Orotidine 5'-Monophosphate Decarboxylase: The Operation of Active Site Chains Within and Across Protein Subunits.


Journal

Biochemistry
ISSN: 1520-4995
Titre abrégé: Biochemistry
Pays: United States
ID NLM: 0370623

Informations de publication

Date de publication:
02 06 2020
Historique:
pubmed: 7 5 2020
medline: 24 2 2021
entrez: 7 5 2020
Statut: ppublish

Résumé

The D37 and T100' side chains of orotidine 5'-monophosphate decarboxylase (OMPDC) interact with the C-3' and C-2' ribosyl hydroxyl groups, respectively, of the bound substrate. We compare the intra-subunit interactions of D37 with the inter-subunit interactions of T100' by determining the effects of the D37G, D37A, T100'G, and T100'A substitutions on the following: (a)

Identifiants

pubmed: 32374983
doi: 10.1021/acs.biochem.0c00241
pmc: PMC7476526
doi:

Substances chimiques

Protein Subunits 0
orotidylic acid 2149-82-8
Uridine Monophosphate E2OU15WN0N
Orotidine-5'-Phosphate Decarboxylase EC 4.1.1.23

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

2032-2040

Subventions

Organisme : NIGMS NIH HHS
ID : R01 GM116921
Pays : United States
Organisme : NIGMS NIH HHS
ID : R35 GM134881
Pays : United States

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Auteurs

Tiago A S Brandão (TAS)

Department of Chemistry, ICEx, Federal University of Minas Gerais, Belo Horizonte, Minas Gerais 31270-901, Brazil.

John P Richard (JP)

Department of Chemistry, University at Buffalo, The State University of New York, Buffalo, New York 14260-3000, United States.

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Classifications MeSH