Information on EC 2.6.1.42 - branched-chain-amino-acid transaminase and Organism(s) Homo sapiens

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Word Map on EC 2.6.1.42
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Homo sapiens


The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea


The taxonomic range for the selected organisms is: Homo sapiens

EC NUMBER
COMMENTARY hide
2.6.1.42
-
RECOMMENDED NAME
GeneOntology No.
branched-chain-amino-acid transaminase
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amino group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
L-alanine biosynthesis I
-
-
L-isoleucine biosynthesis I (from threonine)
-
-
L-isoleucine biosynthesis II
-
-
L-isoleucine biosynthesis III
-
-
L-isoleucine biosynthesis IV
-
-
L-isoleucine biosynthesis V
-
-
L-isoleucine degradation I
-
-
L-isoleucine degradation II
-
-
L-leucine biosynthesis
-
-
L-leucine degradation I
-
-
L-leucine degradation III
-
-
L-valine biosynthesis
-
-
L-valine degradation I
-
-
L-valine degradation II
-
-
leucine degradation IV
-
-
alanine metabolism
-
-
isoleucine metabolism
-
-
leucine metabolism
-
-
valine metabolism
-
-
Cysteine and methionine metabolism
-
-
Valine, leucine and isoleucine degradation
-
-
Valine, leucine and isoleucine biosynthesis
-
-
Pantothenate and CoA biosynthesis
-
-
Glucosinolate biosynthesis
-
-
Metabolic pathways
-
-
Biosynthesis of secondary metabolites
-
-
Biosynthesis of antibiotics
-
-
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
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
beta-chloro-L-alanine + ?
3-chloropyruvate + ?
show the reaction diagram
-
-
-
-
?
L-2-aminobutyrate + 2-oxoglutarate
2-oxobutanoate + L-glutamate
show the reaction diagram
-
-
-
-
r
L-2-aminobutyrate + 4-methyl-2-oxopentanoate
2-oxobutanoate + L-leucine
show the reaction diagram
-
-
-
-
r
L-alanine + 2-oxoglutarate
2-oxopropanoate + L-glutamate
show the reaction diagram
-
-
-
-
r
L-alanine + 4-methyl-2-oxopentanoate
pyruvate + L-leucine
show the reaction diagram
-
-
-
-
r
L-alanine + glyoxylate
pyruvate + glycine
show the reaction diagram
-
-
-
-
?
L-allo-isoleucine + 2-oxobutyrate
3-methyl-2-oxopentanoate + 2-aminobutyrate
show the reaction diagram
-
-
-
-
r
L-allo-isoleucine + 2-oxohexanoate
3-methyl-2-oxopentanoate + 2-aminohexanoate
show the reaction diagram
-
-
-
-
r
L-allo-isoleucine + 2-oxoisohexanoate
3-methyl-2-oxopentanoate + L-leucine
show the reaction diagram
-
-
-
-
r
L-allo-isoleucine + 2-oxoisopentanoate
3-methyl-2-oxopentanoate + L-valine
show the reaction diagram
-
-
-
-
r
L-allo-isoleucine + 2-oxooctanoate
3-methyl-2-oxopentanoate + 2-aminooctanoate
show the reaction diagram
-
-
-
-
r
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
-
r
L-glutamate + 2-oxoglutarate
2-oxoglutarate + L-glutamate
show the reaction diagram
L-glutamate + 4-methyl-2-oxopentanoate
2-oxoglutarate + L-leucine
show the reaction diagram
-
-
-
-
r
L-isoleucine + 2-oxo-isopentanoate
2-oxoisohexanoate + L-valine
show the reaction diagram
-
-
-
-
r
L-isoleucine + 2-oxobutyrate
2-oxoisohexanoate + 2-aminobutyrate
show the reaction diagram
-
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
show the reaction diagram
L-isoleucine + 2-oxohexanoate
L-norleucine + 2-oxoisohexanoate
show the reaction diagram
-
-
-
-
r
L-isoleucine + 2-oxoisohexanoate
3-methyl-2-oxopentanoate + L-leucine
show the reaction diagram
-
-
-
-
r
L-isoleucine + 2-oxooctanoate
2-oxoisohexanoate + 2-aminooctanoate
show the reaction diagram
-
-
-
-
r
L-leucine + 2-oxo-butyrate
2-oxoisohexanoate + 2-aminobutyrate
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-oxohexanoate
2-oxoisohexanoate + 2-aminohexanoate
show the reaction diagram
-
-
-
-
r
L-leucine + 2-oxoisohexanoate
2-oxoisohexanoate + L-leucine
show the reaction diagram
-
-
-
-
r
L-leucine + 2-oxooctanoate
2-oxoisohexanoate + 2-aminooctanoate
show the reaction diagram
-
-
-
-
r
L-leucine + 3-methyl-2-oxobutanoate
4-methyl-2-oxopentanoate + L-valine
show the reaction diagram
-
-
-
-
r
L-leucine + 3-methyl-2-oxopentanoate
2-oxo-4-methylpentanoate + L-isoleucine
show the reaction diagram
-
-
-
-
r
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 + p-hydroxyphenylpyruvate
2-oxoisohexanoate + L-tyrosine
show the reaction diagram
-
-
-
-
r
L-leucine + phenylpyruvate
2-oxoisohexanoate + L-phenylalanine
show the reaction diagram
-
-
-
-
r
L-leucine + pyruvate
2-oxoisohexanoate + L-alanine
show the reaction diagram
-
slight activity
-
-
r
L-norleucine + 4-methyl-2-oxopentanoate
2-oxohexanoate + L-leucine
show the reaction diagram
-
-
-
-
r
L-norvaline + 4-methyl-2-oxopentanoate
2-oxopentanoate + L-leucine
show the reaction diagram
L-valine + 2-oxobutyrate
2-oxoisopentanoate + 2-aminobutanoate
show the reaction diagram
-
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
show the reaction diagram
L-valine + 2-oxohexanoate
2-oxoisopentanoate + 2-aminohexanoate
show the reaction diagram
-
-
-
-
r
L-valine + 2-oxooctanoate
2-oxoisopentanoate + 2-aminooctanoate
show the reaction diagram
-
-
-
-
r
L-valine + 4-methyl-2-oxopentanoate
2-oxoisopentanoate + L-leucine
show the reaction diagram
-
-
-
-
r
S-(1,1,2,2-tetrafluoroethyl)-L-cysteine + ?
S-(1,1,2,2-tetrafluoroethyl)-2-oxo-3-thiobutyrate + ?
show the reaction diagram
-
-
-
-
?
S-(1,2-dichlorovinyl)-L-cysteine + ?
S-(1,2-dichlorovinyl)-2-oxo-3-thiobutyrate + ?
show the reaction diagram
-
-
-
-
?
S-(2-chloro-1,1,2-trifluoroethyl)-L-cysteine + ?
S-(2-chloro-1,1,2-trifluoroethyl)-2-oxo-3-thiobutyrate + ?
show the reaction diagram
-
-
-
-
?
additional information
?
-
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
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
show the reaction diagram
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-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
show the reaction diagram
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-oxoisocaproate
-
-
5-bromo-N'-(phenylsulfonyl)-1-benzofuran-2-carbohydrazide
-
IC50: 0.0025 mM
5-bromo-N'-(phenylsulfonyl)-1H-indole-2-carbohydrazide
-
IC50: 0.015 mM
5-chloro-N'-(phenylsulfonyl)-1-benzofuran-2-carbohydrazide
-
IC50: 0.0042 mM
5-chloro-N'-[(2-chlorophenyl)sulfonyl]-1-benzofuran-2-carbohydrazide
-
IC50: 0.0057 mM
5-chloro-N'-[(2-methylphenyl)sulfonyl]-1-benzofuran-2-carbohydrazide
-
IC50: 0.00116 mM
5-chloro-N'-[(3-methylphenyl)sulfonyl]-1-benzofuran-2-carbohydrazide
-
IC50: 0.0012 mM
5-chloro-N'-[[2-(trifluoromethyl)phenyl]sulfonyl]-1-benzofuran-2-carbohydrazide
-
IC50: 0.0008 mM, potent inhibitor
5-methoxy-N'-(phenylsulfonyl)-1-benzofuran-2-carbohydrazide
-
IC50: 0.0128 mM
5-methoxy-N'-(phenylsulfonyl)-1H-indole-2-carbohydrazide
-
IC50: 0.0568 mM
benzothiazolyl-L-cysteine
-
inhibits the L-leucine-2-oxoglutarate tranamination reaction of both isoenzymes
beta-chloro-L-alanine
-
rapidly inactivated by the beta-lyase substrate
gabapentin
hydrazine
-
-
hydroxylamine
-
-
N'-(phenylsulfonyl)-1-benzofuran-2-carbohydrazide
-
IC50: 0.0183 mM
N'-(phenylsulfonyl)-1H-indole-2-carbohydrazide
-
IC50: 0.036 mM
N'-(phenylsulfonyl)dibenzo[b,d]furan-2-carbohydrazide
-
IC50: 0.00235 mM
N'-(phenylsulfonyl)quinoline-3-carbohydrazide
-
IC50: 0.0333 mM
N'-(phenylsulfonyl)quinoline-6-carbohydrazide
-
IC50: 0.0133 mM
N'-[(2-chlorophenyl)sulfonyl]dibenzo[b,d]furan-2-carbohydrazide
-
IC50: 0.0129 mM
N'-[(2-methylphenyl)sulfonyl]dibenzo[b,d]furan-2-carbohydrazide
-
IC50: 0.0032 mM
N'-[(3-chlorophenyl)sulfonyl]dibenzo[b,d]furan-2-carbohydrazide
-
IC50: above 0.035 mM
N'-[(3-methylphenyl)sulfonyl]dibenzo[b,d]furan-2-carbohydrazide
-
IC50: 0.0028 mM
N'-[(4-chlorophenyl)sulfonyl]dibenzo[b,d]furan-2-carbohydrazide
-
IC50: 0.0372 mM
N'-[(4-methylphenyl)sulfonyl]dibenzo[b,d]furan-2-carbohydrazide
-
IC50: 0.051 mM
p-chloromercuribenzoate
-
isoenzyme I, complete inhibition, isoenzyme III only partially inhibited
S-(1,1,2,2-tetrafluoroethyl)-L-cysteine
-
rapidly inactivated by the beta-lyase substrate
S-(1,2-dichlorovinyl)-L-cysteine
-
rapidly inactivated by the beta-lyase substrate
S-(2-chloro-1,1,2-trifluoroethyl)-L-cysteine
-
rapidly inactivated by the beta-lyase substrate
Tris
-
-
additional information
-
not inhibited by isonicotinic acid and semicarbazide
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.06
(R)-3-methyl-2-oxopentanoate
-
pH 8.0, 25°C, substrate L-glutamate
0.09 - 0.17
(S)-3-methyl-2-oxopentanoate
35.8
2-aminobutyrate
-
pH 8.3, 37°C, 4-methyl-2-oxopentanoate as amino group acceptor
3.62
2-oxobutyrate
-
pH 8.3, 37°C, leucine as amino group donor
1 - 7.6
2-oxoglutarate
0.41
2-Oxohexanoate
-
pH 8.3, 37°C, leucine as amino group donor
0.21
2-Oxoisohexanoate
-
pH 8.3, 37°C, leucine as amino group donor
0.37
2-oxoisopentanoate
-
pH 8.3, 37°C, leucine as amino group donor
1.54
2-oxooctanoate
-
pH 8.3, 37°C, leucine as amino group donor
0.64
2-oxovalerate
-
pH 8.3, 37°C, L-leucine as amino group donor
0.61
3-methyl-2-oxobutanoate
-
pH 8.0, 25°C, substrate L-isoleucine
0.53
4-methyl-2-oxopentanoate
-
pH 8.0, 25°C, substrate L-isoleucine
0.6
beta-chloro-L-alanine
-
pH 7.4, 23°C, recombinant BCATm
0.11 - 0.26
glyoxylate
0.56
isoleucine
-
pH 8.4, 25°C, 2-oxoglutarate as amino group acceptor
35 - 74
L-alanine
1.54
L-alloisoleucine
-
pH 8.4, 25°C, 2-oxoglutarate as amino group acceptor
4.5 - 28.3
L-glutamate
3 - 10.3
L-isoleucine
0.62 - 25
L-leucine
2.96 - 30.8
L-valine
30.72
pyruvate
-
pH 8.3, 37°C, leucine as amino group donor
8.4
S-(1,1,2,2-tetrafluoroethyl)-L-cysteine
-
pH 7.4, 23°C, recombinant BCATm
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
250 - 360
2-oxoglutarate
16 - 42
glyoxylate
17 - 50
L-alanine
50.1 - 1157
L-glutamate
70.5 - 1075
L-isoleucine
60.8 - 898
L-leucine
170 - 1236
L-valine
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
31 - 126
L-glutamate
1118 - 3895
L-isoleucine
474 - 3151
L-leucine
89 - 1397
L-valine
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.3 - 389.2
gabapentin
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0025
5-bromo-N'-(phenylsulfonyl)-1-benzofuran-2-carbohydrazide
Homo sapiens
-
IC50: 0.0025 mM
0.015
5-bromo-N'-(phenylsulfonyl)-1H-indole-2-carbohydrazide
Homo sapiens
-
IC50: 0.015 mM
0.0042
5-chloro-N'-(phenylsulfonyl)-1-benzofuran-2-carbohydrazide
Homo sapiens
-
IC50: 0.0042 mM
0.0057
5-chloro-N'-[(2-chlorophenyl)sulfonyl]-1-benzofuran-2-carbohydrazide
Homo sapiens
-
IC50: 0.0057 mM
0.00116
5-chloro-N'-[(2-methylphenyl)sulfonyl]-1-benzofuran-2-carbohydrazide
Homo sapiens
-
IC50: 0.00116 mM
0.0012
5-chloro-N'-[(3-methylphenyl)sulfonyl]-1-benzofuran-2-carbohydrazide
Homo sapiens
-
IC50: 0.0012 mM
0.0008
5-chloro-N'-[[2-(trifluoromethyl)phenyl]sulfonyl]-1-benzofuran-2-carbohydrazide
Homo sapiens
-
IC50: 0.0008 mM, potent inhibitor
0.0128
5-methoxy-N'-(phenylsulfonyl)-1-benzofuran-2-carbohydrazide
Homo sapiens
-
IC50: 0.0128 mM
0.0568
5-methoxy-N'-(phenylsulfonyl)-1H-indole-2-carbohydrazide
Homo sapiens
-
IC50: 0.0568 mM
0.0183
N'-(phenylsulfonyl)-1-benzofuran-2-carbohydrazide
Homo sapiens
-
IC50: 0.0183 mM
0.036
N'-(phenylsulfonyl)-1H-indole-2-carbohydrazide
Homo sapiens
-
IC50: 0.036 mM
0.00235
N'-(phenylsulfonyl)dibenzo[b,d]furan-2-carbohydrazide
Homo sapiens
-
IC50: 0.00235 mM
0.0333
N'-(phenylsulfonyl)quinoline-3-carbohydrazide
Homo sapiens
-
IC50: 0.0333 mM
0.0133
N'-(phenylsulfonyl)quinoline-6-carbohydrazide
Homo sapiens
-
IC50: 0.0133 mM
0.0129
N'-[(2-chlorophenyl)sulfonyl]dibenzo[b,d]furan-2-carbohydrazide
Homo sapiens
-
IC50: 0.0129 mM
0.0032
N'-[(2-methylphenyl)sulfonyl]dibenzo[b,d]furan-2-carbohydrazide
Homo sapiens
-
IC50: 0.0032 mM
0.035
N'-[(3-chlorophenyl)sulfonyl]dibenzo[b,d]furan-2-carbohydrazide
Homo sapiens
-
IC50: above 0.035 mM
0.0028
N'-[(3-methylphenyl)sulfonyl]dibenzo[b,d]furan-2-carbohydrazide
Homo sapiens
-
IC50: 0.0028 mM
0.0372
N'-[(4-chlorophenyl)sulfonyl]dibenzo[b,d]furan-2-carbohydrazide
Homo sapiens
-
IC50: 0.0372 mM
0.051
N'-[(4-methylphenyl)sulfonyl]dibenzo[b,d]furan-2-carbohydrazide
Homo sapiens
-
IC50: 0.051 mM
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
85
-
recombinant cytosolic enzyme
125
-
recombinant mitochondrial enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
-
isoenzyme III
9
-
isoenzyme I
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 10
-
-
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
cytosolic enzyme form
Manually annotated by BRENDA team
-
cell lines derived from Diamond-Blackfan anemia patients
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
recombinant enzyme, expressed in transfected cells
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
41730
-
2 * 41730, recombinant BCATm, homodimer
43400
-
2 * 43400, recombinant BCATc, homodimer
80000
-
isoenzyme I, gel filtration
90000
-
isoenzyme III, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
-
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
BCATm, orthorhombic space group P2(1)2(1)2(1), monoclinic P2(1), trigonal P3(2)
-
cytosolic isoform in complex with gabapentin or 4-methylvalerate, mitochondrial isoform in complex with gabapentin
hanging drop vapour diffusion method using 22-30% polyethlylene glycol 1500, 100 mM HEPES (pH 6.9-7.2), and 20 mM dithiothreitol
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
65
-
not inactivated by heating for 10 min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
2-mercaptoethanol protects against inactivation by sulfhydryl reagents
-
on the basis of 5,5'-dithiobis(2-nitrobenzoic acid) titration of wild type BCATc, labeling of 6 thiol groups results in a loss of 60-70% of BCAT activity compared to that of the control enzyme incubated without 5,5'-dithiobis(2-nitrobenzoic acid) and assayed without dithiothreitol
-
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
the activity of oxidized BCAT with 0.5 mM hydrogen peroxide for 2 h at 25°C shows 99.5% inhibition
-
674728
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
immobilized metal ion affinity chromatography (Ni2+), anion-exchange chromatography (removal of the His-tag after cleavage)
-
Ni-NTA acid resin column chromatography
-
Ni-NTA resin column chromatography and Mono-Q HR 5/5 column chromatography
-
recombinant Bcatm and BCATc, expressed in E. coli
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; isoform of BCATm, cloned using a yeast two-hybrid system, expressed in transfected monkey kidney CV1 cells
expressed in Escherichia coli BL21 (DE3) cells
-
His-tagged protein expressed in Escherichia coli BL21-DE3
-
recombinant BCATm and BCATc
-
vector pET-28a, overexpression of recombinant BCATm and BCATc in Escherichia coli
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C221S
-
the mutant shows strongly decreased kcat values compared to the wild type enzyme
C235S
-
the mutant enzyme exhibits kcat values that are within 20-30% of wild type BCATc values, but also have lower Km values, hence higher calculated kcat/Km values than those of the wild type enzyme
C242S
-
the mutant shows strongly decreased kcat values compared to the wild type enzyme
C293S
-
the C293S mutant and wild type BCATc have similar kinetic constants with L-valine, L-leucine, and L-glutamate
C315A
-
contains changes in the structure of the beta-turn preceding the CXXC motif when compared with wild type protein, the oxidized mutant enzyme shows limited activity
C315A/C318A
-
contains changes in the structure of the beta-turn preceding the CXXC motif when compared with wild type protein, the oxidized mutant enzyme shows limited activity
C318A
-
contains changes in the structure of the beta-turn preceding the CXXC motif when compared with wild type protein, the oxidized mutant enzyme shows limited activity
C335S
-
for all amino acid substrates, there is a significant decrease (70% to 80%) in kcat with the C335S mutant, the Km value for glutamate with the C335S mutant enzyme is approximately 3fold lower than that observed with wild type enzyme
C335S/C3388S
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the mutant shows kcat values that are similar to values observed with the single C335 mutant enzymes, Km values are largely unchanged compared to those of wild type BCATc, kcat/Km values are significantly lower than wild type values
C338S
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the mutant enzyme exhibits kcat values for the BCAAs that were 50% lower than that observed with wild type enzyme. With the exception of L-glutamate, where the Km value is not changed and L-valine, where the Km value is 50% lower than the value for wild type BCATc, Km values for L-isoleucine and L-leucine are largely unaffected for the C338S mutant
E264K
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heterogeneous BCAT2 gene mutation, in combination heterogeneous BCAT2 gene mutation R170Q, found in a 25-year-old patient presenting with headache complaints and mild memory impairment for about six years
R170Q
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heterogeneous BCAT2 gene mutation, in combination heterogeneous BCAT2 gene mutation E264K, found in a 25-year-old patient presenting with headache complaints and mild memory impairment for about six years
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine