid: FBQ name: AGRIS url: http://www.fao.org/agris/Centre.asp?Menu_1ID=DB&Menu_2ID=DB1&Language=EN&Content=http://www.fao.org/agris/search?Language=EN sourceTypes: Publisher |
DeliveryMethod | fulltext_linktorsrc |
Discipline | Botany |
EISSN | 1365-313X |
EndPage | 193 |
ExternalDocumentID | 10_1046_j_1365_313X_1999_00524_x 10476065 1905648 TPJ524 US201302932784 |
Genre | article Research Support, Non-U.S. Gov't Journal Article |
GroupedDBID | --- -DZ .3N .GA .Y3 05W 0R~ 10A 123 1OC 24P 29O 2WC 31~ 33P 36B 3SF 4.4 50Y 50Z 51W 51X 52M 52N 52O 52P 52S 52T 52U 52W 52X 53G 5HH 5LA 5VS 66C 702 7PT 8-0 8-1 8-3 8-4 8-5 8UM 930 A03 AAESR AAEVG AAHHS AANLZ AAONW AASGY AAXRX AAZKR ABCQN ABCUV ABEML ABHUG ABJNI ABPTK ABPVW ABWRO ACAHQ ACCFJ ACCZN ACFBH ACGFS ACIWK ACNCT ACPOU ACPRK ACSCC ACXBN ACXME ACXQS ADAWD ADBBV ADDAD ADEOM ADIZJ ADKYN ADMGS ADOZA ADXAS ADZMN AEEZP AEGXH AEIGN AEIMD AENEX AEQDE AEUQT AEUYR AFBPY AFEBI AFFPM AFGKR AFPWT AFRAH AFVGU AFZJQ AGJLS AIURR AIWBW AJBDE AJXKR ALAGY ALMA_UNASSIGNED_HOLDINGS ALUQN AMBMR AMYDB ATUGU AUFTA AZBYB AZVAB BAFTC BAWUL BFHJK BHBCM BMNLL BMXJE BNHUX BROTX BRXPI BY8 C45 CAG COF CS3 D-E D-F DCZOG DIK DPXWK DR2 DRFUL DRSTM DU5 E3Z EBS ECGQY EJD ESX F00 F01 F04 F5P FBQ FIJ G-S G.N GODZA H.T H.X HF~ HZI HZ~ IHE IPNFZ IX1 J0M K48 LATKE LC2 LC3 LEEKS LH4 LITHE LOXES LP6 LP7 LUTES LW6 LYRES MEWTI MK4 MRFUL MRSTM MSFUL MSSTM MXFUL MXSTM N04 N05 N9A NF~ O66 O9- OK1 OVD P2P P2W P2X P4D PQQKQ Q.N Q11 QB0 R.K ROL RX1 SUPJJ TEORI TR2 UB1 W8V W99 WBKPD WH7 WIH WIK WIN WNSPC WOHZO WQJ WRC WXSBR WYISQ XG1 YFH YUY ZZTAW ~IA ~KM ~WT AAHBH AHBTC AITYG HGLYW OIG 08R IQODW CGR CUY CVF ECM EIF NPM AAYXX CITATION 7TM 8FD FR3 P64 RC3 7X8 |
ID | FETCH-LOGICAL-c5644-5fff6785e4d9372316779c364ac9c270ea39d0c58863757bc7c7486477a03113 |
IEDL.DBID | DR2 |
ISSN | 0960-7412 |
IngestDate | Sat Aug 17 02:11:41 EDT 2024 Fri Aug 16 22:35:53 EDT 2024 Fri Aug 23 03:20:23 EDT 2024 Sat Sep 28 08:34:46 EDT 2024 Sun Oct 29 17:07:22 EDT 2023 Sat Aug 24 00:41:14 EDT 2024 Wed Dec 27 19:12:12 EST 2023 |
IsDoiOpenAccess | false |
IsOpenAccess | true |
IsPeerReviewed | true |
IsScholarly | true |
Issue | 2 |
Keywords | Immunohistochemistry Heterologous system Petunia hybrida Enzyme Tissue specificity Homology Catharanthus roseus Gene expression Flavonoid Medicinal plant Apocynaceae Enzymatic activity Complementary DNA Flavonoid 3'-monooxygenase Dicotyledones Substrate specificity Angiospermae Spermatophyta Oxidoreductases Solanaceae Kinetics Localization Secondary metabolism |
Language | English |
License | CC BY 4.0 |
LinkModel | DirectLink |
MergedId | FETCHMERGED-LOGICAL-c5644-5fff6785e4d9372316779c364ac9c270ea39d0c58863757bc7c7486477a03113 |
Notes | Present address: Klinische Forschergruppe Prof. Schmitt, Frauenklinik des Klinikums, Ismaningerstraβe 22, 81675 München, Germany. ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 ObjectType-Article-1 ObjectType-Feature-2 |
OpenAccessLink | https://onlinelibrary.wiley.com/doi/pdfdirect/10.1046/j.1365-313X.1999.00524.x |
PMID | 10476065 |
PQID | 17337552 |
PQPubID | 23462 |
PageCount | 11 |
ParticipantIDs | proquest_miscellaneous_70015078 proquest_miscellaneous_17337552 crossref_primary_10_1046_j_1365_313X_1999_00524_x pubmed_primary_10476065 pascalfrancis_primary_1905648 wiley_primary_10_1046_j_1365_313X_1999_00524_x_TPJ524 fao_agris_US201302932784 |
PublicationCentury | 1900 |
PublicationDate | July 1999 |
PublicationDateYYYYMMDD | 1999-07-01 |
PublicationDate_xml | – month: 07 year: 1999 text: July 1999 |
PublicationDecade | 1990 |
PublicationPlace | Oxford, UK |
PublicationPlace_xml | – name: Oxford, UK – name: Oxford – name: England |
PublicationTitle | The Plant journal : for cell and molecular biology |
PublicationTitleAlternate | Plant J |
PublicationYear | 1999 |
Publisher | Blackwell Science Ltd Blackwell Science |
Publisher_xml | – name: Blackwell Science Ltd – name: Blackwell Science |
References | 1982; 37c 1996; 109 1993; 23 1994; 216 1995; 70 1976; 67 1982; 93 1995; 36 1997; 110 1998; 118 1988; 74 1995; 374 1993; 366 1996; 37 1996; 77 1986; 80 1997; 94 1994; 106 1990 1991; 88 1993; 33 1982; 21 1994; 36 1984 1985; 95 1996; 1 1988; 85 1988; 173 1992; 43 1989 1996; 6 1987; 56 1983; 134 1982; 70 1992; 100 1995; 19 1995; 270 1993; 189 1998; 131 1999 1995; 7 1997; 203 1997; 129 1993; 94 1986; 167 1980; 35c 1996; 271 1998; 3 1990; 276 1976; 15 1998; 36 e_1_2_7_5_1 e_1_2_7_3_1 e_1_2_7_9_1 e_1_2_7_7_1 e_1_2_7_19_1 Milo J. (e_1_2_7_31_1) 1985; 95 e_1_2_7_17_1 e_1_2_7_15_1 Schenk P.M. (e_1_2_7_39_1) 1995; 19 e_1_2_7_41_1 e_1_2_7_13_1 e_1_2_7_43_1 e_1_2_7_11_1 e_1_2_7_47_1 e_1_2_7_26_1 e_1_2_7_49_1 e_1_2_7_28_1 Sambrook J. (e_1_2_7_38_1) 1989 e_1_2_7_50_1 e_1_2_7_25_1 e_1_2_7_52_1 Forkmann G. (e_1_2_7_12_1) 1999 e_1_2_7_23_1 e_1_2_7_33_1 e_1_2_7_21_1 e_1_2_7_35_1 e_1_2_7_37_1 e_1_2_7_4_1 e_1_2_7_8_1 e_1_2_7_18_1 e_1_2_7_16_1 e_1_2_7_40_1 e_1_2_7_2_1 Burton W.C. (e_1_2_7_6_1) 1989 e_1_2_7_14_1 e_1_2_7_42_1 e_1_2_7_44_1 e_1_2_7_46_1 e_1_2_7_48_1 e_1_2_7_27_1 e_1_2_7_29_1 Doostdar H. (e_1_2_7_10_1) 1995; 36 Stafford H.A. (e_1_2_7_45_1) 1990 e_1_2_7_51_1 e_1_2_7_53_1 e_1_2_7_24_1 e_1_2_7_32_1 e_1_2_7_22_1 Menting J.G.T. (e_1_2_7_30_1) 1994; 106 e_1_2_7_34_1 e_1_2_7_20_1 e_1_2_7_36_1 |
References_xml | – volume: 106 start-page: 633 year: 1994 end-page: 642 article-title: Characterization of flavonoid 3′5′‐hydroxylase in microsomal membrane fraction of flowers. publication-title: Plant Physiol. – volume: 1 start-page: 377 year: 1996 end-page: 382 article-title: Flavonoid biosynthesis: ‘new’ functions for an ‘old’ pathway. publication-title: Trends Plant Sci. – volume: 36 start-page: 69 year: 1995 end-page: 77 article-title: A cytochrome P450 mediated naringenin 3′‐hydroxylase from sweet orange cell cultures. publication-title: Plant Cell Physiol. – volume: 36 start-page: 135 year: 1998 end-page: 144 article-title: Flavonoid and flavonol glycoside metabolism in . publication-title: Plant Physiol. Biochem. – volume: 276 start-page: 348 year: 1990 end-page: 354 article-title: Purification of flavanone 3β‐hydroxylase from . Antibody preparation and characterization of a chemogenetically defined mutant. publication-title: Arch. Biochem. Biophys. – volume: 270 start-page: 7922 year: 1995 end-page: 7928 article-title: Reaction mechanisms of homodimeric plant polyketide synthases (stilbene and chalcone synthase): a single active site for the condensing reaction is sufficient for synthesis of stilbenes, chalcones, and 6′‐deoxychalcones. publication-title: J. Biol. Chem. – volume: 167 start-page: 196 year: 1986 end-page: 205 article-title: Tissue‐distribution of secondary phenolic biosynthesis in developing primary leaves of L. publication-title: Planta – volume: 94 start-page: 14954 year: 1997 end-page: 14959 article-title: Differentially regulated NADPH: cytochrome P450 oxidoreductases in parsley. publication-title: Proc. Natl Acad. Sci. USA – volume: 43 start-page: 241 year: 1992 end-page: 267 article-title: Spatial organization of enzymes in plant metabolic pathways. publication-title: Annu. Rev. Plant Physiol. Plant Mol. Biol. – year: 1989 – start-page: 713 year: 1999 end-page: 748 – volume: 37 start-page: 711 year: 1996 end-page: 716 article-title: Molecular and biochemical characterization of three anthocyanin synthetic genes from . publication-title: Plant Cell Physiol. – year: 1990 – volume: 74 start-page: 365 year: 1988 end-page: 373 article-title: A vector to express and purify foreign proteins in by fusion to, and separation from, maltose binding protein. publication-title: Gene – volume: 23 start-page: 933 year: 1993 end-page: 946 article-title: Activation of anthocyanin synthesis genes by white light in eggplant hypocotyl tissues, and identification of an inducible P‐450 cDNA. publication-title: Plant Mol. Biol. – volume: 88 start-page: 5597 year: 1991 end-page: 5601 article-title: Expression and enzymatic activity of recombinant cytochrome P450, 17–24–hydroxylase in . publication-title: Proc. Natl Acad. Sci. USA – volume: 173 start-page: 544 year: 1988 end-page: 553 article-title: Chalcone synthases from spinach ( L.). II. Immunofluorescence and immunogold localization. publication-title: Planta – volume: 189 start-page: 39 year: 1993 end-page: 46 article-title: Chalcone synthase and flavonoid products in primary leaf tissues of rye and maize. publication-title: Planta – volume: 129 start-page: 167 year: 1997 end-page: 174 article-title: cDNA cloning and endogenous expression of a flavonoid 3′5′‐hydroxylase from petals of Lisianthus ( ). publication-title: Plant Sci. – volume: 70 start-page: 1 year: 1995 end-page: 6 article-title: Chalcone synthase localization in early stages of plant development. I. Immunohistochemical use of plasmolysis for localizing the enzyme in epidermal cell cytoplasm of illuminated buckwheat hypocotyls. publication-title: Biotechnol. Histochem. – volume: 110 start-page: 431 year: 1997 end-page: 443 article-title: localization of phenylpropanoid biosynthetic mRNAs and proteins in parsley ( ). publication-title: Bot. Acta – volume: 33 start-page: 1419 year: 1993 end-page: 1426 article-title: Flavonoid biosynthesis in petals of . publication-title: Phytochemistry – volume: 366 start-page: 276 year: 1993 end-page: 279 article-title: Cloning and expression of cytochrome P450 genes controlling flower colour. publication-title: Nature – volume: 70 start-page: 745 year: 1982 end-page: 748 article-title: Distribution of secondary plant metabolites and their biosynthetic enzymes in pea ( ) leaves. publication-title: Plant Physiol. – volume: 35c start-page: 691 year: 1980 end-page: 695 article-title: Anthocyanin biosynthesis in flowers of : flavanone 3‐ and flavonoid 3′‐hydroxylases. publication-title: Z. Naturforsch. – volume: 374 start-page: 345 year: 1995 end-page: 350 article-title: Cinnamate 4‐hydroxylase from , and a strategy for the functional expression of plant cytochrome P proteins as translational fusions with P reductase in . publication-title: FEBS Lett. – volume: 37c start-page: 19 year: 1982 end-page: 23 article-title: Hydroxylation of the B‐ring of flavonoids in the 3′‐ and 5′‐position with enzyme extracts from flowers of . publication-title: Z. Naturforsch. – volume: 95 start-page: 352 year: 1985 end-page: 360 article-title: Inheritance of corolla color and anthocyanin pigments in periwinkle ( ). publication-title: Z. Pflanzenzücht. – start-page: 49 year: 1984 end-page: 76 – volume: 80 start-page: 483 year: 1986 end-page: 486 article-title: Microsomal flavonoid 3′‐monooxygenase from maize seedlings. publication-title: Plant Physiol. – volume: 85 start-page: 2989 year: 1988 end-page: 2993 article-title: localization of light‐induced chalcone synthase messenger RNA, chalcone synthase, and flavonoid end products in epidermal cells of parsley leaves. publication-title: Proc. Natl Acad. Sci. USA – volume: 77 start-page: 429 year: 1996 end-page: 432 article-title: Tissue‐specific distribution of glutamine synthetase in potato tubers. publication-title: Ann. Bot. – volume: 3 start-page: 212 year: 1998 end-page: 217 article-title: How genes paint flowers and seeds. publication-title: Trends Plant Sci. – volume: 6 start-page: 1 year: 1996 end-page: 42 article-title: P450 superfamily: Update on new sequences, gene mapping, accession numbers and nomenclature. publication-title: Pharmacogenetics – volume: 15 start-page: 442 year: 1976 article-title: Anthocyanidins of callus cultures. publication-title: Phytochemistry – volume: 19 start-page: 196 year: 1995 end-page: 200 article-title: Improved high‐level expression system for eucaryotic genes in using T7 RNA polymerase and rare tRNAs. publication-title: Biotechniques – volume: 94 start-page: 119 year: 1993 end-page: 126 article-title: The cloning and characterization of a cDNA encoding a cytochrome P450 from the flowers of . publication-title: Plant Sci. – volume: 131 start-page: 173 year: 1998 end-page: 180 article-title: Flower‐specific gene expression directed by the promoter of a chalcone synthase gene from in . publication-title: Plant Sci. – volume: 203 start-page: 275 year: 1997 end-page: 282 article-title: Chalcone synthase activity and polyphenolic compounds of shoot tissues from adult and rejuvenated walnut trees. publication-title: Planta – volume: 109 start-page: 229 year: 1996 end-page: 238 article-title: Expression of chalcone synthase genes in coleoptiles and primary leaves of L. after induction by UV irradiation: evidence for UV‐protective role of the coleoptile. publication-title: Bot. Acta – volume: 216 start-page: 232 year: 1994 end-page: 233 article-title: A rapid protein determination by modification of the Lowry procedure. publication-title: Anal. Biochem. – volume: 7 start-page: 1071 year: 1995 end-page: 1083 article-title: Genetics and biochemistry of anthocyanin biosynthesis. publication-title: Plant Cell – volume: 100 start-page: 998 year: 1992 end-page: 1007 article-title: Molecular analysis and heterologous expression of an inducible cytochrome P‐450 protein from periwinkle ( L.). publication-title: Plant Physiol. – volume: 36 start-page: 1189 year: 1994 end-page: 1196 article-title: Pigmentation patterns of modern rose mutants throw light on the flavonoid pathway in. publication-title: Rosa X Hybrida. Phytochemistry – volume: 67 start-page: 527 year: 1976 end-page: 541 article-title: Light‐induced enzyme synthesis in cell suspension cultures of . Demonstration in a heterologous cell‐free system of rapid changes in the rate of phenylalanine ammonia‐lyase synthesis. publication-title: Eur. J. Biochem. – volume: 56 start-page: 945 year: 1987 end-page: 993 article-title: P‐450 genes. Structure, evolution and regulation. publication-title: Annu. Rev. Biochem. – volume: 21 start-page: 591 year: 1982 end-page: 594 article-title: Medium‐ and light‐induced formation of serpentine and anthocyanins in cell suspension cultures of . publication-title: Phytochemistry – volume: 93 start-page: 97 year: 1982 end-page: 102 article-title: Isolation of intracellular membranes by means of sodium carbonate treatment: application to endoplasmic reticulum. publication-title: J. Cell. Biol. – volume: 271 start-page: 26684 year: 1996 end-page: 26689 article-title: Novel type of receptor‐like protein kinase from a higher plant ( ). cDNA, gene, intramolecular autophosphorylation, and identification of a threonine important for auto‐ and substrate phosphorylation. publication-title: J. Biol. Chem. – volume: 118 start-page: 69 year: 1998 end-page: 81 article-title: Expression patterns conferred by tyrosine/dihydroxyphenylalanine decarboxylase promoters from opium poppy are conserved in transgenic tobacco. publication-title: Plant Physiol. – volume: 134 start-page: 547 year: 1983 end-page: 554 article-title: Induction and characterization of a microsomal flavonoid 3′‐hydroxylase from parsley cell cultures. publication-title: Eur. J. Biochem. – volume-title: The Potato year: 1989 ident: e_1_2_7_6_1 contributor: fullname: Burton W.C. – ident: e_1_2_7_26_1 doi: 10.1016/S0168-9452(97)00236-7 – ident: e_1_2_7_36_1 doi: 10.1006/anbo.1996.0052 – ident: e_1_2_7_46_1 doi: 10.1515/znc-1982-1-205 – ident: e_1_2_7_33_1 doi: 10.1146/annurev.bi.56.070187.004501 – ident: e_1_2_7_9_1 doi: 10.1016/0031-9422(93)85102-W – ident: e_1_2_7_40_1 doi: 10.1073/pnas.85.9.2989 – ident: e_1_2_7_15_1 doi: 10.1016/S0981-9428(98)80098-3 – ident: e_1_2_7_23_1 doi: 10.1007/BF00201341 – ident: e_1_2_7_13_1 doi: 10.1515/znc-1980-9-1004 – ident: e_1_2_7_28_1 doi: 10.1104/pp.80.2.483 – ident: e_1_2_7_18_1 doi: 10.1038/366276a0 – ident: e_1_2_7_35_1 doi: 10.1016/S0168-9452(97)00175-1 – start-page: 713 volume-title: Polyketides and Other Secondary Metabolites Including Fatty Acids and Their Derivatives year: 1999 ident: e_1_2_7_12_1 contributor: fullname: Forkmann G. – ident: e_1_2_7_37_1 doi: 10.1111/j.1438-8677.1997.tb00660.x – ident: e_1_2_7_42_1 doi: 10.1074/jbc.271.43.26684 – ident: e_1_2_7_7_1 doi: 10.1016/S0031-9422(00)86854-5 – volume: 36 start-page: 69 year: 1995 ident: e_1_2_7_10_1 article-title: A cytochrome P450 mediated naringenin 3′‐hydroxylase from sweet orange cell cultures. publication-title: Plant Cell Physiol. contributor: fullname: Doostdar H. – ident: e_1_2_7_14_1 doi: 10.1083/jcb.93.1.97 – ident: e_1_2_7_11_1 doi: 10.1104/pp.118.1.69 – ident: e_1_2_7_34_1 doi: 10.1097/00008571-199602000-00002 – volume: 106 start-page: 633 year: 1994 ident: e_1_2_7_30_1 article-title: Characterization of flavonoid 3′5′‐hydroxylase in microsomal membrane fraction of Petunia hybrida flowers. publication-title: Plant Physiol. doi: 10.1104/pp.106.2.633 contributor: fullname: Menting J.G.T. – ident: e_1_2_7_50_1 doi: 10.1074/jbc.270.14.7922 – ident: e_1_2_7_44_1 doi: 10.1016/1360-1385(96)10040-6 – ident: e_1_2_7_47_1 doi: 10.1093/oxfordjournals.pcp.a029004 – ident: e_1_2_7_21_1 doi: 10.1146/annurev.pp.43.060192.001325 – ident: e_1_2_7_20_1 doi: 10.1016/0014-5793(95)01141-Z – ident: e_1_2_7_27_1 doi: 10.1073/pnas.94.26.14954 – ident: e_1_2_7_53_1 doi: 10.3109/10520299509108308 – volume-title: Flavonoid Metabolism year: 1990 ident: e_1_2_7_45_1 contributor: fullname: Stafford H.A. – ident: e_1_2_7_29_1 doi: 10.1016/0378-1119(88)90170-9 – volume: 19 start-page: 196 year: 1995 ident: e_1_2_7_39_1 article-title: Improved high‐level expression system for eucaryotic genes in Escherichia coli using T7 RNA polymerase and rare ArgtRNAs. publication-title: Biotechniques contributor: fullname: Schenk P.M. – ident: e_1_2_7_2_1 doi: 10.1073/pnas.88.13.5597 – ident: e_1_2_7_17_1 doi: 10.1111/j.1438-8677.1996.tb00568.x – ident: e_1_2_7_8_1 doi: 10.1007/s004250050192 – volume-title: Molecular Cloning: a Laboratory Manual year: 1989 ident: e_1_2_7_38_1 contributor: fullname: Sambrook J. – ident: e_1_2_7_48_1 doi: 10.1016/0168-9452(93)90013-P – ident: e_1_2_7_51_1 doi: 10.1104/pp.100.2.998 – ident: e_1_2_7_3_1 doi: 10.1007/BF00958968 – ident: e_1_2_7_25_1 doi: 10.1007/BF00391415 – ident: e_1_2_7_22_1 doi: 10.1104/pp.70.3.745 – ident: e_1_2_7_16_1 doi: 10.1111/j.1432-1033.1983.tb07601.x – ident: e_1_2_7_43_1 doi: 10.1006/abio.1994.1031 – ident: e_1_2_7_19_1 doi: 10.2307/3870058 – ident: e_1_2_7_5_1 doi: 10.1016/0003-9861(90)90731-D – ident: e_1_2_7_41_1 doi: 10.1111/j.1432-1033.1976.tb10719.x – ident: e_1_2_7_24_1 doi: 10.1016/0031-9422(82)83146-4 – ident: e_1_2_7_52_1 doi: 10.1007/978-3-662-02387-7_6 – ident: e_1_2_7_32_1 doi: 10.1016/S1360-1385(98)01242-4 – ident: e_1_2_7_4_1 doi: 10.1016/S0031-9422(00)89636-3 – ident: e_1_2_7_49_1 doi: 10.1007/BF00021810 – volume: 95 start-page: 352 year: 1985 ident: e_1_2_7_31_1 article-title: Inheritance of corolla color and anthocyanin pigments in periwinkle (Catharanthus roseus). publication-title: Z. Pflanzenzücht. contributor: fullname: Milo J. |
SSID | ssj0017364 |
Score | 1.9663293 |
Snippet | We investigated the P450 dependent flavonoid hydroxylase from the ornamental plant Catharanthus roseus. cDNAs were obtained by heterologous screening with the... Summary We investigated the P450 dependent flavonoid hydroxylase from the ornamental plant Catharanthus roseus. cDNAs were obtained by heterologous screening... Summary We investigated the P450 dependent flavonoid hydroxylase from the ornamental plant Catharanthus roseus . cDNAs were obtained by heterologous screening... |
SourceID | proquest crossref pubmed pascalfrancis wiley fao |
SourceType | Aggregation Database Index Database Publisher |
StartPage | 183 |
SubjectTerms | Acyltransferases - genetics Acyltransferases - metabolism Amino Acid Sequence amino acid sequences Base Sequence Biological and medical sciences Blotting, Southern Catharanthus roseus Cells, Cultured chemical constituents of plants complementary DNA cytochrome P-450 Cytochrome P-450 Enzyme System - genetics Cytochrome P-450 Enzyme System - metabolism dark DNA, Complementary - chemistry DNA, Complementary - genetics enzyme activity Escherichia coli Escherichia coli - genetics Fundamental and applied biological sciences. Psychology genbank/aj011862 genbank/aj131813 gene expression Gene Expression Regulation, Enzymologic Gene Expression Regulation, Plant histochemistry Immunohistochemistry lighting Metabolism Metabolism. Physicochemical requirements Mixed Function Oxygenases - genetics Mixed Function Oxygenases - metabolism Molecular Sequence Data nucleotide sequences oxidoreductases oxygenases Petunia hybrida Plant Cells Plant physiology and development Plants - enzymology Plants - genetics recombinant proteins Sequence Analysis, DNA Sequence Homology, Amino Acid Substrate Specificity substrates Tissue Distribution |
Title | Flavonoid hydroxylase from Catharanthus roseus: cDNA, heterologous expression, enzyme properties and cell-type specific expression in plants |
URI | https://onlinelibrary.wiley.com/doi/abs/10.1046%2Fj.1365-313X.1999.00524.x https://www.ncbi.nlm.nih.gov/pubmed/10476065 https://search.proquest.com/docview/17337552 https://search.proquest.com/docview/70015078 |
Volume | 19 |
hasFullText | 1 |
inHoldings | 1 |
isFullTextHit | |
isPrint | |
link | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwrV3Pb9MwFLZg4sAFGL9WtoEPHJcqie3Y2W3AqmkSE4JO6s1yHJtOG061tmjdib8A8Tfyl-w9Jx0rGhJC3CI1cfOen-0vft_7TMjrnFW1LyB4lfNpwllqE5PlReJTaZjPS2c8bui_PyoOjvnhSIw6_hPWwrT6ENcbbjgy4nyNA9xU7SkkaVS37RhaLGMjLLlD2UmR8z7iSdTVQ3z08VpJKpOsVZICwJ7AIrok9XQJzlsbWlmp7nrTIG_STMF1vj3z4jZQuopx4yI1eEhOl-a13JTT_nxW9e3lb8qP_8f-R-RBh2XpXht86-SOC4_JvTcN4M3FE_J9cGa-NqE5qel4UeMbAVB3FOtZKNYdGjBvNp5PKVjv5tNdat8d7e3QMfJzcEZu4Cd30fF0ww514XLxxdEJZg_OUQaWmlBTTDz8_PYDd5IpVo0i8-nGY_Qk0MkZcn2ekuFgf_j2IOlOf0isAJCWCO89rKTC8RogVI4V-7K00I3GljaXqTOsrFMrlCqYFLKy0kqusK7WwESVsWdkLTTBbUBHF8pnKfNKecOZrRV3hS-M8VzC12eleiRbdrSetBofOubmOdaxoZc1elmjl3X0sr7okQ2ICG0-w1Ssjz_lMQEMWFgq3iPbK2Hyq80S0CaHv3u1DBsNYxn9ZIIDp2qIUjBF5H--Q0ZJSAltPG_j7cYLcwkfo6JHRIyav7ZEDz8cwsWLf3xuk9xvlSyQwbxF1mbnc7cNOG1WvYwj8Aq4qjDZ |
link.rule.ids | 315,786,790,1382,27957,27958,46329,46753 |
linkProvider | Wiley-Blackwell |
linkToHtml | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwrV1fb9MwELdgIMEL_2EFxvzA41KS2I4d3safqoytQtBJfbMcx6YTxanWFq174hMgPiOfhLskHSsaEkK8RUri5M539s--350JeZqyovQZGK9yPo44i21kkjSLfCwN82nujMcN_YNB1j_keyMxao8DwlyYpj7E2YYbekY9XqOD44b0szYs2Xg5UrRYwkaYc4d1J0XKuwAor4D3i3p99f6sllQiWVNLCiB7BNPoitbThjgvbGltrrrsTYXMSTMD5fnm1IuLYOk6yq2nqd5NMlkJ2LBTPnUX86JrT3-r_fifNHCL3GjhLN1t7O82ueTCHXL1RQWQc3mXfOtNzJcqVEclHS9L_CXA6o5iSgvF1EMD8s3HixkF8d1i9pzaV4PdHTpGig4OyhXccictVTfsUBdOl58dnWIA4RgrwVITSoqxhx9fv-NmMsXEUSQ_nXuNHgU6nSDd5x4Z9l4PX_aj9gCIyArAaZHw3sNkKhwvAUWlmLQvcwv9aGxuUxk7w_IytkKpjEkhCyut5ApTaw2MVQm7TzZCFdwm9HSmfBIzr5Q3nNlScZf5zBjPJSxAC9Uhyaqn9bQp86Hr8DzHVDbUskYta9SyrrWsTzpkE0xCm48wGuvDD2kdAwY4LBXvkK01O_nVZg6Ak8Pntld2o8GdUU8mOFCqBjMFUUT65ydkXRVSQhsPGoM798NcwnpUdIiozeavJdHDd3tw8fAf39sm1_rDg329_2bw9hG53hS2QELzY7IxP164LYBt8-JJ7Y4_Ac6XNPs |
linkToPdf | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwrV1Nb9NAEF1BQYgL36UBSvfAsQ72fnjX3AohKgWiClIpt9V6vUuqFjtqEtT0xC9A_EZ-CTO2UxpUJIS4RUq88cy-2X3eeTMm5BnjeRFSAK_2IY4Ej11kE5ZGIVaWB5Z5G_BA__0g3T0QeyM5avVPWAvT9Ic4P3DDyKjXawzwSRGet1nJJshRocUTPsKSO2w7KZnoAp-8JlLOEOG9D-etpBLFm1ZSwNgj2EWXqp42w3npSCtb1dVgKxRO2in4LjQvvbiMla6S3HqX6t8mR0v7GnHKUXc-y7vu7LfWj__HAXfIrZbM0p0GfXfJFV_eI9dfVkA4F_fJt_6x_VKV1WFBx4sC7wiYuqdY0EKx8NCCebPxfErBej-fvqCuN9jZpmMU6OCSXMFX_rQV6pbb1Jdni8-eTjB9cIJ9YKktC4qZhx9fv-NRMsWyUZQ-XbiMHpZ0coxinwdk2H89fLUbta9_iJwElhbJEAJspdKLAjgUw5J9lTmYRusyx1TsLc-K2EmtU66kyp1ySmgsrLWwUiV8nayVVek3YKJTHZKYB62DFdwVWvg0pNYGoeDxM9cdkiwn2kyaJh-mTs4LLGRDLxv0skEvm9rL5rRDNgARxn6CtdgcfGR1BhjIsNKiQzZXYPJrzAzopoC_21rCxkAwo59s6cGpBlAKpkj251-ouiekgjEeNni7cMNCwdOo7BBZo-avLTHD_T348Ogfr9siN_Z7ffPuzeDtY3Kz6WqBauYnZG12MvebwNlm-dM6GH8C_BYzqg |
openUrl | ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Flavonoid+hydroxylase+from+Catharanthus+roseus%3A+cDNA%2C+heterologous+expression%2C+enzyme+properties+and+cell-type+specific+expression+in+plants&rft.jtitle=The+Plant+journal+%3A+for+cell+and+molecular+biology&rft.au=Kaltenbach%2C+M&rft.au=Schr%C3%B6der%2C+G&rft.au=Schmelzer%2C+E&rft.au=Lutz%2C+V&rft.date=1999-07-01&rft.issn=0960-7412&rft.volume=19&rft.issue=2&rft.spage=183&rft_id=info:doi/10.1046%2Fj.1365-313X.1999.00524.x&rft_id=info%3Apmid%2F10476065&rft.externalDocID=10476065 |
thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0960-7412&client=summon |
thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0960-7412&client=summon |
thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0960-7412&client=summon |