BRENDA - Enzyme Database

Structure and molecular mechanism of Bacillus anthracis cofactor-independent phosphoglycerate mutase: a crucial enzyme for spores and growing cells of Bacillus species

Nukui, M.; Mello, L.V.; Littlejohn, J.E.; Setlow, B.; Setlow, P.; Kim, K.; Leighton, T.; Jedrzejas, M.J.; Biophys. J. 92, 977-988 (2007)

Data extracted from this reference:

Cloned(Commentary)
EC Number
Commentary
Organism
5.4.2.12
expression in Escherichia coli
Bacillus anthracis
Crystallization (Commentary)
EC Number
Crystallization
Organism
5.4.2.12
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
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
5.4.2.12
Bacillus anthracis
Q81X77
-
-
Purification (Commentary)
EC Number
Commentary
Organism
5.4.2.12
recombinant protein
Bacillus anthracis
Reaction
EC Number
Reaction
Commentary
Organism
5.4.2.12
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
Source Tissue
EC Number
Source Tissue
Commentary
Organism
Textmining
Specific Activity [micromol/min/mg]
EC Number
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
5.4.2.12
37
-
23°C
Bacillus anthracis
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
5.4.2.12
2-phospho-D-glycerate
-
678734
Bacillus anthracis
3-phospho-D-glycerate
-
-
-
r
5.4.2.12
3-phospho-D-glycerate
-
678734
Bacillus anthracis
2-phospho-D-glycerate
-
-
-
r
Cloned(Commentary) (protein specific)
EC Number
Commentary
Organism
5.4.2.12
expression in Escherichia coli
Bacillus anthracis
Crystallization (Commentary) (protein specific)
EC Number
Crystallization
Organism
5.4.2.12
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
Purification (Commentary) (protein specific)
EC Number
Commentary
Organism
5.4.2.12
recombinant protein
Bacillus anthracis
Source Tissue (protein specific)
EC Number
Source Tissue
Commentary
Organism
Textmining
Specific Activity [micromol/min/mg] (protein specific)
EC Number
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
5.4.2.12
37
-
23°C
Bacillus anthracis
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
5.4.2.12
2-phospho-D-glycerate
-
678734
Bacillus anthracis
3-phospho-D-glycerate
-
-
-
r
5.4.2.12
3-phospho-D-glycerate
-
678734
Bacillus anthracis
2-phospho-D-glycerate
-
-
-
r