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Information on EC 2.6.1.42 - branched-chain-amino-acid transaminase and Organism(s) Rattus norvegicus

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EC Tree
     2 Transferases
         2.6 Transferring nitrogenous groups
             2.6.1 Transaminases
                2.6.1.42 branched-chain-amino-acid transaminase
IUBMB Comments
Also acts on L-isoleucine and L-valine, and thereby differs from EC 2.6.1.6, leucine transaminase, which does not. It also differs from EC 2.6.1.66, valine---pyruvate transaminase.
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This record set is specific for:
Rattus norvegicus
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The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
bcat1, bcatm, branched-chain aminotransferase, bcatc, bcat2, branched-chain amino acid aminotransferase, branched chain aminotransferase, hbcat, hbcatm, branched-chain amino acid transaminase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
branched chain amino acid: 2-oxoglutarate aminotransferase EC 2.6.1
-
formerly
branched chain aminotransferase
-
-
branched-chain amino acid aminotransferase
-
-
-
-
branched-chain amino acid-glutamate transaminase
-
-
-
-
branched-chain aminotransferase
glutamate-branched-chain amino acid transaminase
-
-
-
-
L-branched chain amino acid aminotransferase
-
-
-
-
transaminase B
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amino group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
branched-chain-amino-acid:2-oxoglutarate aminotransferase
Also acts on L-isoleucine and L-valine, and thereby differs from EC 2.6.1.6, leucine transaminase, which does not. It also differs from EC 2.6.1.66, valine---pyruvate transaminase.
CAS REGISTRY NUMBER
COMMENTARY hide
9054-65-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-allo-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
show the reaction diagram
-
-
-
-
r
L-glutamate + 2-oxoglutarate
2-oxoglutarate + L-glutamate
show the reaction diagram
-
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
show the reaction diagram
L-leucine + 2-oxo-3-methiobutyrate
2-oxoisohexanoate + L-methionine
show the reaction diagram
-
-
-
-
r
L-leucine + 2-oxo-butyrate
2-oxoisohexanoate + 2-aminobutyrate
show the reaction diagram
-
-
-
-
r
L-leucine + 2-oxo-hexanoate
2-oxoisohexanoate + 2-aminohexanoate
show the reaction diagram
-
-
-
-
r
L-leucine + 2-oxo-pentanoate
2-oxoisohexanoate + 2-aminopentanoate
show the reaction diagram
-
-
-
-
r
L-leucine + 2-oxoglutarate
2-oxoisohexanoate + L-glutamate
show the reaction diagram
-
-
-
-
?
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
show the reaction diagram
L-leucine + 2-oxoisohexanoate
2-oxoisohexanoate + L-leucine
show the reaction diagram
-
-
-
-
r
L-leucine + 2-oxoisopentanoate
2-oxoisohexanoate + L-valine
show the reaction diagram
-
-
-
-
r
L-leucine + 3-methyl-2-oxobutanoate
4-methyl-2-oxopentanoate + L-valine
show the reaction diagram
-
-
-
-
?
L-leucine + 3-methyl-2-oxopentanoate
4-methyl-2-oxopentanoate + L-isoleucine
show the reaction diagram
-
-
-
-
r
L-leucine + 4-methyl-2-oxopentanoate
4-methyl-2-oxopentanoate + L-leucine
show the reaction diagram
-
-
-
-
r
L-leucine + DL-2-oxo-3-methylpentanoate
2-oxoisohexanoate + L-isoleucine
show the reaction diagram
-
-
-
-
r
L-leucine + phenylpyruvate
2-oxoisohexanoate + L-phenylalanine
show the reaction diagram
-
2-oxo-isohexanoic acid 100%, BCATm relative rate 4%, BCATc 6%
-
-
r
L-leucine + pyruvate
2-oxoisohexanoate + L-alanine
show the reaction diagram
-
2-oxo-isohexanoic acid 100%, BCATm and BCATc, relative rate 6%
-
-
r
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
show the reaction diagram
L-norleucine + 2-oxoglutarate
2-oxohexanoate + L-glutamate
show the reaction diagram
-
-
-
-
r
L-norvaline + 2-oxoglutarate
2-oxopentanoate + L-glutamate
show the reaction diagram
-
-
-
-
r
L-threo-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
show the reaction diagram
-
-
-
-
r
L-valine + 2-oxoglutarate
2-oxoisopentanoate + L-glutamate
show the reaction diagram
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
show the reaction diagram
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
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
show the reaction diagram
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
show the reaction diagram
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
show the reaction diagram
additional information
?
-
-
specific for L-leucine, L-isoleucine or L-valine, no other amino acid would serve as an amino donor
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-methyl-2-oxopentanoate
-
-
Aminooxyacetate
-
-
diethyldicarbonate
-
-
gabapentin
-
structural analogue of leucine, competitive inhibitor of BCATc, does not inhibit BCATm
hydrazine
-
-
hydroxylamine
-
-
Mersalyl
-
-
N-ethylmaleimide
-
-
p-chloromercuribenzoate
additional information
-
no inhibition with isonicotinic acid hydrazide or KCN
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.07
(R,S)-3-methyl-2-oxopentanoate
-
pH 8.3, 25°C
0.68 - 14.2
2-oxoglutarate
0.11
3-methyl-2-oxobutanoate
-
pH 8.3, 25°C
0.14
4-methyl-2-oxopentanoate
-
pH 8.3, 25°C
2.45 - 6.65
L-glutamate
0.84 - 22.2
L-isoleucine
0.3 - 11.1
L-leucine
2.1 - 143
L-valine
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.1
4-methyl-2-oxopentanoate
-
pH 8.3, 25°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
18.6
-
mitochondria of AS-30D cell, pH 7.8, 37°C
7
-
regenerating liver, pH 7.8, 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
hepatoma cell, expresses only mitochondrial isoform
Manually annotated by BRENDA team
-
mitochondrial isoform, secretory epithelia throughout digestive tract, cytosolic isoform, autonomic innervation of digestive tract
Manually annotated by BRENDA team
-
cytosolic isoform, axons of sciatic nerve
Manually annotated by BRENDA team
-
mitochondrial isoform, secretory cells of
Manually annotated by BRENDA team
-
mitochondrial isoform, secretory cells of
Manually annotated by BRENDA team
additional information
-
no overlap in distribution of mitochndrial and cytosolic isoform, mitochondrial isoform is not found in liver
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
granule cells of the cerebellar cortex and dentate gyrus
Manually annotated by BRENDA team
-
of Purkinje cells and hippocampal pyramidal basket cells
Manually annotated by BRENDA team
-
granule cells of the cerebellar cortex and dentate gyrus
-
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
BCAT1_RAT
411
0
46046
Swiss-Prot
other Location (Reliability: 4)
BCAT2_RAT
393
0
44276
Swiss-Prot
Mitochondrion (Reliability: 3)
Q9R170_RAT
362
0
40822
TrEMBL
other Location (Reliability: 2)
A0A8I5ZVC5_RAT
428
0
48054
TrEMBL
Mitochondrion (Reliability: 4)
G3V8U8_RAT
393
0
44229
TrEMBL
Mitochondrion (Reliability: 3)
A0A8I6A0J2_RAT
460
0
51206
TrEMBL
Mitochondrion (Reliability: 2)
A0A8I6AKN8_RAT
401
0
44936
TrEMBL
Mitochondrion (Reliability: 3)
Q6P784_RAT
388
0
43596
TrEMBL
Mitochondrion (Reliability: 3)
Q99JD5_RAT
399
0
44770
TrEMBL
other Location (Reliability: 1)
A0A8I6AKH8_RAT
375
0
42166
TrEMBL
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35000
-
2 * 35000, SDS-PAGE
41000
41200
-
predicted from amino acid sequence
43000
47000
-
1 * 47000, BCATm, SDS-PAGE
50000
-
gel filtration
68000
-
gel filtration
79000
-
sucrose density gradient centrifugation
91000
-
BCATc, gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 41000, SDS-PAGE
dimer
monomer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
enzyme activity is associated with an immunoreactive band of 41000 Da, and an immunoreactive band of 43000 Da corresponds to inactive enzyme
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50 - 65
-
labile to heat, activity is completely lost by heating at 65°C for 1 min, about 30% is lost within 1 min at 50°C and about 70% within 10 min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
2-mercaptoethanol protects against inactivation by sulfhydryl reagents
-
not stable to freezing without addition of dithiothreitol
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70°C, when stored in presence of dithiothreitol activity is stable for at least 4 weeks
-
4°C,stable for several weeks without addition of dithiothreitol
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
mitochondrial and cytosolic isoenzymes
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in transgenic Mus musculus expressing the brain-derived neurotrophic factor cDNA under the control of the alpha-calcium/calmodulin-dependent kinase II promoter
-
RT/PCR of BCATm cDNA
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ichihara, A.; Koyama, E.
Transaminase of branched chain amino acids. I. Branched chain amino acids-alpha-ketoglutarate transaminase
J. Biochem.
59
160-169
1966
Rattus norvegicus, Sus scrofa
Manually annotated by BRENDA team
Aki, K.; Ogawa, K.; Ichihara, A.
Transaminases of branched chain amino acids. IV. Purification and properties of two enzymes from rat liver
Biochim. Biophys. Acta
159
276-284
1968
Rattus norvegicus, Sus scrofa
Manually annotated by BRENDA team
Cooper, A.J.L.
Glutamate-branched-chain amino acid transaminase
Methods Enzymol.
113
71-73
1985
Rattus norvegicus, Sus scrofa
Manually annotated by BRENDA team
Kido, R.
Pancreatic branched-chain-amino-acid aminotransferase
Methods Enzymol.
166
275-281
1988
Canis lupus familiaris, Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Korpela, T.K.
Purification of branched-chain-amino-acid aminotransferase from pig heart
Methods Enzymol.
166
269-274
1988
Rattus norvegicus, Sus scrofa
Manually annotated by BRENDA team
Wallin, R.; Hall, T.R.; Hutson, S.M.
Purification of branched chain aminotransferase from rat heart mitochondria
J. Biol. Chem.
265
6019-6024
1990
Rattus norvegicus, Rattus norvegicus Sprague-Dawley
Manually annotated by BRENDA team
Hall, T.R.; Wallin, R.; Reinhart, G.D.; Hutson, S.M.
Branched chain aminotransferase isoenzymes. Purification and characterization of the rat brain isoenzyme
J. Biol. Chem.
268
3092-3098
1993
Rattus norvegicus
Manually annotated by BRENDA team
Schadewaldt, P.; Adelmeyer, F.
Coupled enzymatic assay for estimation of branched-chain L-amino acid aminotransferase activity with 2-Oxo acid substrates
Anal. Biochem.
238
65-71
1996
Bos taurus, Rattus norvegicus
Manually annotated by BRENDA team
Hutson, S.M.; Berkich, D.; Drown, P.; Xu, B.; Aschner, M.; LaNoue, K.F.
Role of branched-chain aminotransferase isoenzymes and gabapentin in neurotransmitter metabolism
J. Neurochem.
71
863-874
1998
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Conway, M.E.; Hutson, S.M.
Mammalian branched-chain aminotransferases
Methods Enzymol.
324
355-365
2000
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Schadewaldt, P.
Determination of branched-chain L-amino-acid aminotransferase activity
Methods Enzymol.
324
23-32
2000
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Torres, N.; Vargas, C.; Hernandez-Pando, R.; Orozco, H.; Hutson, S.M.; Tovar, A.R.
Ontogeny and subcellular localization of rat liver mitochondrial branched chain amino-acid aminotransferase
Eur. J. Biochem.
268
6132-6139
2001
Rattus norvegicus
Manually annotated by BRENDA team
Cooper, A.J.; Conway, M.; Hutson, S.M.
A continuous 96-well plate spectrophotometric assay for branched-chain amino acid aminotransferases
Anal. Biochem.
308
100-105
2002
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Goto, M.; Miyahara, I.; Hayashi, H.; Kagamiyama, H.; Hirotsu, K.
Crystal structures of branched-chain amino acid aminotransferase complexed with glutamate and glutarate: True reaction intermediate and double substrate recognition of the enzyme
Biochemistry
42
3725-3733
2003
Rattus norvegicus, Escherichia coli (P0AB80), Escherichia coli
Manually annotated by BRENDA team
Sweatt, A.J.; Wood, M.; Suryawan, A.; Wallin, R.; Willingham, M.C.; Hutson, S.M.
Branched-chain amino acid catabolism: unique segregation of pathway enzymes in organ systems and peripheral nerves
Am. J. Physiol.
286
E64-76
2004
Rattus norvegicus
Manually annotated by BRENDA team
Sweatt, A.J.; Garcia-Espinosa, M.A.; Wallin, R.; Hutson, S.M.
Branched-chain amino acids and neurotransmitter metabolism: expression of cytosolic branched-chain aminotransferase (BCATc) in the cerebellum and hippocampus
J. Comp. Neurol.
477
360-370
2004
Rattus norvegicus
Manually annotated by BRENDA team
Perez-Villasenor, G.; Tovar, A.R.; Moranchel, A.H.; Hernandez-Pando, R.; Hutson, S.M.; Torres, N.
Mitochondrial branched chain aminotransferase gene expression in AS-30D hepatoma rat cells and during liver regeneration after partial hepatectomy in rat
Life Sci.
78
334-339
2005
Rattus norvegicus
Manually annotated by BRENDA team
Castellano, S.; Macchi, F.; Scali, M.; Huang, J.Z.; Bozzi, Y.
Cytosolic branched chain aminotransferase (BCATc) mRNA is up-regulated in restricted brain areas of BDNF transgenic mice
Brain Res.
1108
12-18
2006
Rattus norvegicus
Manually annotated by BRENDA team
Garcia-Espinosa, M.A.; Wallin, R.; Hutson, S.M.; Sweatt, A.J.
Widespread neuronal expression of branched-chain aminotransferase in the CNS: implications for leucine/glutamate metabolism and for signaling by amino acids
J. Neurochem.
100
1458-1468
2007
Rattus norvegicus
Manually annotated by BRENDA team