Disaccharides permeases: constituents of xylanolytic and mannanolytic systems of Aureobasidium pullulans

Aureobasidium pullulans, a yeast-like microorganism was found to produce mannobiose permease and xylobiose permease, transporting β-1,4-mannobiose or β-1,4-xylobiose into the cells from extracellular media. Both permeases are induced by the same inducers as the corresponding hemicellulolytic enzyme...

Full description

Saved in:
Bibliographic Details
Published inBiochimica et biophysica acta Vol. 1425; no. 3; pp. 560 - 566
Main Authors Lubomı́r, Kremnický, Peter, Biely
Format Journal Article
LanguageEnglish
Published Netherlands Elsevier B.V 27.11.1998
Subjects
Online AccessGet full text
ISSN0304-4165
0006-3002
1872-8006
DOI10.1016/S0304-4165(98)00112-3

Cover

Loading…
Abstract Aureobasidium pullulans, a yeast-like microorganism was found to produce mannobiose permease and xylobiose permease, transporting β-1,4-mannobiose or β-1,4-xylobiose into the cells from extracellular media. Both permeases are induced by the same inducers as the corresponding hemicellulolytic enzyme systems. Mannobiose permease is induced by β-1,4-mannobiose or is formed in the cells growing on mannan (inducers of β-mannanolytic enzymes) and xylobiose permease is induced by d-xylose, β-1,4-xylobiose or during the growth on xylan (inducers of xylanolytic enzymes). The permeases are energy dependent, synthesized de novo and their activities are inhibited by d-glucose. Since mannobiose permease transports β-1,4-mannobiose, xylobiose permease appears to be less specific and transports β-1,4-mannobiose, β-1,4-xylobiose and methyl β- d-xylopyranoside. Methyl β- d-mannopyranoside or methyl β- d-xylopyranoside serve as less efficient inducers of the corresponding permeases than β-1,4-mannobiose or β-1,4-xylobiose.
AbstractList Aureobasidium pullulans, a yeast-like microorganism was found to produce mannobiose permease and xylobiose permease, transporting β-1,4-mannobiose or β-1,4-xylobiose into the cells from extracellular media. Both permeases are induced by the same inducers as the corresponding hemicellulolytic enzyme systems. Mannobiose permease is induced by β-1,4-mannobiose or is formed in the cells growing on mannan (inducers of β-mannanolytic enzymes) and xylobiose permease is induced by d-xylose, β-1,4-xylobiose or during the growth on xylan (inducers of xylanolytic enzymes). The permeases are energy dependent, synthesized de novo and their activities are inhibited by d-glucose. Since mannobiose permease transports β-1,4-mannobiose, xylobiose permease appears to be less specific and transports β-1,4-mannobiose, β-1,4-xylobiose and methyl β- d-xylopyranoside. Methyl β- d-mannopyranoside or methyl β- d-xylopyranoside serve as less efficient inducers of the corresponding permeases than β-1,4-mannobiose or β-1,4-xylobiose.
Aureobasidium pullulans, a yeast-like microorganism was found to produce mannobiose permease and xylobiose permease, transporting beta-1,4-mannobiose or beta-1,4-xylobiose into the cells from extracellular media. Both permeases are induced by the same inducers as the corresponding hemicellulolytic enzyme systems. Mannobiose permease is induced by beta-1,4-mannobiose or is formed in the cells growing on mannan (inducers of beta-mannanolytic enzymes) and xylobiose permease is induced by d-xylose, beta-1,4-xylobiose or during the growth on xylan (inducers of xylanolytic enzymes). The permeases are energy dependent, synthesized de novo and their activities are inhibited by d-glucose. Since mannobiose permease transports beta-1,4-mannobiose, xylobiose permease appears to be less specific and transports beta-1,4-mannobiose, beta-1,4-xylobiose and methyl beta-d-xylopyranoside. Methyl beta-d-mannopyranoside or methyl beta-d-xylopyranoside serve as less efficient inducers of the corresponding permeases than beta-1,4-mannobiose or beta-1, 4-xylobiose.Aureobasidium pullulans, a yeast-like microorganism was found to produce mannobiose permease and xylobiose permease, transporting beta-1,4-mannobiose or beta-1,4-xylobiose into the cells from extracellular media. Both permeases are induced by the same inducers as the corresponding hemicellulolytic enzyme systems. Mannobiose permease is induced by beta-1,4-mannobiose or is formed in the cells growing on mannan (inducers of beta-mannanolytic enzymes) and xylobiose permease is induced by d-xylose, beta-1,4-xylobiose or during the growth on xylan (inducers of xylanolytic enzymes). The permeases are energy dependent, synthesized de novo and their activities are inhibited by d-glucose. Since mannobiose permease transports beta-1,4-mannobiose, xylobiose permease appears to be less specific and transports beta-1,4-mannobiose, beta-1,4-xylobiose and methyl beta-d-xylopyranoside. Methyl beta-d-mannopyranoside or methyl beta-d-xylopyranoside serve as less efficient inducers of the corresponding permeases than beta-1,4-mannobiose or beta-1, 4-xylobiose.
Aureobasidium pullulans, a yeast-like microorganism was found to produce mannobiose permease and xylobiose permease, transporting beta-1,4-mannobiose or beta-1,4-xylobiose into the cells from extracellular media. Both permeases are induced by the same inducers as the corresponding hemicellulolytic enzyme systems. Mannobiose permease is induced by beta-1,4-mannobiose or is formed in the cells growing on mannan (inducers of beta-mannanolytic enzymes) and xylobiose permease is induced by d-xylose, beta-1,4-xylobiose or during the growth on xylan (inducers of xylanolytic enzymes). The permeases are energy dependent, synthesized de novo and their activities are inhibited by d-glucose. Since mannobiose permease transports beta-1,4-mannobiose, xylobiose permease appears to be less specific and transports beta-1,4-mannobiose, beta-1,4-xylobiose and methyl beta-d-xylopyranoside. Methyl beta-d-mannopyranoside or methyl beta-d-xylopyranoside serve as less efficient inducers of the corresponding permeases than beta-1,4-mannobiose or beta-1, 4-xylobiose.
Author Peter, Biely
Lubomı́r, Kremnický
Author_xml – sequence: 1
  givenname: Kremnický
  surname: Lubomı́r
  fullname: Lubomı́r, Kremnický
  email: chemkrem@savba.sk
– sequence: 2
  givenname: Biely
  surname: Peter
  fullname: Peter, Biely
BackLink https://www.ncbi.nlm.nih.gov/pubmed/9838219$$D View this record in MEDLINE/PubMed
BookMark eNqFkUFP3DAUhC1EBQvtT0DKCbWHtHYcO057QIhCWwmph7Zny7FfhFFiL34O6v77mt2FQy_4Yskz38iaOSGHIQYg5IzRj4wy-ekX5bStWybF-159oJSxpuYHZMVU19SKUnlIVi-WY3KCeE_LEb04Ike94qph_YrcffVorL0zyTvAag1pBoOAnysbA2afFwgZqzhWfzeTCXHaZG8rE1w1mxBeHnCDGeat73JJEAeD3vllrtbLNC0FxLfkzWgmhHf7-5T8ubn-ffW9vv357cfV5W1tuaS5bmknmJI9s9wK7hTt-qExwjVta-UolFFgizzKse-MlE72MDo-SNpwPowd8FNyvstdp_iwAGY9e7QwlT9AXFB3pSgquCzGs71xGWZwep38bNJG76sp-pedblNETDBq67PJPoacjJ80o_ppB73dQT-VXFC93UHzQov_6Of817iLHQelo0cPSaP1ECw4n8Bm7aJ_JeEfNP-hig
CitedBy_id crossref_primary_10_1007_s12355_014_0357_7
crossref_primary_10_1007_s13205_019_1586_y
crossref_primary_10_1016_j_biortech_2010_01_088
crossref_primary_10_1016_j_biotechadv_2022_107981
crossref_primary_10_1016_j_jbiotec_2008_07_1789
crossref_primary_10_3109_07388551_2015_1128878
crossref_primary_10_1128_AEM_69_10_5957_5967_2003
crossref_primary_10_1128_AEM_69_4_1944_1952_2003
crossref_primary_10_1590_S1516_89132002000600005
Cites_doi 10.1016/S0021-9258(19)36523-8
10.1016/0922-338X(91)90325-B
10.1128/jb.178.8.2245-2254.1996
10.1016/0141-0229(93)90068-D
10.1007/BF02816339
10.1007/s002030050454
10.1002/jlcr.2590100407
10.1007/BF01078647
10.1002/bit.260380810
10.1021/ac60111a017
10.1111/j.1432-1033.1992.tb17313.x
10.1016/S0065-2911(08)60227-1
10.1021/ac60155a072
10.1515/hfsg.1967.21.3.74
10.1016/0304-4165(69)90032-4
10.1128/jb.173.5.1817-1820.1991
ContentType Journal Article
Copyright 1998 Elsevier Science B.V.
Copyright_xml – notice: 1998 Elsevier Science B.V.
DBID AAYXX
CITATION
CGR
CUY
CVF
ECM
EIF
NPM
7X8
DOI 10.1016/S0304-4165(98)00112-3
DatabaseName CrossRef
Medline
MEDLINE
MEDLINE (Ovid)
MEDLINE
MEDLINE
PubMed
MEDLINE - Academic
DatabaseTitle CrossRef
MEDLINE
Medline Complete
MEDLINE with Full Text
PubMed
MEDLINE (Ovid)
MEDLINE - Academic
DatabaseTitleList
MEDLINE - Academic
MEDLINE
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
DeliveryMethod fulltext_linktorsrc
Discipline Chemistry
Biology
EISSN 1872-8006
EndPage 566
ExternalDocumentID 9838219
10_1016_S0304_4165_98_00112_3
S0304416598001123
Genre Research Support, Non-U.S. Gov't
Journal Article
GroupedDBID ---
--K
--M
.~1
0R~
1B1
1RT
1~.
1~5
23N
3O-
4.4
457
4G.
53G
5GY
5RE
5VS
7-5
71M
8P~
9JM
AACTN
AAEDT
AAEDW
AAIAV
AAIKJ
AAKOC
AALRI
AAOAW
AAQFI
AAQXK
AAXUO
ABEFU
ABFNM
ABGSF
ABMAC
ABUDA
ABXDB
ABYKQ
ACDAQ
ACIUM
ACRLP
ADBBV
ADEZE
ADMUD
ADUVX
AEBSH
AEHWI
AEKER
AFKWA
AFTJW
AFXIZ
AGHFR
AGRDE
AGUBO
AGYEJ
AHHHB
AIEXJ
AIKHN
AITUG
AJBFU
AJOXV
ALMA_UNASSIGNED_HOLDINGS
AMFUW
AMRAJ
ASPBG
AVWKF
AXJTR
AZFZN
BKOJK
BLXMC
CS3
DOVZS
EBS
EFJIC
EFLBG
EJD
EO8
EO9
EP2
EP3
FDB
FEDTE
FGOYB
FIRID
FNPLU
FYGXN
G-2
G-Q
GBLVA
HLW
HVGLF
HZ~
IHE
J1W
KOM
LX3
M41
MO0
N9A
O-L
O9-
OAUVE
OHT
OZT
P-8
P-9
PC.
Q38
R2-
ROL
RPZ
SBG
SCC
SDF
SDG
SDP
SES
SEW
SPCBC
SSU
SSZ
T5K
UQL
WH7
WUQ
XJT
XPP
~G-
AAHBH
AATTM
AAXKI
AAYWO
AAYXX
ABWVN
ACRPL
ACVFH
ADCNI
ADNMO
AEIPS
AEUPX
AFJKZ
AFPUW
AGCQF
AGQPQ
AGRNS
AIGII
AIIUN
AKBMS
AKRWK
AKYEP
ANKPU
APXCP
BNPGV
CITATION
SSH
-~X
.55
.GJ
ABJNI
CGR
CUY
CVF
ECM
EIF
F5P
H~9
MVM
NPM
PKN
TWZ
UHS
X7M
Y6R
ZGI
~KM
7X8
ID FETCH-LOGICAL-c360t-407518691c3c53d8079b2a5d244c6f58a8ec869f6f97a66d69efd3b60233bf7e3
IEDL.DBID AIKHN
ISSN 0304-4165
0006-3002
IngestDate Fri Jul 11 15:16:47 EDT 2025
Wed Feb 19 02:33:23 EST 2025
Thu Apr 24 23:04:03 EDT 2025
Tue Jul 01 03:48:51 EDT 2025
Fri Feb 23 02:32:49 EST 2024
IsPeerReviewed true
IsScholarly true
Issue 3
Keywords β-Xylosidase
Methyl β- d-mannopyranoside
β-Mannosidase
Xylobiose permease
Aureobasidium pullulans
β-1,4-Xylanase
β-1,4-Mannanase
Mannobiose permease
Transport
Methyl β- d-xylopyranoside
Language English
License https://www.elsevier.com/tdm/userlicense/1.0
LinkModel DirectLink
MergedId FETCHMERGED-LOGICAL-c360t-407518691c3c53d8079b2a5d244c6f58a8ec869f6f97a66d69efd3b60233bf7e3
Notes ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
PMID 9838219
PQID 70110536
PQPubID 23479
PageCount 7
ParticipantIDs proquest_miscellaneous_70110536
pubmed_primary_9838219
crossref_citationtrail_10_1016_S0304_4165_98_00112_3
crossref_primary_10_1016_S0304_4165_98_00112_3
elsevier_sciencedirect_doi_10_1016_S0304_4165_98_00112_3
ProviderPackageCode CITATION
AAYXX
PublicationCentury 1900
PublicationDate 1998-11-27
PublicationDateYYYYMMDD 1998-11-27
PublicationDate_xml – month: 11
  year: 1998
  text: 1998-11-27
  day: 27
PublicationDecade 1990
PublicationPlace Netherlands
PublicationPlace_xml – name: Netherlands
PublicationTitle Biochimica et biophysica acta
PublicationTitleAlternate Biochim Biophys Acta
PublicationYear 1998
Publisher Elsevier B.V
Publisher_xml – name: Elsevier B.V
References Leathers, Kurzman, Detroy (BIB1) 1984; 14
Kremnický, Biely (BIB5) 1997; 167
Kobata (BIB19) 1992; 209
Myburgh, Prior, Kilian (BIB3) 1991; 72
Cheng, Michels (BIB11) 1991; 173
Görts (BIB10) 1969; 184
Leathers, Detroy, Bothast (BIB2) 1986; 8
Ballou (BIB18) 1976; 14
Paleg (BIB8) 1959; 31
J. Puls, J. Schuseil, in: M.P. Coughlan, G.P. Hazlewood (Eds.), Hemicellulose and Hemicellulases, Portland press, London, 1993, pp. 1–29.
Ebringerová, Kramár, Rendoš, Domanský (BIB9) 1967; 21
Dubois, Gilles, Hamilton, Rebers, Smith (BIB7) 1956; 28
Purkathofer, Sinner, Steiner (BIB17) 1993; 15
Smith, Wood (BIB16) 1991; 38
Evans, Sheppard, Turner, Wavell (BIB6) 1974; 10
Yasui, Nguyen, Nakanishi (BIB15) 1984; 62
Kremnický, Sláviková, Mislovičová, Biely (BIB4) 1996; 41
Kubicek, Messner, Gruber, Mendels, Kubicek-Pranz (BIB12) 1993; 268
Medintz, Jiang, Han, Cui, Michels (BIB13) 1996; 178
Leathers (10.1016/S0304-4165(98)00112-3_BIB2) 1986; 8
Medintz (10.1016/S0304-4165(98)00112-3_BIB13) 1996; 178
Ebringerová (10.1016/S0304-4165(98)00112-3_BIB9) 1967; 21
Kobata (10.1016/S0304-4165(98)00112-3_BIB19) 1992; 209
Leathers (10.1016/S0304-4165(98)00112-3_BIB1) 1984; 14
Kremnický (10.1016/S0304-4165(98)00112-3_BIB5) 1997; 167
Smith (10.1016/S0304-4165(98)00112-3_BIB16) 1991; 38
Cheng (10.1016/S0304-4165(98)00112-3_BIB11) 1991; 173
Dubois (10.1016/S0304-4165(98)00112-3_BIB7) 1956; 28
10.1016/S0304-4165(98)00112-3_BIB14
Ballou (10.1016/S0304-4165(98)00112-3_BIB18) 1976; 14
Evans (10.1016/S0304-4165(98)00112-3_BIB6) 1974; 10
Myburgh (10.1016/S0304-4165(98)00112-3_BIB3) 1991; 72
Kremnický (10.1016/S0304-4165(98)00112-3_BIB4) 1996; 41
Paleg (10.1016/S0304-4165(98)00112-3_BIB8) 1959; 31
Purkathofer (10.1016/S0304-4165(98)00112-3_BIB17) 1993; 15
Kubicek (10.1016/S0304-4165(98)00112-3_BIB12) 1993; 268
Görts (10.1016/S0304-4165(98)00112-3_BIB10) 1969; 184
Yasui (10.1016/S0304-4165(98)00112-3_BIB15) 1984; 62
References_xml – volume: 209
  start-page: 483
  year: 1992
  end-page: 501
  ident: BIB19
  publication-title: Eur. J. Biochem.
– volume: 72
  start-page: 135
  year: 1991
  end-page: 137
  ident: BIB3
  publication-title: J. Ferment. Bioeng.
– volume: 167
  start-page: 350
  year: 1997
  end-page: 355
  ident: BIB5
  publication-title: Arch. Microbiol.
– volume: 15
  start-page: 677
  year: 1993
  end-page: 682
  ident: BIB17
  publication-title: Enzyme Microb. Technol.
– volume: 14
  start-page: 225
  year: 1984
  end-page: 240
  ident: BIB1
  publication-title: Biotech. Bioeng. Symp.
– volume: 10
  start-page: 569
  year: 1974
  end-page: 587
  ident: BIB6
  publication-title: J. Label. Compd.
– reference: J. Puls, J. Schuseil, in: M.P. Coughlan, G.P. Hazlewood (Eds.), Hemicellulose and Hemicellulases, Portland press, London, 1993, pp. 1–29.
– volume: 28
  start-page: 350
  year: 1956
  end-page: 356
  ident: BIB7
  publication-title: Anal. Chem.
– volume: 41
  start-page: 43
  year: 1996
  end-page: 47
  ident: BIB4
  publication-title: Folia Microbiol.
– volume: 8
  start-page: 867
  year: 1986
  end-page: 872
  ident: BIB2
  publication-title: Biotechnol. Lett.
– volume: 268
  start-page: 19364
  year: 1993
  end-page: 19368
  ident: BIB12
  publication-title: J. Biol. Chem.
– volume: 38
  start-page: 883
  year: 1991
  end-page: 890
  ident: BIB16
  publication-title: Biotechnol. Bioeng.
– volume: 21
  start-page: 74
  year: 1967
  end-page: 77
  ident: BIB9
  publication-title: Holzforschung
– volume: 184
  start-page: 299
  year: 1969
  end-page: 305
  ident: BIB10
  publication-title: Biochim. Biophys. Acta
– volume: 62
  start-page: 353
  year: 1984
  end-page: 359
  ident: BIB15
  publication-title: J. Ferment. Technol.
– volume: 178
  start-page: 2245
  year: 1996
  end-page: 2254
  ident: BIB13
  publication-title: J. Bacteriol.
– volume: 14
  start-page: 93
  year: 1976
  end-page: 158
  ident: BIB18
  publication-title: Adv. Microbial Physiol.
– volume: 31
  start-page: 1902
  year: 1959
  end-page: 1904
  ident: BIB8
  publication-title: Anal. Chem.
– volume: 173
  start-page: 1817
  year: 1991
  end-page: 1820
  ident: BIB11
  publication-title: J. Bacteriol.
– volume: 268
  start-page: 19364
  year: 1993
  ident: 10.1016/S0304-4165(98)00112-3_BIB12
  publication-title: J. Biol. Chem.
  doi: 10.1016/S0021-9258(19)36523-8
– volume: 72
  start-page: 135
  year: 1991
  ident: 10.1016/S0304-4165(98)00112-3_BIB3
  publication-title: J. Ferment. Bioeng.
  doi: 10.1016/0922-338X(91)90325-B
– volume: 178
  start-page: 2245
  year: 1996
  ident: 10.1016/S0304-4165(98)00112-3_BIB13
  publication-title: J. Bacteriol.
  doi: 10.1128/jb.178.8.2245-2254.1996
– volume: 15
  start-page: 677
  year: 1993
  ident: 10.1016/S0304-4165(98)00112-3_BIB17
  publication-title: Enzyme Microb. Technol.
  doi: 10.1016/0141-0229(93)90068-D
– volume: 41
  start-page: 43
  year: 1996
  ident: 10.1016/S0304-4165(98)00112-3_BIB4
  publication-title: Folia Microbiol.
  doi: 10.1007/BF02816339
– volume: 167
  start-page: 350
  year: 1997
  ident: 10.1016/S0304-4165(98)00112-3_BIB5
  publication-title: Arch. Microbiol.
  doi: 10.1007/s002030050454
– volume: 10
  start-page: 569
  year: 1974
  ident: 10.1016/S0304-4165(98)00112-3_BIB6
  publication-title: J. Label. Compd.
  doi: 10.1002/jlcr.2590100407
– volume: 8
  start-page: 867
  year: 1986
  ident: 10.1016/S0304-4165(98)00112-3_BIB2
  publication-title: Biotechnol. Lett.
  doi: 10.1007/BF01078647
– volume: 62
  start-page: 353
  year: 1984
  ident: 10.1016/S0304-4165(98)00112-3_BIB15
  publication-title: J. Ferment. Technol.
– volume: 14
  start-page: 225
  year: 1984
  ident: 10.1016/S0304-4165(98)00112-3_BIB1
  publication-title: Biotech. Bioeng. Symp.
– ident: 10.1016/S0304-4165(98)00112-3_BIB14
– volume: 38
  start-page: 883
  year: 1991
  ident: 10.1016/S0304-4165(98)00112-3_BIB16
  publication-title: Biotechnol. Bioeng.
  doi: 10.1002/bit.260380810
– volume: 28
  start-page: 350
  year: 1956
  ident: 10.1016/S0304-4165(98)00112-3_BIB7
  publication-title: Anal. Chem.
  doi: 10.1021/ac60111a017
– volume: 209
  start-page: 483
  year: 1992
  ident: 10.1016/S0304-4165(98)00112-3_BIB19
  publication-title: Eur. J. Biochem.
  doi: 10.1111/j.1432-1033.1992.tb17313.x
– volume: 14
  start-page: 93
  year: 1976
  ident: 10.1016/S0304-4165(98)00112-3_BIB18
  publication-title: Adv. Microbial Physiol.
  doi: 10.1016/S0065-2911(08)60227-1
– volume: 31
  start-page: 1902
  year: 1959
  ident: 10.1016/S0304-4165(98)00112-3_BIB8
  publication-title: Anal. Chem.
  doi: 10.1021/ac60155a072
– volume: 21
  start-page: 74
  year: 1967
  ident: 10.1016/S0304-4165(98)00112-3_BIB9
  publication-title: Holzforschung
  doi: 10.1515/hfsg.1967.21.3.74
– volume: 184
  start-page: 299
  year: 1969
  ident: 10.1016/S0304-4165(98)00112-3_BIB10
  publication-title: Biochim. Biophys. Acta
  doi: 10.1016/0304-4165(69)90032-4
– volume: 173
  start-page: 1817
  year: 1991
  ident: 10.1016/S0304-4165(98)00112-3_BIB11
  publication-title: J. Bacteriol.
  doi: 10.1128/jb.173.5.1817-1820.1991
SSID ssj0000595
ssj0025309
Score 1.6225426
Snippet Aureobasidium pullulans, a yeast-like microorganism was found to produce mannobiose permease and xylobiose permease, transporting β-1,4-mannobiose or...
Aureobasidium pullulans, a yeast-like microorganism was found to produce mannobiose permease and xylobiose permease, transporting beta-1,4-mannobiose or...
SourceID proquest
pubmed
crossref
elsevier
SourceType Aggregation Database
Index Database
Enrichment Source
Publisher
StartPage 560
SubjectTerms Aureobasidium pullulans
Disaccharides - metabolism
Mannans - metabolism
Mannobiose permease
Mannosidases - biosynthesis
Membrane Transport Proteins - biosynthesis
Methyl β- d-mannopyranoside
Methyl β- d-xylopyranoside
Mitosporic Fungi - enzymology
Polysaccharides - metabolism
Substrate Specificity
Transport
Xylobiose permease
Xylosidases - biosynthesis
β-1,4-Mannanase
β-1,4-Xylanase
β-Mannosidase
β-Xylosidase
Title Disaccharides permeases: constituents of xylanolytic and mannanolytic systems of Aureobasidium pullulans
URI https://dx.doi.org/10.1016/S0304-4165(98)00112-3
https://www.ncbi.nlm.nih.gov/pubmed/9838219
https://www.proquest.com/docview/70110536
Volume 1425
hasFullText 1
inHoldings 1
isFullTextHit
isPrint
link http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV3Nb9MwFH_ahxBcEAwmymD4wAEOXtu4dmxuVWEqVOwATOxmObajReqSamkketnfzrOTtOIwTeIUyfFzrLyX937O-wJ4bzJrjGOWeqksnaSOU2OMp1mqQrV0BAlZ-N_x_ULMLyffrvjVHsz6XJgQVtnp_lanR23djQy7tzlcFcXwZ3DqIZzgSgZck7B9OEyYEijah9Ovi_nFTiHz2HwlzKeBYJfI0y4SBz8o-TGuQ9l9Juo-CBpN0fkzeNphSDJtt_kc9nx5BI_arpKbI3g865u4vYDrz0VtbEitKpyvyQr1cPDH1J-IrdowgRBIQaqc_NksTVktN7gmMaUjN6YstwNtvec4b9rcetQBKMRFc0NWeIJtkLB-CZfnX37N5rRrrkAtE6M1nhuDw0WosWWWMydHqcoSwx2aeytyLo30Fm_nIlepEcIJ5XPHMoE2nmV56tkxHJRV6V8BsWmeI-7gdmTVBPVl5pRlIxezVvGD5wOY9O9T267yeGiAsdS7EDNkgw5s0ErGMLtEswGcbclWbemNhwhkzyz9jwxpNA8Pkb7rmauRQ8FpYkpfNbVOA0DiTAzguOX5di9KMon6_vX_P_UEnsQUx_GYJukbOFjfNv4tYpx1dgr7Z3fj006Sw3Xx4_fiL7F-9-o
linkProvider Elsevier
linkToHtml http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1LT9wwEB5RqopeqpYWdVtafOihPYR9OHZsbmgp2rbApSBxsxzbEZGWZEU2UvfCb2dsJ7vqASFxdTyO5bFnPnteAN90brS21CROSJOkmWWJ1toleSZ9tnQECbl_7zi_4LOr9Pc1u96CaR8L490qO9kfZXqQ1l3LsFvN4aIsh3-9UQ_hBJPC45oJfQEvUzy-_nQe3m_8PBA_sGhKSBPffRPGE4cIjd-l-BFGSehjCuoxABoU0elbeNMhSHIcJ_kOtly1C69iTcnVLuxM-xJu7-HmpGy08YFVpXUNWaAU9taY5oiYOjoJeDcKUhfk32quq3q-wjGJriy51VW1bojZnkO_4_bOoQTALVy2t2SB99cWCZsPcHX683I6S7rSComhfLTEW6M3t3A5NtQwasUok_lEM4vK3vCCCS2cwc8FL2SmObdcusLSnKOGp3mROboH21VduY9ATFYUiDqYGRmZorTMrTR0ZEPMKh53NoC0X09lurzjvvzFXG0czJANyrNBSRGc7CaKDuBwTbaIiTeeIhA9s9R_O0ihcniK9KBnrkIOeZOJrlzdNirz8IhRPoC9yPP1XKSgAqX9p-f_9QB2ZpfnZ-rs18Wfz_A6BDuOx8kk24ft5V3rviDaWeZfw25-APAV9ws
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=Disaccharides+permeases%3A+constituents+of+xylanolytic+and+mannanolytic+systems+of+Aureobasidium+pullulans&rft.jtitle=Biochimica+et+biophysica+acta&rft.au=Lubom%C3%ADr%2C+K&rft.au=Peter%2C+B&rft.date=1998-11-27&rft.issn=0006-3002&rft.volume=1425&rft.issue=3&rft.spage=560&rft_id=info:doi/10.1016%2FS0304-4165%2898%2900112-3&rft_id=info%3Apmid%2F9838219&rft.externalDocID=9838219
thumbnail_l http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0304-4165&client=summon
thumbnail_m http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0304-4165&client=summon
thumbnail_s http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0304-4165&client=summon