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Information on EC 2.6.1.42 - branched-chain-amino-acid transaminase and Organism(s) Arabidopsis thaliana

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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:
Arabidopsis thaliana
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Word Map
The taxonomic range for the selected organisms is: Arabidopsis thaliana
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
At1g50110
locus name
branched-chain amino acid aminotransferase
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branched-chain amino acid-glutamate transaminase
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branched-chain aminotransferase
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branched-chain aminotransferase4
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glutamate-branched-chain amino acid transaminase
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L-branched chain amino acid aminotransferase
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transaminase B
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amino group transfer
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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
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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-oxoglutarate + L-isoleucine
L-glutamate + 3-methyl-2-oxopentanoate
show the reaction diagram
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-
-
r
2-oxoglutarate + L-leucine
L-glutamate + 4-methyl-2-oxopentanoate
show the reaction diagram
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-
-
r
3-methyl-2-oxobutanoate + L-glutamate
L-valine + 2-oxoglutarate
show the reaction diagram
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-
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r
4-methylthio-2-oxobutanoate + L-glutamate
L-methionine + 2-oxoglutarate
show the reaction diagram
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-
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r
L-2-aminobutanoate + 4-methylthio-2-oxo-butanoate
2-oxobutanoate + L-methionine
show the reaction diagram
-
-
-
-
r
L-glutamate + 3-methyl-2-oxopentanoate
2-oxoglutarate + L-isoleucine
show the reaction diagram
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-
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r
L-glutamate + 4-methyl-2-oxopentanoate
2-oxoglutarate + L-leucine
show the reaction diagram
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-
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r
L-homomethionine + 2-oxoglutarate
5-methylthio-2-oxopentanoate + L-glutamate
show the reaction diagram
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-
-
-
?
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
show the reaction diagram
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-
-
-
?
L-methionine + 2-oxobutanoate
4-methylthio-2-oxobutanoate + L-2-aminobutanoate
show the reaction diagram
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-
-
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r
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
show the reaction diagram
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-
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-
?
L-methionine + 2-oxoglutarate
4-methylthio-2-oxobutanoate + L-glutamate
show the reaction diagram
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r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
show the reaction diagram
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r
additional information
?
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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
additional information
?
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enzyme may influence methionine levels and play an important role in the metabolism of the nonprotein amino acid alpha-aminobutanoate
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?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.69
3-methyl-2-oxobutanoate
pH 8.3, 337°C
1.08
3-methyl-2-oxopentanoate
pH 8.3, 337°C
2.64
4-methyl-2-oxopentanoate
pH 8.3, 337°C
0.045
4-methylsulfanyl-2-oxobutanoate
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2.83
4-methylthio-2-oxobutanoate
pH 8.3, 337°C
3.27
L-isoleucine
pH 8.3, 337°C
3.34 - 4.86
L-leucine
0.93 - 6.58
L-methionine
4.41
L-valine
pH 8.3, 337°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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predominant expression of isoform Atbcat-1
Manually annotated by BRENDA team
additional information
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isoforms Atbcat-1, Atbcat-3 are expressed in all tissues, isoforms Atbcat-4, Atbcat-6 mainly in tissues associated with transport function and meristematic tissues
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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isoforms Atbcat-4, Atbcat-6
Manually annotated by BRENDA team
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isoform Atbcat-1
Manually annotated by BRENDA team
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isoforms Atbcat-2, Atbcat-3, Atbcat-5
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
mutant plants lacking the activities of isoforms bcat3, Bcat4, Bcat6 exhibit a clear macroscopic phenotype with smaller plants and abnormal leaf morphology. The triple mutant shows a dramatic reduction of Met-derived glucosinolate species down to 32 and 14% of wild-type levels in plant foliage and seeds, respectively, accompanied by a 46fold increase of free Met. 5?-Deoxy-5?-methylthioadenosine, an intermediate of the Met recycling pathway, accumulates to relative high amounts in the absence of the cytosolic Bcat4 and Bcat6
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
BCAT1_ARATH
384
0
41934
Swiss-Prot
Mitochondrion (Reliability: 2)
BCAT2_ARATH
388
0
42591
Swiss-Prot
Mitochondrion (Reliability: 4)
BCAT3_ARATH
413
0
44972
Swiss-Prot
Chloroplast (Reliability: 2)
BCAT5_ARATH
415
0
45581
Swiss-Prot
Chloroplast (Reliability: 3)
BCAT6_ARATH
356
0
38861
Swiss-Prot
other Location (Reliability: 2)
A0A5S9XJH3_ARATH
413
0
44985
TrEMBL
Chloroplast (Reliability: 2)
A0A178WHD8_ARATH
384
0
41858
TrEMBL
Mitochondrion (Reliability: 2)
A0A178WMB7_ARATH
367
0
39999
TrEMBL
other Location (Reliability: 2)
Q0WQT2_ARATH
415
0
45581
TrEMBL
Chloroplast (Reliability: 3)
F4I2Q0_ARATH
309
0
33785
TrEMBL
Mitochondrion (Reliability: 2)
A0A1P8APA3_ARATH
469
1
52132
TrEMBL
other Location (Reliability: 2)
B9DHH5_ARATH
388
0
42591
TrEMBL
Mitochondrion (Reliability: 4)
A0A7G2DVN9_ARATH
1463
0
162079
TrEMBL
other Location (Reliability: 2)
A0A5S9WKZ4_ARATH
367
0
39984
TrEMBL
other Location (Reliability: 2)
A0A654FG91_ARATH
413
0
44972
TrEMBL
Chloroplast (Reliability: 2)
A0A1P8APE4_ARATH
373
1
41069
TrEMBL
Mitochondrion (Reliability: 2)
A0A1P8APB7_ARATH
405
0
44848
TrEMBL
other Location (Reliability: 2)
B9DFH1_ARATH
384
0
41934
TrEMBL
Mitochondrion (Reliability: 2)
A0A178WB05_ARATH
356
0
38861
TrEMBL
other Location (Reliability: 2)
A0A7G2E154_ARATH
358
0
39049
TrEMBL
other Location (Reliability: 2)
A0A1P8AMV4_ARATH
321
0
34931
TrEMBL
other Location (Reliability: 3)
Q0V7U6_ARATH
415
0
45577
TrEMBL
Chloroplast (Reliability: 3)
A0A7G2FJ30_ARATH
409
0
44872
TrEMBL
Chloroplast (Reliability: 3)
A0A7G2EV74_ARATH
396
0
43138
TrEMBL
Chloroplast (Reliability: 2)
A0A178WHC5_ARATH
142
0
15251
TrEMBL
other Location (Reliability: 4)
A0A384KYR5_ARATH
415
0
45581
TrEMBL
Chloroplast (Reliability: 3)
A0A654EIJ4_ARATH
367
0
40013
TrEMBL
other Location (Reliability: 2)
A0A5S9TK08_ARATH
1451
0
160715
TrEMBL
other Location (Reliability: 2)
A0A654E8C8_ARATH
388
0
42577
TrEMBL
Mitochondrion (Reliability: 4)
Q2V4P2_ARATH
318
0
34575
TrEMBL
other Location (Reliability: 1)
B3H658_ARATH
411
0
44731
TrEMBL
Chloroplast (Reliability: 2)
A0A1P8APA5_ARATH
480
0
52997
TrEMBL
other Location (Reliability: 2)
B3H7M6_ARATH
318
0
34420
TrEMBL
other Location (Reliability: 2)
A0A654EAD5_ARATH
360
0
39086
TrEMBL
other Location (Reliability: 2)
A0A5S9WNE0_ARATH
356
0
38833
TrEMBL
other Location (Reliability: 2)
Q0WUX7_ARATH
356
0
38859
TrEMBL
other Location (Reliability: 2)
A0A178W8L2_ARATH
388
0
42611
TrEMBL
Mitochondrion (Reliability: 5)
A0A178VH13_ARATH
413
0
44969
TrEMBL
Chloroplast (Reliability: 2)
BCAT4_ARATH
354
0
39019
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
51900
-
predicted mass
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
S-protein agarose chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Diebold, R.; Schuster, J.; Daeschner, K.; Binder, S.
The branched-chain amino acid transaminase gene family in Arabidopsis encodes plastid and mitochondrial proteins
Plant Physiol.
129
540-550
2002
Arabidopsis sp., Arabidopsis thaliana (Q93Y32), Arabidopsis thaliana (Q9FYA6), Arabidopsis thaliana (Q9LE06), Arabidopsis thaliana (Q9LPM9), Arabidopsis thaliana (Q9M401), Arabidopsis thaliana (Q9M439)
Manually annotated by BRENDA team
Schuster, J.; Binder, S.
The mitochondrial branched-chain aminotransferase (AtBCAT-1) is capable to initiate degradation of leucine, isoleucine and valine in almost all tissues in Arabidopsis thaliana
Plant Mol. Biol.
57
241-254
2005
Arabidopsis thaliana
Manually annotated by BRENDA team
Schuster, J.; Knill, T.; Reichelt, M.; Gershenzon, J.; Binder, S.
Branched-chain aminotransferase4 is part of the chain elongation pathway in the biosynthesis of methionine-derived glucosinolates in Arabidopsis
Plant Cell
18
2664-2679
2006
Arabidopsis thaliana
Manually annotated by BRENDA team
Laechler, K.; Imhof, J.; Reichelt, M.; Gershenzon, J.; Binder, S.
The cytosolic branched-chain aminotransferases of Arabidopsis thaliana influence methionine supply, salvage and glucosinolate metabolism
Plant Mol. Biol.
88
119-131
2015
Arabidopsis thaliana (Q9LPM9), Arabidopsis thaliana
Manually annotated by BRENDA team