Literature summary for 4.1.1.23 extracted from

Wu, N.; Gillon, W.; Pai, E.F.
Mapping the active site-ligand interactions of orotidine 5'-monophosphate decarboxylase by crystallography (2002), Biochemistry, 41, 4002-4011.

Search for more literature for 4.1.1.23

Cloned(Commentary)

Cloned (Comment)	Organism
expression in SKP10 cells	Methanothermobacter thermautotrophicus

Crystallization (Commentary)

Crystallization (Comment)	Organism
native ODCase complexed with 6-azauridine 5'-phosphate, several active site mutants complexed with a variety of ligands, including substrate, product and inhibitors	Methanothermobacter thermautotrophicus

Protein Variants

Protein Variants	Comment	Organism
D70A	inactive active site mutant	Methanothermobacter thermautotrophicus
D70A/K72A	active site double mutant, markedly less stable than native enzyme	Methanothermobacter thermautotrophicus
D70G	active site mutant, markedly less stable than native enzyme	Methanothermobacter thermautotrophicus
D70N	active site mutant	Methanothermobacter thermautotrophicus
D75N	mutation of an active site residue contributed by the other monomer in the active dimer	Methanothermobacter thermautotrophicus
K42A	active site mutant	Methanothermobacter thermautotrophicus
K72A	inactive active site mutant	Methanothermobacter thermautotrophicus
Q185A	active site mutant, orotate recognition mutant	Methanothermobacter thermautotrophicus
S127A	active site mutant, orotate recognition mutant	Methanothermobacter thermautotrophicus

General Stability

General Stability	Organism
Asp-70 makes a crucial contribution to enzyme stability	Methanothermobacter thermautotrophicus

Inhibitors

Inhibitors	Comment	Organism	Structure
6-Azauracil	competitive inhibitor	Methanothermobacter thermautotrophicus
6-hydroxyuridine 5'-monophosphate	tightly binding competitive inhibitor	Methanothermobacter thermautotrophicus
guanidine hydrochloride	2 M, denaturates	Methanothermobacter thermautotrophicus

Metals/Ions

Metals/Ions	Comment	Organism	Structure
additional information	no metal ion requirement	Methanothermobacter thermautotrophicus

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
Orotidine 5'-phosphate	Methanothermobacter thermautotrophicus	catalyzes the last step of de novo pyrimidine synthesis	UMP + CO2	-	?

Organism

Organism	UniProt	Comment	Textmining
Methanothermobacter thermautotrophicus	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant enzyme	Methanothermobacter thermautotrophicus

Reaction

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

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
Orotidine 5'-phosphate	mechanism, Lys-42, Asp-70, Lys-72 and Asp-75b form an alternate charged network around the reactive part of substrate, Lys-72 protonates the intermediate C6 carbanion	Methanothermobacter thermautotrophicus	UMP + CO2	-	?
Orotidine 5'-phosphate	catalyzes the last step of de novo pyrimidine synthesis	Methanothermobacter thermautotrophicus	UMP + CO2	-	?

Subunits

Subunits	Comment	Organism
dimer	-	Methanothermobacter thermautotrophicus

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
70	-	Tm above 70°C	Methanothermobacter thermautotrophicus

Turnover Number [1/s]

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

Cofactor

Cofactor	Comment	Organism	Structure
additional information	no cofactor requirement	Methanothermobacter thermautotrophicus

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Release 2023.1 (January 2023)