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Information on EC 2.6.1.42 - branched-chain-amino-acid transaminase and Organism(s) Pseudomonas aeruginosa

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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:
Pseudomonas aeruginosa
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The taxonomic range for the selected organisms is: Pseudomonas aeruginosa
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 aminotransferase
branched-chain amino acid-glutamate transaminase
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branched-chain aminotransferase
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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
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-leucine + 2-oxoglutarate = 4-methyl-2-oxopentanoate + L-glutamate
show the reaction diagram
reaction mechanism of aminotransferases via external aldimine, quinonoid intermediate, ketimine, and carbinolamine, overview
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-oxovalerate + L-glutamate
norvaline + 2-oxoglutarate
show the reaction diagram
-
-
-
r
3-methyl-2-oxobutanoate + L-glutamate
L-valine + 2-oxoglutarate
show the reaction diagram
-
-
-
r
3-methyl-2-oxopentanoate + L-glutamate
L-isoleucine + 2-oxoglutarate
show the reaction diagram
-
-
-
r
4-methyl-2-oxopentanoate + L-glutamate
L-leucine + 2-oxoglutarate
show the reaction diagram
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
show the reaction diagram
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
show the reaction diagram
high activity
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-
r
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
show the reaction diagram
-
-
-
r
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
show the reaction diagram
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
show the reaction diagram
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-
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r
norvaline + 2-oxoglutarate
2-oxovalerate + L-glutamate
show the reaction diagram
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r
additional information
?
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the substrate preference of 2-oxoacids is specific for 2-oxoglutarate, and for amino acids it is L-Leu > L-Ile > L-Val > L-norVal > L-Met > L-Phe. No activity with L-alanine, L-aspartate, L-glycine, L-serine, L-threonine, L-tryptophan, and L-tyrosine
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
PLP, dependent on
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.4
2-oxoglutarate
pH 8.0, 37°C
1
2-oxovalerate
pH 8.0, 37°C
1.2
3-methyl-2-oxopentanoate
pH 8.0, 37°C
18
L-glutamate
pH 8.0, 37°C
1
L-leucine
pH 8.0, 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
90
pH 8.0, 37°C, substrate L-leucine
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
branched-chain amino acid aminotransferases (BCATs) differ from other (S)-selective transaminases (TAs) in 3D-structure and organization of the PLP-binding domain. Unlike other (S)-selective TAs, BCATs belong to the PLP fold type IV and are characterized by the proton transfer on the re-face of PLP, in contrast to the si-specificity of proton transfer in fold type I (S)-selective TAs. Moreover, BCATs are the only (S)-selective enzymes within fold type IV TAs. Dual substrate recognition in BCATs is implemented via the lock and key mechanism without side-chain rearrangements of the active site residues. Another feature of the active site organization in BCATs is the binding of the substrate alpha-COOH group on the P-side of the active site near the PLP phosphate group. Close localization of two charged groups seems to increase the effectiveness of external aldimine formation in BCAT catalysis
metabolism
BCAT are the key enzymes of BCAA metabolism in all organisms
physiological function
branched-chain amino acid aminotransferases (BCATs) catalyze reversible stereoselective transamination of branched-chain amino acids (BCAAs) L-leucine, L-isoleucine, and L-valine. The catalysis proceeds through the ping-pong mechanism with the assistance of the cofactor pyridoxal 5'-phosphate (PLP)
additional information
structure-function analysis and substrate specificity, comparisons, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
A0A431X9Y9_PSEAI
307
0
34086
TrEMBL
-
A0A8G3ASJ0_PSEAI
307
0
34066
TrEMBL
-
A0A8G3BH79_PSEAI
307
0
34113
TrEMBL
-
A0A444M7G5_PSEAI
307
0
34055
TrEMBL
-
A0A2R3J1B2_PSEAI
307
0
34116
TrEMBL
-
A0A069Q145_PSEAI
307
0
34085
TrEMBL
-
A0A8G5UZ31_PSEAI
307
0
34025
TrEMBL
-
A0A8G2RR04_PSEAI
325
0
35673
TrEMBL
-
A0A8G6GY88_PSEAI
307
0
34058
TrEMBL
-
A0A8G4IYT3_PSEAI
307
0
34027
TrEMBL
-
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotetramer
4 * 34000, SDS-PAGE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bezsudnova, E.Y.; Boyko, K.M.; Popov, V.O.
Properties of bacterial and archaeal branched-chain amino acid aminotransferases
Biochemistry (Moscow)
82
1572-1591
2017
Brevibacillus brevis (A0A2Z4MEX9), Escherichia coli (P0AB80), Gluconobacter oxydans (Q5FTR3), Gluconobacter oxydans 621H (Q5FTR3), Helicobacter pylori (O26004), Helicobacter pylori 26695 (O26004), Helicobacter pylori ATCC 700392 (O26004), Lacticaseibacillus paracasei (A0A5Q8BPF5), Lactococcus lactis, Methanococcus aeolicus (A6UWA0), Methanococcus aeolicus ATCC BAA-1280 (A6UWA0), Methanococcus aeolicus DSM 17508 (A6UWA0), Methanococcus aeolicus Nankai-3 (A6UWA0), Methanococcus aeolicus OCM 812 (A6UWA0), Mycobacterium tuberculosis (P9WQ75), Mycobacterium tuberculosis ATCC 25618 (P9WQ75), Mycobacterium tuberculosis H37Rv (P9WQ75), Pseudomonas aeruginosa (O86428), Pseudomonas aeruginosa 1C (O86428), Pseudomonas aeruginosa ATCC 15692 (O86428), Pseudomonas aeruginosa CIP 104116 (O86428), Pseudomonas aeruginosa DSM 22644 (O86428), Pseudomonas aeruginosa JCM 14847 (O86428), Pseudomonas aeruginosa LMG 12228 (O86428), Pseudomonas aeruginosa PRS 101 (O86428), Pseudomonas sp., Thermococcus sp. CKU-1, Thermoproteus uzoniensis (F2L0W0), Thermoproteus uzoniensis 768-20 (F2L0W0), Vulcanisaeta moutnovskia (F0QW25), Vulcanisaeta moutnovskia 768-28 (F0QW25)
Manually annotated by BRENDA team