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Cited by 32Biochemical Acid Research StudiesPhysical Organic Chemistry and Reaction KineticsEnzyme Structure and Function

The DOI matches its Crossref record; 18 of the 18 references it cites were found in a registry or an index.

Reaction Mechanism of the Heterotetrameric (α 2 β 2 ) E1 Component of 2-Oxo Acid Dehydrogenase Multienzyme Complexes

Fries, Markus, Jung, Hyo-Il, Perham, Richard N.·2003·Biochemistry
DOI 10.1021/bi027397z
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Abstract

Pyruvate decarboxylase (E1) catalyzes the first two reactions of the four involved in oxidative decarboxylation of pyruvate by the pyruvate dehydrogenase (PDH) multienzyme complex. It requires thiamin diphosphate to bring about the decarboxylation of pyruvate, which is followed by the reductive acetylation of a lipoyl group covalently bound to the N(6) amino group of a lysine residue in the second catalytic component, a dihydrolipoyl acetyltransferase (E2). Replacement of two histidine residues in the E1alpha and E1beta chains of the heterotetrameric E1 (alpha(2)beta(2)) component of the PDH complex of Bacillus stearothermophilus, considered possible proton donors at the active site, was carried out. Subsequent characterization of the mutants permitted different roles to be assigned to these two particular residues in the reaction catalyzed by E1: E1alpha His271 to stabilize the dianion formed during decarboxylation of the 2-oxo acid and E1beta His128 to provide the proton required to protonate the incoming dithiolane ring in the subsequent reductive acetylation of the lipoyl goup. On the basis of these and other results from a separate investigation into the roles of individual residues in a loop region in the E1alpha chain close to the active site of E1 [Fries, M., Chauhan, H. J., Domingo, G. J., Jung, H., and Perham, R. N. (2002) Eur. J. Biochem. 270, 861-870] together with work from other laboratories, a detailed mechanism for the E1 reaction can be formulated.

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Research works printed but not linked: 27

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Metadata

Authors
Fries, M., Jung, H.-I., & Perham, R. N.
Affiliations
University of Cambridge (GB)
Corresponding author
Perham, Richard N.
ORCID
Jung, Hyo-Il
Venue
Biochemistry
Publisher
American Chemical Society (ACS)
Published
2003-05-23
Volume
42
Issue
23
Pages
6996-7002
ISSN
  • 0006-2960 (ISSN-L)
  • 1520-4995
DOI
10.1021/bi027397z
OpenAlex
W1964930482
Cited by
32
References
18
Citations by year
2026: 2 · 2024: 1 · 2021: 2 · 2020: 1 · 2019: 2 · 2017: 1 · 2016: 1 · 2015: 4 · 2014: 2 · 2013: 1 · 2012: 2
FWCI
1.27
Type
journal article
Language
en
Open access
closed
Locations
  • Biochemistry (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Biochemical Acid Research Studies
  • Physical Sciences › Chemistry › Organic Chemistry › Physical Organic Chemistry and Reaction Kinetics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
Keywords
pyruvate decarboxylase, reaction mechanism, histidine mutants, proton transfer, thiamine pyrophosphate, Bacillus stearothermophilus, active site residues
MeSH terms
Acetylation, Geobacillus stearothermophilus, Binding Sites, Decarboxylation, Histidine, Ketone Oxidoreductases, Kinetics, Models, Molecular, Multienzyme Complexes, Protons, Pyruvate Decarboxylase, Recombinant Proteins, Temperature, Mutagenesis, Site-Directed, Protein Structure, Tertiary, Surface Plasmon Resonance, 3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide)

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