The Thr45Gly substitution in yeast alcohol dehydrogenase substantially decreases catalysis, alters pH dependencies, and disrupts the proton relay system.
Enzyme kinetics
Enzyme mechanism
Mutagenesis
Protein structure
Proton transfer
Journal
Chemico-biological interactions
ISSN: 1872-7786
Titre abrégé: Chem Biol Interact
Pays: Ireland
ID NLM: 0227276
Informations de publication
Date de publication:
01 Nov 2021
01 Nov 2021
Historique:
received:
03
06
2021
revised:
19
08
2021
accepted:
09
09
2021
pubmed:
17
9
2021
medline:
27
10
2021
entrez:
16
9
2021
Statut:
ppublish
Résumé
X-Ray crystallography shows that the hydroxyl group of Thr-45 in the fermentative alcohol dehydrogenase (ADH1) from Saccharomyces cerevisiae is hydrogen-bonded to the hydroxyl group of the alcohol bound to the catalytic zinc and is part of a proton relay system linked to His-48. The contribution of Thr-45 to catalysis was studied with steady state kinetics of the enzyme with the T45G substitution. Affinities for coenzymes decrease by only 2-4-fold, but the turnover numbers (V/E
Identifiants
pubmed: 34529977
pii: S0009-2797(21)00288-X
doi: 10.1016/j.cbi.2021.109650
pmc: PMC8530938
mid: NIHMS1742947
pii:
doi:
Substances chimiques
Protons
0
Saccharomyces cerevisiae Proteins
0
Alcohol Dehydrogenase
EC 1.1.1.1
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
109650Subventions
Organisme : NIAAA NIH HHS
ID : R01 AA000279
Pays : United States
Informations de copyright
Copyright © 2021 Elsevier B.V. All rights reserved.
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