Information on EC 5.4.99.3 - 2-Acetolactate mutase

for references in articles please use BRENDA:EC5.4.99.3
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The expected taxonomic range for this enzyme is: Mycobacterium tuberculosis

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EC NUMBER
COMMENTARY hide
5.4.99.3
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RECOMMENDED NAME
GeneOntology No.
2-Acetolactate mutase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2-acetolactate = 3-hydroxy-3-methyl-2-oxobutanoate
show the reaction diagram
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
group transfer
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intramolecular
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isomerization
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Valine, leucine and isoleucine biosynthesis
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Biosynthesis of secondary metabolites
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Biosynthesis of antibiotics
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SYSTEMATIC NAME
IUBMB Comments
2-acetolactate methylmutase
Requires ascorbic acid; also converts 2-aceto-2-hydroxybutanoate to 3-hydroxy-3-methyl-2-oxopentanoate.
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CAS REGISTRY NUMBER
COMMENTARY hide
37318-52-8
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
H37Rv
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-
Manually annotated by BRENDA team
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-aceto-2-hydroxybutanoate
3-hydroxy-3-methyl-2-oxopentanoate
show the reaction diagram
2-Acetolactate
3-Hydroxy-3-methyl-2-oxobutanoate
show the reaction diagram
2-Acetolactate
?
show the reaction diagram
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2-Acetolactate
?
show the reaction diagram
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ascorbic acid
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required, D-ascorbate shows 80% of L-ascorbate in enhancing the reaction, cannot be replaced by other reducing agents
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.4
2-acetolactate
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-
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
90% loss of activity after 2 days, even when kept under frozen state
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LINKS TO OTHER DATABASES (specific for EC-Number 5.4.99.3)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)