Alcohol dehydrogenase polymorphism in Drosophila: enzyme kinetics of product inhibition
Because natural populations of Drosophila melanogaster are polymorphic for different allozymes of alcohol dehydrogenase (ADH) and because D. melanogaster is more tolerant to the toxic effects of ethanol than its sibling species D. simulans, information regarding the sensitivities of the different fo...
Saved in:
Published in | Journal of molecular evolution Vol. 28; no. 1-2; p. 145 |
---|---|
Main Authors | , , |
Format | Journal Article |
Language | English |
Published |
Germany
1989
|
Subjects | |
Online Access | Get more information |
Cover
Loading…
Abstract | Because natural populations of Drosophila melanogaster are polymorphic for different allozymes of alcohol dehydrogenase (ADH) and because D. melanogaster is more tolerant to the toxic effects of ethanol than its sibling species D. simulans, information regarding the sensitivities of the different forms of ADH to the products of ethanol degradation are of ecological importance. ADH-F, ADH-S, ADH-71k of D. melanogaster and the ADH of D. simulans were inhibited by NADH, but the inhibition was relieved by NAD+. The order of sensitivity to NADH was ADH-F less than ADH-71k, ADH-S less than ADH-simulans with ADH-F being about four times less sensitive than the D. melanogaster enzymes and 12 times less sensitive than the D. simulans enzyme. Acetaldehyde inhibited the ethanol-to-acetaldehyde activity of the ADHs, but at low acetaldehyde concentrations ethanol and NAD+ reduced the inhibition. ADH-71k and ADH-F were more subject to the inhibitory action of acetaldehyde than ADH-S and ADH-simulans, with ADH-71k being seven times more sensitive than ADH-S. The pattern of product inhibition of ADH-71k suggests a rapid equilibrium random mechanism for ethanol oxidation. Thus, although the ADH variants only differ by a few amino acids, these differences exert a far larger impact on their intrinsic properties than previously thought. How differences in product inhibition may be of significance in the evolution of the ADHs is discussed. |
---|---|
AbstractList | Because natural populations of Drosophila melanogaster are polymorphic for different allozymes of alcohol dehydrogenase (ADH) and because D. melanogaster is more tolerant to the toxic effects of ethanol than its sibling species D. simulans, information regarding the sensitivities of the different forms of ADH to the products of ethanol degradation are of ecological importance. ADH-F, ADH-S, ADH-71k of D. melanogaster and the ADH of D. simulans were inhibited by NADH, but the inhibition was relieved by NAD+. The order of sensitivity to NADH was ADH-F less than ADH-71k, ADH-S less than ADH-simulans with ADH-F being about four times less sensitive than the D. melanogaster enzymes and 12 times less sensitive than the D. simulans enzyme. Acetaldehyde inhibited the ethanol-to-acetaldehyde activity of the ADHs, but at low acetaldehyde concentrations ethanol and NAD+ reduced the inhibition. ADH-71k and ADH-F were more subject to the inhibitory action of acetaldehyde than ADH-S and ADH-simulans, with ADH-71k being seven times more sensitive than ADH-S. The pattern of product inhibition of ADH-71k suggests a rapid equilibrium random mechanism for ethanol oxidation. Thus, although the ADH variants only differ by a few amino acids, these differences exert a far larger impact on their intrinsic properties than previously thought. How differences in product inhibition may be of significance in the evolution of the ADHs is discussed. |
Author | Scharloo, W Thorig, G E Heinstra, P W |
Author_xml | – sequence: 1 givenname: P W surname: Heinstra fullname: Heinstra, P W organization: Department of Population and Evolutionary Biology, University of Utrecht, The Netherlands – sequence: 2 givenname: W surname: Scharloo fullname: Scharloo, W – sequence: 3 givenname: G E surname: Thorig fullname: Thorig, G E |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/3148735$$D View this record in MEDLINE/PubMed |
BookMark | eNotj8tKAzEARbOo1La6cS_kB0bznEzc1dqqUHCjuCyZPJzoTBKS6WL8egt2dTlwOHCXYBZisADcYHSHERL3jztEMKMc1TOwQIiQijSMXYJlKd8IYcElnYM5xawRlC_A57rXsYs9NLabTI5fNqhiYYr9NMScOl8G6AN8yrHEE_XqAdrwOw0W_vhgR68LjA6mHM1Rjyez860ffQxX4MKpvtjr867Ax277vnmp9m_Pr5v1vkqkrscKK0IZbywnWmjJDce2xZQxJag2XLraaeRqIilymkphWtKaRnFFFdZICkpW4Pa_m47tYM0hZT-oPB3OB8kfNSRS1Q |
ContentType | Journal Article |
DBID | CGR CUY CVF ECM EIF NPM |
DOI | 10.1007/BF02143506 |
DatabaseName | Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed |
DatabaseTitle | MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) |
DatabaseTitleList | 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 | no_fulltext_linktorsrc |
Discipline | Biology |
ExternalDocumentID | 3148735 |
Genre | Journal Article Comparative Study |
GroupedDBID | --- -4W -56 -5G -BR -DZ -EM -Y2 -~C -~X .86 .GJ 06C 06D 0R~ 0VY 186 199 1N0 1SB 2.D 203 28- 29L 29~ 2J2 2JN 2JY 2KG 2KM 2LR 2P1 2VQ 2~H 30V 36B 3SX 3V. 4.4 406 408 409 40D 40E 53G 5GY 5QI 5VS 67N 67Z 6NX 78A 7X7 88A 88E 8AO 8FE 8FH 8FI 8FJ 8G5 8TC 8UJ 95- 95. 95~ 96X A8Z AAAVM AABHQ AACDK AAEOY AAGAY AAHNG AAIAL AAJBT AAJKR AANXM AANZL AAQLM AARHV AARTL AASML AATNV AATVU AAUYE AAWCG AAYIU AAYQN AAYTO AAYZH ABAKF ABBBX ABBXA ABDBF ABDZT ABECU ABFTV ABHLI ABHQN ABJNI ABJOX ABKCH ABKTR ABLJU ABMNI ABMQK ABNWP ABPLI ABQBU ABSXP ABTEG ABTHY ABTKH ABTMW ABULA ABUWG ABWNU ABXPI ACAOD ACBXY ACDTI ACGFS ACHSB ACHXU ACIPQ ACIWK ACKNC ACMDZ ACMLO ACNCT ACOKC ACOMO ACPRK ACZOJ ADBBV ADHHG ADHIR ADIMF ADINQ ADKNI ADKPE ADRFC ADTPH ADURQ ADYFF ADYPR ADZKW AEBTG AEFIE AEFQL AEGAL AEGNC AEJHL AEJRE AEKMD AEMSY AENEX AEOHA AEPYU AESKC AETLH AEVLU AEXYK AFBBN AFDYV AFEXP AFGCZ AFKRA AFLOW AFQWF AFRAH AFWTZ AFZKB AGAYW AGDGC AGGDS AGJBK AGMZJ AGQEE AGQMX AGRTI AGWIL AGWZB AGYKE AHAVH AHBYD AHKAY AHMBA AHSBF AHYZX AI. AIAKS AIGIU AIIXL AILAN AITGF AJBLW AJRNO AJZVZ AKMHD ALIPV ALMA_UNASSIGNED_HOLDINGS ALWAN AMKLP AMXSW AMYLF AMYQR AOCGG ARMRJ ASPBG AVWKF AXYYD AZFZN AZQEC B-. B0M BA0 BBNVY BBWZM BDATZ BENPR BGNMA BHPHI BPHCQ BVXVI CCPQU CGR CS3 CSCUP CUY CVF DDRTE DL5 DNIVK DPUIP DU5 DWQXO EAD EAP EAS EBD EBLON EBS ECM EIF EIOEI EJD EMB EMK EMOBN EN4 EPAXT EPL ESBYG ESTFP ESX F5P FEDTE FERAY FFXSO FIGPU FINBP FNLPD FRRFC FSGXE FWDCC FYUFA G-Y G-Z GGCAI GGRSB GJIRD GNUQQ GNWQR GQ6 GQ7 GQ8 GUQSH GXS H13 HCIFZ HF~ HG5 HG6 HMCUK HMJXF HQYDN HRMNR HVGLF HZ~ I-F I09 IHE IJ- IKXTQ ITM IWAJR IXC IZIGR IZQ I~X I~Z J-C J0Z JBSCW JCJTX JZLTJ KDC KOV KOW KPH LAS LK8 LLZTM M0L M1P M2O M4Y M7P MA- MQGED MVM N2Q N9A NB0 NDZJH NPM NPVJJ NQJWS NU0 O9- O93 O9G O9I O9J OAM OHT P19 P2P PF- PQQKQ PROAC PSQYO PT4 PT5 Q2X QF4 QM4 QN7 QO4 QOK QOR QOS R4E R89 R9I RHV RIG RNI RNS ROL RPX RRX RSV RZK S16 S1Z S26 S27 S28 S3A S3B SAP SBL SBY SCLPG SDH SDM SHX SISQX SJYHP SNE SNPRN SNX SOHCF SOJ SPISZ SRMVM SSLCW SSXJD STPWE SV3 SZN T13 T16 TN5 TSG TSK TSV TUC TUS U2A U9L UG4 UKHRP UOJIU UTJUX UZXMN VC2 VFIZW VH1 W23 W48 WH7 WJK WK6 WK8 XJT XOL YLTOR YQT Z45 Z7U Z7V Z7W Z82 Z83 Z8O Z8P Z8Q Z8V Z8W ZMTXR ZOVNA ZXP ~02 ~8M ~EX ~KM |
ID | FETCH-LOGICAL-p266t-1a23458e52c7c95d51eb1344a73cd59f6fc0f62930fc397db2bd8a5a3a1c09732 |
ISSN | 0022-2844 |
IngestDate | Wed Oct 16 00:47:29 EDT 2024 |
IsPeerReviewed | true |
IsScholarly | true |
Issue | 1-2 |
Language | English |
LinkModel | OpenURL |
MergedId | FETCHMERGED-LOGICAL-p266t-1a23458e52c7c95d51eb1344a73cd59f6fc0f62930fc397db2bd8a5a3a1c09732 |
PMID | 3148735 |
ParticipantIDs | pubmed_primary_3148735 |
PublicationCentury | 1900 |
PublicationDate | 1988 Dec-1989 Feb |
PublicationDateYYYYMMDD | 1989-01-01 |
PublicationDate_xml | – year: 1989 text: 1988 Dec-1989 Feb |
PublicationDecade | 1980 |
PublicationPlace | Germany |
PublicationPlace_xml | – name: Germany |
PublicationTitle | Journal of molecular evolution |
PublicationTitleAlternate | J Mol Evol |
PublicationYear | 1989 |
SSID | ssj0017593 |
Score | 1.4143862 |
Snippet | Because natural populations of Drosophila melanogaster are polymorphic for different allozymes of alcohol dehydrogenase (ADH) and because D. melanogaster is... |
SourceID | pubmed |
SourceType | Index Database |
StartPage | 145 |
SubjectTerms | Alcohol Dehydrogenase - antagonists & inhibitors Alcohol Dehydrogenase - genetics Animals Drosophila - enzymology Drosophila - genetics Drosophila melanogaster - enzymology Drosophila melanogaster - genetics Kinetics NAD - metabolism Polymorphism, Genetic Species Specificity |
Title | Alcohol dehydrogenase polymorphism in Drosophila: enzyme kinetics of product inhibition |
URI | https://www.ncbi.nlm.nih.gov/pubmed/3148735 |
Volume | 28 |
hasFullText | |
inHoldings | 1 |
isFullTextHit | |
isPrint | |
link | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1JS8NAGB1cELyIW3FnDt5CJMnMNKm34opg8aDoTWZJaNAmpRSh_fV-szTporhcQsiEkMx7M9-bybcgdKoCENWgw30iKfFB_3MfzIL0GQdzJqWMKdXByfed5u0TvXthL7Urr4kuGYozOf4yruQ_qMI1wFVHyf4B2eqhcAHOAV84AsJw_BXGbVvf1lNpd6QGJdwHNknXXYAFPfSfrn-RF97lwNQqyN9tGZ5iPOql3huoS5OhWXs826yvcG83F3mF1KJk7U1q6Xrph_uwei8117lojRR98OqNGx3V9V6WlSufc0IZ5GaKuXGBEIpXflXVtkMdBgC2jU5PpVEyTRkX12hnxtBmjVyYsYOJH3qklZvJPjCcgq7fM9gRWLXFhP3YOJc727Uso-U40dNfR2_luF9M8SQjs_uO2dy17m3W0Zp7xtyyw8iPx0204UDAbUuCLbSUFttozVYSHe2gZ0cFPEMFPE0FnBe4psI5tkTAEyLgMsOOCLgmwi56ur56vLj1Xc0Mvw9Sa-iHPCKUJSmLZCxbTLEQjDGhlMdEKtbKmpkMsiZovCCTIEWViIRKOOOEh9JkbmqglaIs0j2EGSUyDlRLMhixIhUJDYRqwchWXIBVDPdRw_bIa98mRnl1XXXwXcMhWq-pdIRWMxiH6TGIuqE4MeB8Ai0CTYA |
link.rule.ids | 786 |
linkProvider | National Library of Medicine |
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=Alcohol+dehydrogenase+polymorphism+in+Drosophila%3A+enzyme+kinetics+of+product+inhibition&rft.jtitle=Journal+of+molecular+evolution&rft.au=Heinstra%2C+P+W&rft.au=Scharloo%2C+W&rft.au=Thorig%2C+G+E&rft.date=1989-01-01&rft.issn=0022-2844&rft.volume=28&rft.issue=1-2&rft.spage=145&rft_id=info:doi/10.1007%2FBF02143506&rft_id=info%3Apmid%2F3148735&rft_id=info%3Apmid%2F3148735&rft.externalDocID=3148735 |
thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0022-2844&client=summon |
thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0022-2844&client=summon |
thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0022-2844&client=summon |