Literature summary for 4.1.1.23 extracted from

Gao, J.
Catalysis by enzyme conformational change as illustrated by orotidine 5'-monophosphate decarboxylase (2003), Curr. Opin. Struct. Biol., 13, 184-192.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
X-ray structure of ODCase complexed with 6-azaorotidine 5-phosphate	Methanothermobacter thermautotrophicus

Protein Variants

Protein Variants	Comment	Organism
D70A	active site mutant	Methanothermobacter thermautotrophicus

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
Orotidine 5'-phosphate	Methanothermobacter thermautotrophicus	-	UMP + CO2	-	?

Organism

Organism	UniProt	Comment	Textmining
Methanothermobacter thermautotrophicus	-	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
orotidine 5'-phosphate = UMP + CO2	mechanism, thermodynamic data	Methanothermobacter thermautotrophicus	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
2'-deoxyorotidine 5'-phosphate	decreased catalytic rate compared with orotidine 5'-phosphate as substrate	Methanothermobacter thermautotrophicus	2'-deoxyuridine 5'-phosphate + CO2	-	?
Orotidine 5'-phosphate	-	Methanothermobacter thermautotrophicus	UMP + CO2	-	?
Orotidine 5'-phosphate	mechanism, enzyme conformation is more distorted in the reactant state than in the transition state, the energy released from conformation relaxation provides the predominant contribution to the rate enhancement, the active site consists of a network of charged residues Lys-42, Asp-70, Lys-72, Asp-75b	Methanothermobacter thermautotrophicus	UMP + CO2	-	?

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
additional information	-	additional information	-	Methanothermobacter thermautotrophicus

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Release 2023.1 (January 2023)