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Information on EC 4.1.1.72 - branched-chain-2-oxoacid decarboxylase and Organism(s) Bacillus subtilis and UniProt Accession Q04789

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EC Tree
     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.1 Carboxy-lyases
                4.1.1.72 branched-chain-2-oxoacid decarboxylase
IUBMB Comments
Acts on a number of 2-oxo acids, with a high affinity towards branched-chain substrates. The aldehyde formed may be enzyme-bound, and may be an intermediate in the bacterial system for the biosynthesis of branched-chain fatty acids.
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Bacillus subtilis
UNIPROT: Q04789
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The taxonomic range for the selected organisms is: Bacillus subtilis
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
bckad, ydl080c, alpha-keto acid decarboxylase, branched-chain alpha-keto acid decarboxylase, branched-chain 2-keto acid decarboxylase, mtkdc, branched-chain keto acid decarboxylase, branched-chain oxo acid decarboxylase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
BCKA
-
-
-
-
branched-chain 2-oxoacid decarboxylase
-
-
-
-
branched-chain alpha-keto acid decarboxylase
-
-
-
-
branched-chain keto acid decarboxylase
-
-
-
-
branched-chain oxo acid decarboxylase
-
-
-
-
decarboxylase, branched-chain oxo acid
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decarboxylation
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
(3S)-3-methyl-2-oxopentanoate carboxy-lyase (2-methylbutanal-forming)
Acts on a number of 2-oxo acids, with a high affinity towards branched-chain substrates. The aldehyde formed may be enzyme-bound, and may be an intermediate in the bacterial system for the biosynthesis of branched-chain fatty acids.
CAS REGISTRY NUMBER
COMMENTARY hide
63653-19-0
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-oxoisovalerate
isobutanal + CO2
show the reaction diagram
-
-
-
?
2-oxoglutarate
CO2 + succinate semialdehyde
show the reaction diagram
-
5% of the activity with L-3-methyl-2-oxopentanoate
-
-
?
2-oxoisohexanoate
CO2 + isopentanal
show the reaction diagram
-
38% of the activity with L-3-methyl-2-oxopentanoate
-
-
?
2-oxoisopentanoate
CO2 + isobutanal
show the reaction diagram
-
63% of the activity with L-3-methyl-
-
-
?
3-methyl-2-oxopentanoate
CO2 + 2-methylbutanal
show the reaction diagram
-
-
-
-
?
L-3-methyl-2-oxopentanoate
CO2 + 2-methylbutanal
show the reaction diagram
-
stereospecificity towards the L-isomer
-
-
?
pyruvate
ethanal + CO2
show the reaction diagram
-
25% of the activity with L-3-methyl-2-oxopentanoate
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
3-methyl-2-oxopentanoate
CO2 + 2-methylbutanal
show the reaction diagram
-
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ferricyanide
-
stimulates
additional information
-
no requirement for MgCl2
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
154 - 342
2-oxoisovalerate
0.001
L-3-Methyl-2-oxopentanoate
-
and 2-oxoisopentanoate, 2-oxoisohexanoate, value below, 30°C, pH 7.5
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.8 - 8.9
2-oxoisovalerate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.005 - 0.03
2-oxoisovalerate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.02
-
30°C, pH 7.5
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9
-
pH 6: about 60% of maximum activity, pH 9: about 55% of maximum activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
cf. EC 2.2.1.6
UniProt
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
175000
-
gel filtration
33000
-
2 * 33000, A-subunit, + 2 * 39800, B-subunit, SDS-PAGE  
39800
-
2 * 33000, A-subunit, + 2 * 39800, B-subunit, SDS-PAGE  
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
-
2 * 33000, A-subunit, + 2 * 39800, B-subunit, SDS-PAGE  
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Q487A
mutation diminishes the decarboxylase activity but maintains the acetolactate synthase activity
Q487G
mutation diminishes only the decarboxylase activity but maintains the acetolactate synthase activity
Q487I
loss of acetolactate synthase activity, decrease in decarboxylase activity
Q487L
loss of acetolactate synthase activity, decrease in decarboxylase activity
Q487S
mutation diminishes only the decarboxylase activity but maintains the acetolactate synthase activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agriculture
-
plants with enzymic activity show enhanced cold tolerance, role as a protective mechanism for growth of plants under sub optimal temperatures
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Oku, H.; Kaneda, T.
Biosynthesis of branched-chain fatty acids in Bacillus subtilis. A decarboxylase is essential for branched-chain fatty acid synthetase
J. Biol. Chem.
263
18386-18396
1988
Bacillus subtilis
Manually annotated by BRENDA team
Wang-Pruski, G.; Szalay, A.A.
Transfer and expression of the genes of Bacillus branched chain alpha-oxo acid decarboxylase in Lycopersicum esculentum
Electron. J. Biotechnol.
5
141-153
2002
Bacillus subtilis
-
Manually annotated by BRENDA team
Atsumi, S.; Li, Z.; Liao, J.C.
Acetolactate synthase from Bacillus subtilis serves as a 2-ketoisovalerate decarboxylase for isobutanol biosynthesis in Escherichia coli
Appl. Environ. Microbiol.
75
6306-6311
2009
Bacillus subtilis (Q04789), Bacillus subtilis 168 (Q04789)
Manually annotated by BRENDA team