Information on EC 2.7.2.14 - branched-chain-fatty-acid kinase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.7.2.14
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RECOMMENDED NAME
GeneOntology No.
branched-chain-fatty-acid kinase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + 2-methylpropanoate = ADP + 2-methylpropanoyl phosphate
show the reaction diagram
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
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-
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SYSTEMATIC NAME
IUBMB Comments
ATP:branched-chain-fatty-acid 1-phosphotransferase
3-Methylbutanoate, 2-methylbutanoate, pentanoate, butanoate and propanoate can also act as acceptors (cf. EC 2.7.2.7 butyrate kinase).
CAS REGISTRY NUMBER
COMMENTARY hide
84177-54-8
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MA-2
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Manually annotated by BRENDA team
MA-2
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + 2-methylbutanoate
ADP + 2-methylbutanoyl phosphate
show the reaction diagram
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-
-
?
ATP + butanoate
ADP + butanoyl phosphate
show the reaction diagram
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-
-
-
?
ATP + isobutanoate
ADP + isobutanoyl phosphate
show the reaction diagram
ATP + isopentanoate
ADP + isopentanoyl phosphate
show the reaction diagram
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-
-
-
?
ATP + pentanoate
ADP + pentanoyl phosphate
show the reaction diagram
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-
-
-
?
ATP + propionate
ADP + propanoyl phosphate
show the reaction diagram
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-
-
-
?
CTP + isobutanoate
CDP + isobutanoyl phosphate
show the reaction diagram
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103% of the activity with ATP
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-
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GTP + isobutanoate
GDP + isobutanoyl phosphate
show the reaction diagram
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70% of the activity with ATP
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-
?
ITP + isobutanoate
IDP + isobutanoyl phosphate
show the reaction diagram
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68% of the activity with ATP
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-
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additional information
?
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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
additional information
?
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involved in catabolism of branched-chain amino acids
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
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65% of the activity with Mn2+
Cu2+
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58% of the activity with Mn2+
Mg2+
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96% of the activity with Mn2+
Mn2+
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divalent cation required, highest activity with Mn2+
Zn2+
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42% of the activity with Mn2+
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
10.8
2-methylbutyrate
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pH 7.5, 30C
1.8
ATP
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pH 7.5, 30C
16.9
Butyrate
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pH 7.5, 30C
4.3
Isobutyrate
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pH 7.5, 30C
9.5
Isovalerate
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pH 7.5, 30C
14.3
Propionate
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pH 7.5, 30C
12.5
valerate
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pH 7.5, 30C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
12
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pH 8.3, 50C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.3
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assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 8.5
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more than 80% of maximal activity at pH 6.0 and 8.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
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assay at
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
76000
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gel filtration
380000
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dynamic light scattering
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
octamer
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crystallization data, 8 * 43000, calculated for recombinant protein with His6-tag
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant protein with His6-tag
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45
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30 min, 25% loss of activity
60
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30 min, complete loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
complete loss of activity if filtered through columns of Sephacryl S-300 at room temperature
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dialysis, 6 h at 5C, significant loss of activity
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-50C, crude cell extract stable for 2 months
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