Literature summary for 5.4.2.12 extracted from

Nukui, M.; Mello, L.V.; Littlejohn, J.E.; Setlow, B.; Setlow, P.; Kim, K.; Leighton, T.; Jedrzejas, M.J.
Structure and molecular mechanism of Bacillus anthracis cofactor-independent phosphoglycerate mutase: a crucial enzyme for spores and growing cells of Bacillus species (2007), Biophys. J., 92, 977-988.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Bacillus anthracis

Crystallization (Commentary)

Crystallization (Comment)	Organism
protein is composed of two structural and functiional domains, the phosphatase and the transferase. Comparison with the structurally similar domains of in Bacillus stearothermophilus	Bacillus anthracis

Organism

Organism	UniProt	Comment	Textmining
Bacillus anthracis	Q81X77	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant protein	Bacillus anthracis

Reaction

Reaction	Comment	Organism	Reaction ID
2-phospho-D-glycerate = 3-phospho-D-glycerate	in the phospho-D-glycerate-free state the enzyme assumes an open conformation. Upon substrate binding the enzyme closes to the catalytically functional conformation, in the closed form the enzyme catalyzes 2/3-phospho-D-glycerate isomerization resulting in product release. Product release causes opening of the enzyme and return to the open conformation	Bacillus anthracis	a

Source Tissue

Source Tissue	Comment	Organism	Textmining

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
37	-	23°C	Bacillus anthracis

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
2-phospho-D-glycerate	-	Bacillus anthracis	3-phospho-D-glycerate	-	r
3-phospho-D-glycerate	-	Bacillus anthracis	2-phospho-D-glycerate	-	r

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Release 2023.1 (January 2023)