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L-glutamate + 2-oxoglutarate
2-oxoglutarate + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
beta-chloro-L-alanine + ?
3-chloropyruvate + ?
-
-
-
-
?
L-2-aminobutyrate + 2-oxoglutarate
2-oxobutanoate + L-glutamate
-
-
-
-
r
L-2-aminobutyrate + 4-methyl-2-oxopentanoate
2-oxobutanoate + L-leucine
-
-
-
-
r
L-alanine + 2-oxoglutarate
2-oxopropanoate + L-glutamate
-
-
-
-
r
L-alanine + 4-methyl-2-oxopentanoate
pyruvate + L-leucine
-
-
-
-
r
L-alanine + glyoxylate
pyruvate + glycine
-
-
-
-
?
L-allo-isoleucine + 2-oxobutyrate
3-methyl-2-oxopentanoate + 2-aminobutyrate
-
-
-
-
r
L-allo-isoleucine + 2-oxohexanoate
3-methyl-2-oxopentanoate + 2-aminohexanoate
-
-
-
-
r
L-allo-isoleucine + 2-oxoisohexanoate
3-methyl-2-oxopentanoate + L-leucine
-
-
-
-
r
L-allo-isoleucine + 2-oxoisopentanoate
3-methyl-2-oxopentanoate + L-valine
-
-
-
-
r
L-allo-isoleucine + 2-oxooctanoate
3-methyl-2-oxopentanoate + 2-aminooctanoate
-
-
-
-
r
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
-
-
-
r
L-glutamate + (R)-3-methyl-2-oxopentanoate
L-isoleucine + 2-oxoglutarate
-
-
-
-
?
L-glutamate + (S)-3-methyl-2-oxopentanoate
L-isoleucine + 2-oxoglutarate
-
-
-
-
?
L-glutamate + 2-oxoglutarate
2-oxoglutarate + L-glutamate
-
-
-
-
r
L-glutamate + 4-methyl-2-oxopentanoate
2-oxoglutarate + L-leucine
-
-
-
-
r
L-isoleucine + 2-oxo-isopentanoate
2-oxoisohexanoate + L-valine
-
-
-
-
r
L-isoleucine + 2-oxobutyrate
2-oxoisohexanoate + 2-aminobutyrate
-
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
L-isoleucine + 2-oxohexanoate
L-norleucine + 2-oxoisohexanoate
-
-
-
-
r
L-isoleucine + 2-oxoisohexanoate
3-methyl-2-oxopentanoate + L-leucine
-
-
-
-
r
L-isoleucine + 2-oxooctanoate
2-oxoisohexanoate + 2-aminooctanoate
-
-
-
-
r
L-leucine + 2-oxo-butyrate
2-oxoisohexanoate + 2-aminobutyrate
-
-
-
-
r
L-leucine + 2-oxoglutarate
2-oxoisohexanoate + L-glutamate
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
L-leucine + 2-oxohexanoate
2-oxoisohexanoate + 2-aminohexanoate
-
-
-
-
r
L-leucine + 2-oxoisohexanoate
2-oxoisohexanoate + L-leucine
-
-
-
-
r
L-leucine + 2-oxooctanoate
2-oxoisohexanoate + 2-aminooctanoate
-
-
-
-
r
L-leucine + 3-methyl-2-oxobutanoate
4-methyl-2-oxopentanoate + L-valine
-
-
-
-
r
L-leucine + 3-methyl-2-oxopentanoate
2-oxo-4-methylpentanoate + L-isoleucine
-
-
-
-
r
L-leucine + 3-methyl-2-oxopentanoate
4-methyl-2-oxopentanoate + L-isoleucine
-
-
-
-
r
L-leucine + 4-methyl-2-oxopentanoate
4-methyl-2-oxopentanoate + L-leucine
-
-
-
-
r
L-leucine + p-hydroxyphenylpyruvate
2-oxoisohexanoate + L-tyrosine
-
-
-
-
r
L-leucine + phenylpyruvate
2-oxoisohexanoate + L-phenylalanine
-
-
-
-
r
L-leucine + pyruvate
2-oxoisohexanoate + L-alanine
-
slight activity
-
-
r
L-norleucine + 4-methyl-2-oxopentanoate
2-oxohexanoate + L-leucine
-
-
-
-
r
L-norvaline + 4-methyl-2-oxopentanoate
2-oxopentanoate + L-leucine
L-valine + 2-oxobutyrate
2-oxoisopentanoate + 2-aminobutanoate
-
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
L-valine + 2-oxohexanoate
2-oxoisopentanoate + 2-aminohexanoate
-
-
-
-
r
L-valine + 2-oxooctanoate
2-oxoisopentanoate + 2-aminooctanoate
-
-
-
-
r
L-valine + 4-methyl-2-oxopentanoate
2-oxoisopentanoate + L-leucine
-
-
-
-
r
S-(1,1,2,2-tetrafluoroethyl)-L-cysteine + ?
S-(1,1,2,2-tetrafluoroethyl)-2-oxo-3-thiopropanoate + ?
-
-
-
-
?
S-(1,2-dichlorovinyl)-L-cysteine + ?
S-(1,2-dichlorovinyl)-2-oxo-3-thiopropanoate + ?
-
-
-
-
?
S-(2-chloro-1,1,2-trifluoroethyl)-L-cysteine + ?
S-(2-chloro-1,1,2-trifluoroethyl)-2-oxo-3-thiopropanoate + ?
-
-
-
-
?
additional information
?
-
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
?
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
?
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
2-oxoisohexanoate + L-glutamate
-
-
-
-
?
L-leucine + 2-oxoglutarate
2-oxoisohexanoate + L-glutamate
-
-
-
?
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
?
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
?
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-norvaline + 4-methyl-2-oxopentanoate
2-oxopentanoate + L-leucine
-
-
-
-
?
L-norvaline + 4-methyl-2-oxopentanoate
2-oxopentanoate + L-leucine
-
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
-
?
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
?
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
r
additional information
?
-
in addition to this traditional role, BCAT possesses other activities including its role as a cysteine S-conjugate beta-lyase and a thiol disulfide isomerase. Aminotransferase proteins including BCAT have been shown to catalyse beta-lyase reactions with amino acids containing a good leaving group in the beta position. Possible BCAT oxidoreductase activity. BCAT enhances the overall PDI activity and increases the rate of refolding. BCATm may be a chaperone for PDI operating through a thiol disulfide exchange mechanism or independently as an oxidoreductase regulated through the redox environment
-
-
-
additional information
?
-
in addition to this traditional role, BCAT possesses other activities including its role as a cysteine S-conjugate beta-lyase and a thiol disulfide isomerase. Aminotransferase proteins including BCAT have been shown to catalyse beta-lyase reactions with amino acids containing a good leaving group in the beta position. Possible BCAT oxidoreductase activity. BCAT enhances the overall PDI activity and increases the rate of refolding. BCATm may be a chaperone for PDI operating through a thiol disulfide exchange mechanism or independently as an oxidoreductase regulated through the redox environment
-
-
-
additional information
?
-
-
recombinant human BCATm and BCATc have beta-lyase activity towards 3 toxic L-cysteine S-conjugates, S-(1,1,2,2-tetrafluoroethyl)-L-cysteine, S-(1,2-dichlorovinyl)-L-cysteine and S-(2-chloro-1,1,2-trifluoroethyl)-L-cysteine and toward 3-chloro-L-alanine, BCATm is also active toward benzothiazolyl-L-cysteine, pyruvate formed from beta-lyase substrates
-
-
?
additional information
?
-
-
transamination activity with oxaloacetate is too low to be evaluated, DL-aminoadipate, glycine, L-phenylalanine, L-tyrosine and L-methionine are no substrates
-
-
?
additional information
?
-
-
novel co-repressor for thyroid hormone nuclear receptors
-
-
?
additional information
?
-
novel co-repressor for thyroid hormone nuclear receptors
-
-
?
additional information
?
-
in addition to this traditional role, BCAT possesses other activities including its role as a cysteine S-conjugate beta-lyase and a thiol disulfide isomerase. Aminotransferase proteins including BCAT have been shown to catalyse beta-lyase reactions with amino acids containing a good leaving group in the beta position. Possible BCAT oxidoreductase activity
-
-
-
additional information
?
-
in addition to this traditional role, BCAT possesses other activities including its role as a cysteine S-conjugate beta-lyase and a thiol disulfide isomerase. Aminotransferase proteins including BCAT have been shown to catalyse beta-lyase reactions with amino acids containing a good leaving group in the beta position. Possible BCAT oxidoreductase activity
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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(1,2-benzoxazol-3-yl)acetic acid
-
(2,1,3-benzothiadiazol-5-yl)methanol
-
2-(2-((4-(1H-pyrazol-3-yl)phenyl)carbamoyl)phenyl)acetic acid
-
2-(2-(5-methyl-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-6-carboxamido)phenyl)acetic Acid
-
2-(4-(1H-pyrazol-3-yl)phenyl)-3,4-dihydroisoquinolin-1(2H)-one
-
2-(methanesulfonyl)-N-phenylbenzamide
-
2-ethoxy-5-methyl-7-oxo-4,7-dihydropyrazolo[1,5-a]-pyrimidine-3-carbonitrile
-
2-hydroxy-N-(1,2,3,4-tetrahydronaphthalen-1-yl)acetamide
-
3,5-dimethyl-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-6-carboxylic acid
-
3,5-dimethyl-4-oxo-N-phenyl-3,4-dihydrothieno[2,3-d]-pyrimidine-6-carboxamide
-
3,5-dimethyl-6-(piperidine-1-carbonyl)thieno[2,3-d]-pyrimidin-4(3H)-one
-
3-methyl-1,2,3,4-tetrahydroquinoline-8-sulfonamide
-
3-methyl-2-[(quinazolin-4-yl)sulfanyl]butanoic acid
-
3-phenylthiophene-2-carboxamide
-
4-(1-oxo-3,4-dihydroisoquinolin-2(1H)-yl)benzamide
-
5-benzyl-7-oxo-4,7-dihydropyrazolo[1,5-a]pyrimidine-3-carbonitrile
-
5-ethyl-2-methyl-7-oxo-4,7-dihydropyrazolo[1,5-a]pyrimidine-3-carbonitrile
-
5-methyl-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-6-carboxylic acid
-
5-methyl-4-oxo-N-(1,3,4-thiadiazol-2-yl)-3,4-dihydrothieno-[2,3-d]pyrimidine-6-carboxamide
-
5-methyl-4-oxo-N-(2-sulfamoylphenyl)-3,4-dihydrothieno-[2,3-d]pyrimidine-6-carboxamide
-
5-methyl-4-oxo-N-(m-tolyl)-3,4-dihydrothieno[2,3-d]-pyrimidine-6-carboxamide
-
5-methyl-4-oxo-N-(o-tolyl)-3,4-dihydrothieno[2,3-d]-pyrimidine-6-carboxamide
-
5-methyl-4-oxo-N-(p-tolyl)-3,4-dihydrothieno[2,3-d]-pyrimidine-6-carboxamide
-
5-methyl-4-oxo-N-(pyridin-3-yl)-3,4-dihydrothieno[2,3-d]-pyrimidine-6-carboxamide
-
5-methyl-4-oxo-N-(thiophen-2-yl)-3,4-dihydrothieno[2,3-d]-pyrimidine-6-carboxamide
-
5-methyl-4-oxo-N-phenyl-3,4-dihydrothieno[2,3-d]-pyrimidine-6-carboxamide
-
5-methyl-N-(2-(methylsulfonyl )phenyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-6-carboxamide
-
6-phenoxypyridazin-3-amine
-
benzothiazolyl-L-cysteine
BTC, is a substrate and inactivator of BCATm but not BCATc, but BTC inhibits transamination between leucine and 2-oxoglutarate for both enzymes. Inactivation of BCATm can occur through the interaction of aminoacrylate generated from the beta-lyase reaction with the PLP cofactor, through alkylation of a key residue at the active site, or through thioacylation by the eliminated sulphur-containing fragment
beta-chloro-L-alanine
the compound is able to fit into the active site of BCATm, leading to inhibition of BCATm
ethyl 2-(2-(5-methyl-4-oxo-3,4-dihydrothieno[2,3-d]-pyrimidine-6-carboxamido)phenyl)acetate
-
gabapentin
inhibition is isoform-specific
N-(2-(1H-pyrazol-3-yl)pyrimidin-5-yl)benzamide
-
N-(2-(hydroxymethyl)phenyl)-5-methyl-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-6-carboxamide
-
N-(2-hydroxy-2-phenylethyl)urea
-
N-(4-(1H-pyrazol-3-yl)phenyl)benzamide
-
N-(4-carbamoylphenyl)-3,4-dichlorobenzamide
-
N-(4-carbamoylphenyl)benzamide
-
N-(isoxazol-3-yl)-5-methyl-4-oxo-3,4-dihydrothieno[2,3-d]-pyrimidine-6-carboxamide
-
N-(pyrimidin-5-yl)benzamide
-
N-cyclopentyl-3,5-dimethyl-4-oxo-3,4-dihydrothieno[2,3-d]-pyrimidine-6-carboxamide
-
[(3,6,7-trimethylquinolin-2-yl)sulfanyl]acetic acid
-
[1,1'-biphenyl]-2-carboxamide
-
[2-(phenylcarbamoyl)phenyl]acetic acid
-
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
beta-chloro-L-alanine
-
rapidly inactivated by the beta-lyase substrate
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
trichloroethylene/dichloroacetylene
DCVC, selectively inhibits BCATc, resulting in suppressed transamination and subsequent neurotoxicity
benzothiazolyl-L-cysteine
-
inhibits the L-leucine-2-oxoglutarate tranamination reaction of both isoenzymes
benzothiazolyl-L-cysteine
BTC, is a substrate and inactivator of BCATm but not BCATc, but BTC inhibits transamination between leucine and 2-oxoglutarate for both enzymes
gabapentin
-
structural analogue of leucine, competitive inhibitor of BCATc, does not inhibit BCATm
gabapentin
-
inhibitor of the cytosolic enzyme
additional information
synthesis and evaluation of diverse inhibitors, pIC50 values, overview
-
additional information
-
not inhibited by isonicotinic acid and semicarbazide
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Acute Coronary Syndrome
THE BRANCHED-CHAIN AMINO ACID TRANSAMINASE 1 -23C/G POLYMORPHISM CONFERS PROTECTION AGAINST ACUTE CORONARY SYNDROME.
Adenocarcinoma
[The Expression and Significance of c-myc and bcat1 in Cervical Cancer].
Adenoma
Evaluation of a panel of tumor-specific differentially-methylated DNA regions in IRF4, IKZF1 and BCAT1 for blood-based detection of colorectal cancer.
Alzheimer Disease
Altered Expression of Human Mitochondrial Branched Chain Aminotransferase in Dementia with Lewy Bodies and Vascular Dementia.
Alzheimer Disease
BCAT-induced autophagy regulates A? load through an interdependence of redox state and PKC phosphorylation-implications in Alzheimer's disease.
Alzheimer Disease
Regional Increase in the Expression of the BCAT Proteins in Alzheimer's Disease Brain: Implications in Glutamate Toxicity.
Alzheimer Disease
THE BRANCHED-CHAIN AMINOTRANSFERASE PROTEINS: NOVEL REDOX CHAPERONES FOR PROTEIN DISULFIDE ISOMERASE- IMPLICATIONS IN ALZHEIMER'S DISEASE.
Astrocytoma
Loss of BCAT1 Expression is a Sensitive Marker for IDH-Mutant Diffuse Glioma.
Blast Crisis
Cancer progression by reprogrammed BCAA metabolism in myeloid leukaemia.
Brain Diseases
Expanding the genetic and phenotypic spectrum of branched-chain amino acid transferase 2 deficiency.
Brain Neoplasms
Differential expression and prognostic significance of SOX genes in pediatric medulloblastoma and ependymoma identified by microarray analysis.
branched-chain-amino-acid transaminase deficiency
BCATm deficiency ameliorates endotoxin-induced decrease in muscle protein synthesis and improves survival in septic mice.
branched-chain-amino-acid transaminase deficiency
Branched-chain aminotransferase deficiency in Chinese hamster cells complemented by two independent genes on human chromosomes 12 and 19.
branched-chain-amino-acid transaminase deficiency
ENU mutagenesis identifies mice with mitochondrial branched-chain aminotransferase deficiency resembling human maple syrup urine disease.
branched-chain-amino-acid transaminase deficiency
Expanding the genetic and phenotypic spectrum of branched-chain amino acid transferase 2 deficiency.
branched-chain-amino-acid transaminase deficiency
Localization of a gene which complements branched-chain amino acid transaminase deficiency to the short arm of human chromosome 12.
Breast Neoplasms
BCATc modulates crosstalk between the PI3K/Akt and the Ras/ERK pathway regulating proliferation in triple negative breast cancer.
Breast Neoplasms
Branched-chain amino acid transaminase 1 (BCAT1) promotes the growth of breast cancer cells through improving mTOR-mediated mitochondrial biogenesis and function.
Breast Neoplasms
DOT1L histone methyltransferase regulates the expression of BCAT1 and is involved in sphere formation and cell migration of breast cancer cell lines.
Breast Neoplasms
The branched-chain amino acid transaminase 1 sustains growth of antiestrogen-resistant and ER?-negative breast cancer.
Carcinogenesis
BCAT1 expression associates with ovarian cancer progression: possible implications in altered disease metabolism.
Carcinogenesis
BCAT1 Overexpression Promotes Proliferation, Invasion, and Wnt Signaling in Non-Small Cell Lung Cancers.
Carcinogenesis
Data mining of the expression and regulatory role of BCAT1 in hepatocellular carcinoma.
Carcinogenesis
Identification of genes with differential expression in chemoresistant epithelial ovarian cancer using high-density oligonucleotide microarrays.
Carcinogenesis
Isozyme patterns of branched-chain amino acid transaminase during cellular differentiation and carcinogenesis.
Carcinogenesis
Silencing of Long Noncoding RNA LINC00324 Interacts with MicroRNA-3200-5p to Attenuate the Tumorigenesis of Gastric Cancer via Regulating BCAT1.
Carcinoma
BCAT1 overexpression is an indicator of poor prognosis in patients with urothelial carcinomas of the upper urinary tract and urinary bladder.
Carcinoma
BCAT1 overexpression regulates proliferation and c?Myc/GLUT1 signaling in head and neck squamous cell carcinoma.
Carcinoma, Hepatocellular
BCAT1 expression in hepatocellular carcinoma.
Carcinoma, Hepatocellular
BCAT1 promotes tumor cell migration and invasion in hepatocellular carcinoma.
Carcinoma, Hepatocellular
BCAT1, a key prognostic predictor of hepatocellular carcinoma, promotes cell proliferation and induces chemoresistance to cisplatin.
Carcinoma, Hepatocellular
Branched chain aminotransferase isoenzymes. Purification and characterization of the rat brain isoenzyme.
Carcinoma, Hepatocellular
Branched-chain amino acid aminotransferase 2 regulates ferroptotic cell death in cancer cells.
Carcinoma, Hepatocellular
Cloning and expression of the mammalian cytosolic branched chain aminotransferase isoenzyme.
Carcinoma, Hepatocellular
Data mining of the expression and regulatory role of BCAT1 in hepatocellular carcinoma.
Carcinoma, Hepatocellular
Isozyme patterns of branched-chain amino acid transaminase in various rat hepatomas.
Carcinoma, Hepatocellular
LncRNA CRNDE promotes hepatocellular carcinoma cell proliferation, invasion, and migration through regulating miR-203/ BCAT1 axis.
Carcinoma, Hepatocellular
Mitochondrial branched chain aminotransferase gene expression in AS-30D hepatoma rat cells and during liver regeneration after partial hepatectomy in rat.
Carcinoma, Ovarian Epithelial
BCAT1 expression associates with ovarian cancer progression: possible implications in altered disease metabolism.
Carcinoma, Squamous Cell
BCAT1 overexpression regulates proliferation and c?Myc/GLUT1 signaling in head and neck squamous cell carcinoma.
Carcinoma, Squamous Cell
[The Expression and Significance of c-myc and bcat1 in Cervical Cancer].
Cardiovascular Diseases
Oxoeicosanoid receptor inhibition alleviates acute myocardial infarction through activation of BCAT1.
Chondrosarcoma
Leucine and branched-chain amino acid metabolism contribute to the growth of bone sarcomas by regulating AMPK and mTORC1 signaling.
Colorectal Neoplasms
A cross-sectional study comparing a blood test for methylated BCAT1 and IKZF1 tumor-derived DNA with CEA for detection of recurrent colorectal cancer.
Colorectal Neoplasms
BCATc modulates crosstalk between the PI3K/Akt and the Ras/ERK pathway regulating proliferation in triple negative breast cancer.
Colorectal Neoplasms
Circulating tumour DNA for monitoring colorectal cancer-a prospective cohort study to assess relationship to tissue methylation, cancer characteristics and surgical resection.
Colorectal Neoplasms
Detection of Circulating Tumor DNA Methylation in Diagnosis of Colorectal Cancer.
Colorectal Neoplasms
Differential expression of the BCAT isoforms between breast cancer subtypes.
Colorectal Neoplasms
Evaluation of a panel of tumor-specific differentially-methylated DNA regions in IRF4, IKZF1 and BCAT1 for blood-based detection of colorectal cancer.
Colorectal Neoplasms
Evaluation of an assay for methylated BCAT1 and IKZF1 in plasma for detection of colorectal neoplasia.
Colorectal Neoplasms
Evaluation of Circulating Tumor DNA for Methylated BCAT1 and IKZF1 to Detect Recurrence of Stage II/Stage III Colorectal Cancer (CRC).
Colorectal Neoplasms
Evaluation of Methylation Biomarkers for Detection of Circulating Tumor DNA and Application to Colorectal Cancer.
Colorectal Neoplasms
Long non-coding RNA TMPO-AS1 facilitates the progression of colorectal cancer cells via sponging miR-98-5p to upregulate BCAT1 expression.
Colorectal Neoplasms
Methylation and Gene Expression of BCAT1 and IKZF1 in Colorectal Cancer Tissues.
Colorectal Neoplasms
Relationship between post-surgery detection of methylated circulating tumor DNA with risk of residual disease and recurrence-free survival.
Colorectal Neoplasms
Validation of a Circulating Tumor-Derived DNA Blood Test for Detection of Methylated BCAT1 and IKZF1 DNA.
Colorectal Neoplasms
Variables associated with detection of methylated BCAT1 or IKZF1 in blood from patients without colonoscopically-evident colorectal cancer.
Dementia
Altered Expression of Human Mitochondrial Branched Chain Aminotransferase in Dementia with Lewy Bodies and Vascular Dementia.
Dementia, Vascular
Altered Expression of Human Mitochondrial Branched Chain Aminotransferase in Dementia with Lewy Bodies and Vascular Dementia.
Diabetes Mellitus, Type 2
Identification of novel candidate genes for type 2 diabetes from a genome-wide association scan in the Old Order Amish: evidence for replication from diabetes-related quantitative traits and from independent populations.
Dyslipidemias
Inhibitors of BCATm: A Tough Nut To Crack.
Endometrial Hyperplasia
BCAT1 promotes proliferation of endometrial cancer cells through reprogrammed BCAA metabolism.
Endometrial Neoplasms
BCAT1 promotes proliferation of endometrial cancer cells through reprogrammed BCAA metabolism.
Ependymoma
Differential expression and prognostic significance of SOX genes in pediatric medulloblastoma and ependymoma identified by microarray analysis.
Fatty Liver
Changes in activity levels and isozyme patterns of isoleucine aminotransferase in response to experimentally induced hepatic lesion.
Fatty Liver
Genome-scale metabolic modelling of hepatocytes reveals serine deficiency in patients with non-alcoholic fatty liver disease.
Glioblastoma
Assessment of bevacizumab resistance increased by expression of BCAT1 in IDH1 wild-type glioblastoma: application of DSC perfusion MR imaging.
Glioblastoma
BCAT1 is a New MR Imaging-related Biomarker for Prognosis Prediction in IDH1-wildtype Glioblastoma Patients.
Glioblastoma
BCAT1 promotes cell proliferation through amino acid catabolism in gliomas carrying wild-type IDH1.
Glioblastoma
Enrichment of branched chain amino acid transaminase 1 correlates with multiple biological processes and contributes to poor survival of IDH1 wild-type gliomas.
Glioblastoma
Intact Protein Analysis at 21 Tesla and X-Ray Crystallography Define Structural Differences in Single Amino Acid Variants of Human Mitochondrial Branched-Chain Amino Acid Aminotransferase 2 (BCAT2).
Glioblastoma
Multistage Ultraviolet Photodissociation Mass Spectrometry To Characterize Single Amino Acid Variants of Human Mitochondrial BCAT2.
Glioblastoma
Regulation of branched-chain amino acid metabolism by hypoxia-inducible factor in glioblastoma.
Glioma
BCAT1 defines gliomas by IDH status.
Glioma
BCAT1 promotes cell proliferation through amino acid catabolism in gliomas carrying wild-type IDH1.
Glioma
BCATc modulates crosstalk between the PI3K/Akt and the Ras/ERK pathway regulating proliferation in triple negative breast cancer.
Glioma
Clinical aggressiveness of malignant gliomas is linked to augmented metabolism of amino acids.
Glioma
Diagnostic value of glutamate with 2-hydroxyglutarate in magnetic resonance spectroscopy for IDH1 mutant glioma.
Glioma
Differential expression of the BCAT isoforms between breast cancer subtypes.
Glioma
Enrichment of branched chain amino acid transaminase 1 correlates with multiple biological processes and contributes to poor survival of IDH1 wild-type gliomas.
Glioma
In search of druggable targets for GBM amino acid metabolism.
Glioma
LINC00963 Confers Oncogenic Properties in Glioma by Regulating the miR-506/BCAT1 Axis.
Glioma
Loss of BCAT1 Expression is a Sensitive Marker for IDH-Mutant Diffuse Glioma.
Glioma
Neuro-oncology: BCAT1 promotes cell proliferation in aggressive gliomas.
Glioma
Systematic identification of single amino Acid variants in glioma stem-cell-derived chromosome 19 proteins.
Hypertension
Genetic susceptibility to salt-sensitive hypertension in a Han Chinese population: a validation study of candidate genes.
Insulin Resistance
Effect of the BCAT2 polymorphism (rs11548193) on plasma branched-chain amino acid concentrations after dietary intervention in subjects with obesity and insulin resistance.
Insulin Resistance
Serum amino acid concentrations are modified by age, insulin resistance, and BCAT2 rs11548193 and BCKDH rs45500792 polymorphisms in subjects with obesity.
Leukemia
Curcumin induces apoptosis by inhibiting BCAT1 expression and mTOR signaling in cytarabine?resistant myeloid leukemia cells.
Leukemia
Loss of EZH2 Reprograms BCAA Metabolism to Drive Leukemic Transformation.
Leukemia, Myeloid
BCAT1 Enhances BCAA Production to Drive Myeloid Leukemia.
Leukemia, Myeloid
Curcumin induces apoptosis by inhibiting BCAT1 expression and mTOR signaling in cytarabine?resistant myeloid leukemia cells.
Liver Failure
Ammonia detoxification by accelerated oxidation of branched chain amino acids in brains of acute hepatic failure rats.
Liver Neoplasms
Circulating Tumor Cells Undergoing EMT Provide a Metric for Diagnosis and Prognosis of Patients with Hepatocellular Carcinoma.
Liver Neoplasms
LncRNA CRNDE promotes hepatocellular carcinoma cell proliferation, invasion, and migration through regulating miR-203/ BCAT1 axis.
Liver Neoplasms, Experimental
Isozyme patterns of branched-chain amino acid transminase in cultured Morris hepatoma 7316A.
Lung Diseases
BCAT1 binds the RNA-binding protein ZNF423 to activate autophagy via the IRE1-XBP-1-RIDD axis in hypoxic PASMCs.
Lung Neoplasms
BCAT1 Overexpression Promotes Proliferation, Invasion, and Wnt Signaling in Non-Small Cell Lung Cancers.
Lymphatic Metastasis
BCAT1 promotes proliferation of endometrial cancer cells through reprogrammed BCAA metabolism.
Lymphatic Metastasis
Over-expression of BCAT1 is a prognostic marker in gastric cancer.
Lymphoma
Mice deficient in the mitochondrial branched-chain aminotransferase (BCATm) respond with delayed tumour growth to a challenge with EL-4 lymphoma.
Maple Syrup Urine Disease
ENU mutagenesis identifies mice with mitochondrial branched-chain aminotransferase deficiency resembling human maple syrup urine disease.
Medulloblastoma
Differential expression and prognostic significance of SOX genes in pediatric medulloblastoma and ependymoma identified by microarray analysis.
Melanoma
BCAT1 and miR-2504: novel methylome signature distinguishes spindle/desmoplastic melanoma from superficial malignant peripheral nerve sheath tumor.
Melanoma
BCAT1 knockdown-mediated suppression of melanoma cell proliferation and migration is associated with reduced oxidative phosphorylation.
Melanoma, Experimental
BCAT1 knockdown-mediated suppression of melanoma cell proliferation and migration is associated with reduced oxidative phosphorylation.
Movement Disorders
High-throughput behavioral screen in C. elegans reveals Parkinson's disease drug candidates.
Movement Disorders
Metformin rescues Parkinson's disease phenotypes caused by hyperactive mitochondria.
Myocardial Infarction
Oxoeicosanoid receptor inhibition alleviates acute myocardial infarction through activation of BCAT1.
Nasopharyngeal Carcinoma
Flotillin-2 promotes cell proliferation via activating the c-Myc/BCAT1 axis by suppressing miR-33b-5p in nasopharyngeal carcinoma.
Nasopharyngeal Carcinoma
Over-expression of BCAT1, a c-Myc target gene, induces cell proliferation, migration and invasion in nasopharyngeal carcinoma.
Neoplasm Metastasis
BCAT1 Overexpression Promotes Proliferation, Invasion, and Wnt Signaling in Non-Small Cell Lung Cancers.
Neoplasm Metastasis
BCAT1 overexpression regulates proliferation and c?Myc/GLUT1 signaling in head and neck squamous cell carcinoma.
Neoplasm Metastasis
BCAT1 promotes proliferation of endometrial cancer cells through reprogrammed BCAA metabolism.
Neoplasm Metastasis
BCATc modulates crosstalk between the PI3K/Akt and the Ras/ERK pathway regulating proliferation in triple negative breast cancer.
Neoplasm Metastasis
Differential expression and prognostic significance of SOX genes in pediatric medulloblastoma and ependymoma identified by microarray analysis.
Neoplasm Metastasis
Over-expression of BCAT1 is a prognostic marker in gastric cancer.
Neoplasm Metastasis
Relationship between post-surgery detection of methylated circulating tumor DNA with risk of residual disease and recurrence-free survival.
Neoplasm Metastasis
Src promotes castration-recurrent prostate cancer through androgen receptor-dependent canonical and non-canonical transcriptional signatures.
Neoplasm Metastasis
[The Expression and Significance of c-myc and bcat1 in Cervical Cancer].
Neoplasms
A Blood Test for Methylated BCAT1 and IKZF1 vs. a Fecal Immunochemical Test for Detection of Colorectal Neoplasia.
Neoplasms
A two-gene blood test for methylated DNA sensitive for colorectal cancer.
Neoplasms
Assay of leucine aminotransferase in rat tissues and tumors.
Neoplasms
Assessment of bevacizumab resistance increased by expression of BCAT1 in IDH1 wild-type glioblastoma: application of DSC perfusion MR imaging.
Neoplasms
BCAT1 Activates PI3K/AKT/mTOR Pathway and Contributes to the Angiogenesis and Tumorigenicity of Gastric Cancer.
Neoplasms
BCAT1 and miR-2504: novel methylome signature distinguishes spindle/desmoplastic melanoma from superficial malignant peripheral nerve sheath tumor.
Neoplasms
BCAT1 decreases the sensitivity of cancer cells to cisplatin by regulating mTOR-mediated autophagy via branched-chain amino acid metabolism.
Neoplasms
BCAT1 Enhances BCAA Production to Drive Myeloid Leukemia.
Neoplasms
BCAT1 expression associates with ovarian cancer progression: possible implications in altered disease metabolism.
Neoplasms
BCAT1 knockdown-mediated suppression of melanoma cell proliferation and migration is associated with reduced oxidative phosphorylation.
Neoplasms
BCAT1 overexpression is an indicator of poor prognosis in patients with urothelial carcinomas of the upper urinary tract and urinary bladder.
Neoplasms
BCAT1 Overexpression Promotes Proliferation, Invasion, and Wnt Signaling in Non-Small Cell Lung Cancers.
Neoplasms
BCAT1 overexpression regulates proliferation and c?Myc/GLUT1 signaling in head and neck squamous cell carcinoma.
Neoplasms
BCAT1 promotes cell proliferation through amino acid catabolism in gliomas carrying wild-type IDH1.
Neoplasms
BCAT1 promotes proliferation of endometrial cancer cells through reprogrammed BCAA metabolism.
Neoplasms
BCAT1 promotes tumor cell migration and invasion in hepatocellular carcinoma.
Neoplasms
BCAT1, a key prognostic predictor of hepatocellular carcinoma, promotes cell proliferation and induces chemoresistance to cisplatin.
Neoplasms
BCAT2-mediated BCAA catabolism is critical for development of pancreatic ductal adenocarcinoma.
Neoplasms
BCATc modulates crosstalk between the PI3K/Akt and the Ras/ERK pathway regulating proliferation in triple negative breast cancer.
Neoplasms
Branched-chain amino acid aminotransferase 2 regulates ferroptotic cell death in cancer cells.
Neoplasms
Branched-chain amino acid metabolism in cancer.
Neoplasms
Circulating tumour DNA for monitoring colorectal cancer-a prospective cohort study to assess relationship to tissue methylation, cancer characteristics and surgical resection.
Neoplasms
Curcumin induces apoptosis by inhibiting BCAT1 expression and mTOR signaling in cytarabine?resistant myeloid leukemia cells.
Neoplasms
Data mining of the expression and regulatory role of BCAT1 in hepatocellular carcinoma.
Neoplasms
Detection of Circulating Tumor DNA Methylation in Diagnosis of Colorectal Cancer.
Neoplasms
Differential expression and prognostic significance of SOX genes in pediatric medulloblastoma and ependymoma identified by microarray analysis.
Neoplasms
Differential expression of the BCAT isoforms between breast cancer subtypes.
Neoplasms
Enrichment of branched chain amino acid transaminase 1 correlates with multiple biological processes and contributes to poor survival of IDH1 wild-type gliomas.
Neoplasms
Evaluation of a panel of tumor-specific differentially-methylated DNA regions in IRF4, IKZF1 and BCAT1 for blood-based detection of colorectal cancer.
Neoplasms
Evaluation of an assay for methylated BCAT1 and IKZF1 in plasma for detection of colorectal neoplasia.
Neoplasms
Evaluation of Circulating Tumor DNA for Methylated BCAT1 and IKZF1 to Detect Recurrence of Stage II/Stage III Colorectal Cancer (CRC).
Neoplasms
Functional evidence for a nasopharyngeal carcinoma-related gene BCAT1 located at 12p12.
Neoplasms
Hyperpolarized [1-13C] glutamate: a metabolic imaging biomarker of IDH1 mutational status in glioma.
Neoplasms
Identification of genes with differential expression in chemoresistant epithelial ovarian cancer using high-density oligonucleotide microarrays.
Neoplasms
Intact Protein Analysis at 21 Tesla and X-Ray Crystallography Define Structural Differences in Single Amino Acid Variants of Human Mitochondrial Branched-Chain Amino Acid Aminotransferase 2 (BCAT2).
Neoplasms
Isozyme patterns of branched-chain amino acid transaminase in human tissues and tumors.
Neoplasms
Leucine and branched-chain amino acid metabolism contribute to the growth of bone sarcomas by regulating AMPK and mTORC1 signaling.
Neoplasms
LINC00963 Confers Oncogenic Properties in Glioma by Regulating the miR-506/BCAT1 Axis.
Neoplasms
LncRNA CRNDE promotes hepatocellular carcinoma cell proliferation, invasion, and migration through regulating miR-203/ BCAT1 axis.
Neoplasms
Loss of BCAT1 Expression is a Sensitive Marker for IDH-Mutant Diffuse Glioma.
Neoplasms
Loss of EZH2 Reprograms BCAA Metabolism to Drive Leukemic Transformation.
Neoplasms
Methylation and Gene Expression of BCAT1 and IKZF1 in Colorectal Cancer Tissues.
Neoplasms
Mice deficient in the mitochondrial branched-chain aminotransferase (BCATm) respond with delayed tumour growth to a challenge with EL-4 lymphoma.
Neoplasms
MicroRNA-218 inhibits tumor growth and increases chemosensitivity to CDDP treatment by targeting BCAT1 in prostate cancer.
Neoplasms
miR-98-5p inhibits gastric cancer cell stemness and chemoresistance by targeting branched-chain aminotransferases 1.
Neoplasms
Multistage Ultraviolet Photodissociation Mass Spectrometry To Characterize Single Amino Acid Variants of Human Mitochondrial BCAT2.
Neoplasms
Over-expression of BCAT1 is a prognostic marker in gastric cancer.
Neoplasms
Prognostic significance of branched-chain amino acid transferase 1 and CD133 in triple-negative breast cancer.
Neoplasms
The branched-chain amino acid transaminase 1 sustains growth of antiestrogen-resistant and ER?-negative breast cancer.
Neoplasms
The role of DNMT1/hsa-miR-124-3p/BCAT1 pathway in regulating growth and invasion of esophageal squamous cell carcinoma.
Neoplasms
Tissue of origin dictates branched-chain amino acid metabolism in mutant Kras-driven cancers.
Neoplasms
Tumour-reprogrammed stromal BCAT1 fuels branched-chain ketoacid dependency in stromal-rich PDAC tumours.
Neoplasms
Variables associated with detection of methylated BCAT1 or IKZF1 in blood from patients without colonoscopically-evident colorectal cancer.
Neoplasms
[The Expression and Significance of c-myc and bcat1 in Cervical Cancer].
Nephrosis
Hepatic histidase and muscle branched chain aminotransferase gene expression in experimental nephrosis.
Nephrotic Syndrome
Reduced kidney branched chain aminotransferase expression in puromycin aminonucleoside-induced nephrotic syndrome.
Neurodegenerative Diseases
The design and synthesis of human branched-chain amino acid aminotransferase inhibitors for treatment of neurodegenerative diseases.
Neurofibrosarcoma
BCAT1 and miR-2504: novel methylome signature distinguishes spindle/desmoplastic melanoma from superficial malignant peripheral nerve sheath tumor.
Non-alcoholic Fatty Liver Disease
Branched chain amino acid transaminase 1 (BCAT1) is overexpressed and hypomethylated in patients with non-alcoholic fatty liver disease who experience adverse clinical events: A pilot study.
Obesity
Adverse Childhood Experiences, Epigenetic Measures, and Obesity in Youth.
Obesity
Discovery, SAR, and X-ray Binding Mode Study of BCATm Inhibitors from a Novel DNA-Encoded Library.
Obesity
Effect of the BCAT2 polymorphism (rs11548193) on plasma branched-chain amino acid concentrations after dietary intervention in subjects with obesity and insulin resistance.
Obesity
Inhibitors of BCATm: A Tough Nut To Crack.
Obesity
Metabolic Fate of Branched-Chain Amino Acids During Adipogenesis, in Adipocytes From Obese Mice and C2C12 Myotubes.
Obesity
Obesity-related elevations in plasma leucine are associated with alterations in enzymes involved in branched-chain amino acid metabolism.
Obesity
Serum amino acid concentrations are modified by age, insulin resistance, and BCAT2 rs11548193 and BCKDH rs45500792 polymorphisms in subjects with obesity.
Osteosarcoma
Leucine and branched-chain amino acid metabolism contribute to the growth of bone sarcomas by regulating AMPK and mTORC1 signaling.
Ovarian Neoplasms
BCAT1 expression associates with ovarian cancer progression: possible implications in altered disease metabolism.
Pancreatic Neoplasms
Acetylation promotes BCAT2 degradation to suppress BCAA catabolism and pancreatic cancer growth.
Pancreatic Neoplasms
Branched-chain amino acid aminotransferase 2 regulates ferroptotic cell death in cancer cells.
Pancreatitis
[Diagnostic importance of determining leucine aminotransferase activity in acute pancreatitis]
Parkinson Disease
High-throughput behavioral screen in C. elegans reveals Parkinson's disease drug candidates.
Parkinson Disease
Metformin rescues Parkinson's disease phenotypes caused by hyperactive mitochondria.
Prostatic Neoplasms
MicroRNA-218 inhibits tumor growth and increases chemosensitivity to CDDP treatment by targeting BCAT1 in prostate cancer.
Prostatic Neoplasms
The feasibility of assessing branched-chain amino acid metabolism in cellular models of prostate cancer with hyperpolarized [1-(13)C]-ketoisocaproate.
Sarcoma, Avian
Change of isozyme pattern during activation of a transforming gene product: its relation to other biochemical markers of cellular transformation and differentiation.
Scrapie
Arabidopsis and maize RidA proteins preempt reactive enamine/imine damage to branched-chain amino acid biosynthesis in plastids.
Scrapie
Crystal structures of RidA, an important enzyme for the prevention of toxic side products.
Scrapie
RidA proteins prevent metabolic damage inflicted by PLP-dependent dehydratases in all domains of life.
Scrapie
Suppressor Analyses Identify Threonine as a Modulator of ridA Mutant Phenotypes in Salmonella enterica.
Squamous Cell Carcinoma of Head and Neck
BCAT1 overexpression regulates proliferation and c?Myc/GLUT1 signaling in head and neck squamous cell carcinoma.
Starvation
Amino acid metabolism enzyme activities in the obese Zucker rat.
Starvation
Amino-acid metabolism enzyme activities in rat white adipose tissue.
Starvation
Impact of short-term starvation and refeeding on the expression of KLF15 and regulatory mechanism of branched-chain amino acids metabolism in muscle of Chinese soft-shelled turtle (Pelodiscus sinensis).
Starvation
MiR-125a-3p-KLF15-BCAA Regulates the Skeletal Muscle Branched-Chain Amino Acid Metabolism in Nile Tilapia (Oreochromis niloticus) During Starvation.
Starvation
Studies on metabolism of branched chain amino acids in brain and other tissues of rat with special reference to leucine.
Stomach Neoplasms
BCAT1 Activates PI3K/AKT/mTOR Pathway and Contributes to the Angiogenesis and Tumorigenicity of Gastric Cancer.
Stomach Neoplasms
BCAT1 and miR-2504: novel methylome signature distinguishes spindle/desmoplastic melanoma from superficial malignant peripheral nerve sheath tumor.
Stomach Neoplasms
miR-98-5p inhibits gastric cancer cell stemness and chemoresistance by targeting branched-chain aminotransferases 1.
Stomach Neoplasms
Over-expression of BCAT1 is a prognostic marker in gastric cancer.
Stomach Neoplasms
Silencing of Long Noncoding RNA LINC00324 Interacts with MicroRNA-3200-5p to Attenuate the Tumorigenesis of Gastric Cancer via Regulating BCAT1.
Teratocarcinoma
Identification of amplified genes from SV40 large T antigen-induced rat PNET cell lines by subtractive cDNA analysis and radiation hybrid mapping.
Thyroid Neoplasms
Six1 Overexpression Promotes Glucose Metabolism and Invasion Through Regulation of GLUT3, MMP2 and Snail in Thyroid Cancer Cells.
Triple Negative Breast Neoplasms
BCATc modulates crosstalk between the PI3K/Akt and the Ras/ERK pathway regulating proliferation in triple negative breast cancer.
Triple Negative Breast Neoplasms
Prognostic significance of branched-chain amino acid transferase 1 and CD133 in triple-negative breast cancer.
Triple Negative Breast Neoplasms
The branched-chain amino acid transaminase 1 sustains growth of antiestrogen-resistant and ER?-negative breast cancer.
Tuberculosis
Branched-chain amino acid aminotransferase and methionine formation in Mycobacterium tuberculosis.
Tuberculosis
Chemical Mechanism of the Branched-Chain Aminotransferase IlvE from Mycobacterium tuberculosis.
Tuberculosis
Mechanism-Based Inhibition of the Mycobacterium tuberculosis Branched-Chain Aminotransferase by d- and l-Cycloserine.
Tuberculosis
Structural analysis of mycobacterial branched-chain aminotransferase: implications for inhibitor design.
Tuberculosis
The 1.9 A structure of the branched-chain amino-acid transaminase (IlvE) from Mycobacterium tuberculosis.
Uterine Cervical Neoplasms
[The Expression and Significance of c-myc and bcat1 in Cervical Cancer].
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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
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
0.56
isoleucine
-
pH 8.4, 25°C, 2-oxoglutarate as amino group acceptor
1.54
L-alloisoleucine
-
pH 8.4, 25°C, 2-oxoglutarate as amino group acceptor
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
0.09
(S)-3-methyl-2-oxopentanoate
-
pH 8.3, 37°C, leucine as amino group donor
0.17
(S)-3-methyl-2-oxopentanoate
-
pH 8.0, 25°C, substrate L-glutamate
1
2-oxoglutarate
-
pH 8.0, 37°C, isoenzyme III, leucine as amino group donor
1.1
2-oxoglutarate
-
pH 8.0, 37°C, isoenzyme III, isoleucine as amino group donor
1.52
2-oxoglutarate
-
pH 8.3, 37°C, leucine as amino group donor
1.7
2-oxoglutarate
-
pH 8.0, 37°C, isoenzyme III, valine as amino group donor
2.4
2-oxoglutarate
-
pH 8.4, 25°C, substrate L-alloisoleucine
4
2-oxoglutarate
-
pH 8.4, 25°C, valine as amino group donor
4.8
2-oxoglutarate
-
pH 8.0, 37°C, isoenzyme I, isoleucine as amino group donor
5
2-oxoglutarate
-
pH 8.0, 37°C, isoenzyme I, valine as amino group donor
5.5
2-oxoglutarate
-
pH 8.4, 25°C, isoleucine as amino group donor
7.6
2-oxoglutarate
-
pH 8.0, 37°C, isoenzyme I, leucine as amino group donor
0.11
glyoxylate
-
wild-type, pH 7.4, 25°C
0.26
glyoxylate
-
TAT-peptide fusion protein, pH 7.4, 25°C
35
L-alanine
-
wild-type, pH 7.4, 25°C
74
L-alanine
-
TAT-peptide fusion protein, pH 7.4, 25°C
4.5
L-glutamate
-
pH 8.0, 25°C, (R)-3-methyl-2-oxopentanoate as amino group acceptor
10.4
L-glutamate
-
pH 8.0, 25°C, 3-methyl-2-oxobutanoate as amino group acceptor
18.1
L-glutamate
-
pH 8.3, 37°C, 4-methyl-2-oxopentanoate as amino group acceptor
21.3
L-glutamate
-
pH 8.0, 25°C, (S)-3-methyl-2-oxopentanoate as amino group acceptor
28.3
L-glutamate
-
pH 8.0, 25°C, 4-methyl-2-oxopentanoate as amino group acceptor
3
L-isoleucine
-
pH 8.0, 37°C, isoenzyme III, 2-oxoglutarate as amino group acceptor
10.3
L-isoleucine
-
pH 8.0, 37°C, isoenzyme I, 2-oxoglutarate as amino group acceptor
0.62
L-leucine
-
pH 8.4, 25°C, 2-oxoglutarate as amino group acceptor
6.8
L-leucine
-
pH 8.0, 37°C, isoenzyme III, 2-oxoglutarate as amino group acceptor
25
L-leucine
-
pH 8.0, 37°C, isoenzyme I, 2-oxoglutarate as amino group acceptor
2.96
L-valine
-
pH 8.4, 25°C, 2-oxoglutarate as amino group acceptor
8.3
L-valine
-
pH 8.0, 37°C, isoenzyme III, 2-oxoglutarate as amino group acceptor
30.8
L-valine
-
pH 8.0, 37°C, isoenzyme I, 2-oxoglutarate as amino group acceptor
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malfunction
mutation of the redox sensor (Cys315) results in a significant loss of activity, with no loss of activity reported on the mutation of the resolving cysteine (Cys318), which allows the reversible formation of a disulfide bond between Cys315 and Cys318
metabolism
the enzyme is part of the branched-chain amino acids metabolism, redox regulation of BCAT, detailed overview. Redox regulation of BCATm is important for substrate channelling. For association to occur, BCATm needs to be in its reduced-PLP form and both proteins in their open structure. In the PLP-form, binding of BCATm to E1 increases the kinetic rate of decarboxylation of the BCKAs, whereas no binding occurs when BCATm is in the PMP form
physiological function
human branched-chain aminotransferase (hBCAT) catalyzes the transamination of the branched-chain amino acids leucine, valine and isoleucine and 2-oxoglutarate to their respective 2-oxo acids and glutamate. hBCAT activity is regulated by a CXXC center located approx. 10 A from the active site. This redox-active center facilitates recycling between the reduced and oxidized states, representing hBCAT in its active and inactive forms, respectively. The structure reveals the modified CXXC center in a conformation similar to that in the oxidized wild type, supporting the notion that its regulatory mechanism depends on switching the Cys315 side chain between active and inactive conformations. The enzyme plays a significant role in amino-acid metabolism and whole-body nitrogen shuttling, in particular with respect to the de novo synthesis of the neurotransmitter glutamate in the brain
physiological function
human mitochondrial branched-chain amino acid aminotransferase 2 is a putative factor of resistance of glioblastoma to standard-of-care-treatments. The enzyme generates glutamate, which is neurotoxic
physiological function
the BCAT proteins have been assigned an additional thiol oxidoreductase activity that can accelerate the refolding of proteins, in particular when S-glutathionylated, supporting a chaperone role for BCAT in protein folding. Interplay of the redox regulation of BCAT with important cell signalling mechanisms. The two isozymes BCAT1 and 2 have similar substrate specificities, but their regulation, tissue specific expression and compartmentation together with their response to different redox environments point to alternate functions for these proteins. The mitochondrial form is responsible for the majority of transamination in the body due to its ubiquitous expression in almost every tissue excluding the liver. High levels of BCAAs may exacerbate the generation of sorbitol accumulation. Moreover, increased levels of BCAAs have also been shown to reduce fatty acid oxidation in muscles, leading to the accumulation of acylcarnitines and insulin resistance. The metabolic imbalances include a role of BCATm and its regulation through changes in the redox environment. BCAT enhances the overall PDI activity and increases the rate of refolding. BCATm may be a chaperone for PDI operating through a thiol disulfide exchange mechanism or independently as an oxidoreductase regulated through the redox environment. BCATm may operate in a neuroprotective capacity, as an auxiliary mechanism to the endothelial system to support glutamate efflux. The redox state of BCAT signals differential phosphorylation by protein kinase C regulating the trafficking of cellular pools of BCAT
malfunction
knockdown of BCAT1 represses the growth rate and colony formation capacity of breast cancer cells, opposing results are observed when BCAT1 is overexpressed. BCAT1 can promote mitochondrial biogenesis, ATP production and repress mitochondrial ROS in breast cancer cells by regulating the expression of related genes. BCAA catabolism is activated in human breast cancer, and abolishment of BCAA catabolism by knocking down BCAT1 inhibits breast cancer cell growth by repressing mTOR-mediated mitochondrial biogenesis and function. BCAT1 overexpression is unable to affect the mRNA levels of the genes involved in mitochondrial biogenesis (PGC1alpha, NRF-1, Tfam, and beta-F1-ATPase) and oxidative stress (SOD1, SOD2, catalase, and Gpx1)
malfunction
with respect to BCATc, single point mutations of all six detectable thiols show that those in the CXXC motif, C335 and C338, have the most impact on BCAT activity. Steady state kinetics show that mutation of the thiol at position C335 had the largest effect relative to all other single point mutations. For all amino acid substrates there is a significant decrease in kcat/Km values. The other non-CXXC cysteine mutants show differential effects on turnover, with the most significant observed for C221S. When the thiol at position C338 is substituted an increase in peroxide sensitivity is observed, indicating that C335 is the redox sensor
metabolism
levels of branched-chain amino acids (BCAAs: leucine, isoleucine, and valine) are significantly upregulated in the serum of patients with breast cancer compared with healthy donors. Also the mRNA levels of BCAT1, BCAT2, mitochondrial targeted 2C-type serine/threonine protein phosphatase (PP2Cm), branched chain keto acid dehydrogenase E1, alpha polypeptide (BCKDHA), BCKDHB, and enoyl-CoA hydratase, short chain 1 (ECHS1) are increased in human breast cancer tissues compared with matched adjacent normal tissues
metabolism
the enzyme is part of the branched-chain amino acids metabolism, redox regulation of BCAT, residue C335 is the redox sensor, detailed overview. Like whole body transamination, neurotransmitter synthesis can be finely regulated through dietary BCAAs. S-glutathionylation of BCATc is a mechanism to preserve BCAT integrity under cellular stress
physiological function
branched-chain amino acids (BCAAs) are important nutrient signals that have direct and indirect effects. BCAA catabolism is a conserved regulator of physiological aging and participates in diverse physiological and pathological processes, including carcinoma development. BCAA catabolism is involved in human breast cancer. The plasma and tissue levels of BCAAs are increased in breast cancer, which is accompanied by the elevated expression of the catabolic enzymes, including branched-chain amino acid transaminase 1 (BCAT1). BCAT1 promotes the growth of breast cancer cells through improving mTOR-mediated mitochondrial biogenesis and function. BCAT1 activates the mTOR, but not AMPK or SIRT1, signaling to promote mitochondrial biogenesis and function, and subsequently facilitates growth and colony formation of breast cancer cells. BCAA catabolism is activated in human breast cancer. Isozyme BCAT1 promotes growth and colony formation of breast cancer cells
physiological function
the BCAT proteins have been assigned an additional thiol oxidoreductase activity that can accelerate the refolding of proteins, in particular when S-glutathionylated, supporting a chaperone role for BCAT in protein folding. Interplay of the redox regulation of BCAT with important cell signalling mechanisms. The two isozymes BCAT1 and 2 have similar substrate specificity, but their regulation, tissue specific expression and compartmentation together with their response to different redox environments point to alternate functions for these proteins. In human brain, BCATc is solely expressed in glutamatergic and GABAergic neurons in all brain regions examined. In the hippocampal and temporal region of the brain, intense staining of BCATc is reported in the neuronal cell bodies indicating that the role of BCATc is to contribute to the glutamate pool rather than excitation. A role in neurotransmitter release during excitation is also proposed as BCATc is localised along the axons. Roles of isozyme BCAT1 in cancer, detailed overview
additional information
active site structure
additional information
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active site structure
additional information
in silico structural homology modeling reveals that the Lys59 side-chain of BCAT2 may repulse the Arg186 in the variant protein (PDB ID 5MPR), leading to destabilization of the protein dimer and altered enzyme kinetics
additional information
-
in silico structural homology modeling reveals that the Lys59 side-chain of BCAT2 may repulse the Arg186 in the variant protein (PDB ID 5MPR), leading to destabilization of the protein dimer and altered enzyme kinetics
additional information
the redox active CXXC motif is unique to the branched-chain aminotransferase (BCAT) proteins. The CXXC motif is at the heart of the catalytic center and functions through thiol disulfide exchange. Importance of the CXXC motif in regulating BCAT activity under hypoxic conditions, a characteristic of tumours. The key active-site residues involved in substrate and PLP binding are identical between isoforms, with the exception of one residue (Val336 in BCATc is Gln in BCATm), which does not explain the catalytic or regulatory differences presented for the BCAT proteins. BCATs contain a redox active CXXC center, analysis of the functional role
additional information
the redox active CXXC motif is unique to the branched-chain aminotransferase (BCAT) proteins. The CXXC motif is at the heart of the catalytic center and functions through thiol disulfide exchange. Importance of the CXXC motif in regulating BCAT activity under hypoxic conditions, a characteristic of tumours. The key active-site residues involved in substrate and PLP binding are identical between isoforms, with the exception of one residue (Val336 in BCATc is Gln in BCATm), which does not explain the catalytic or regulatory differences presented for the BCAT proteins. BCATs contain a redox active CXXC center, analysis of the functional role
additional information
the redox active CXXC motif is unique to the branched-chain aminotransferase (BCAT) proteins, the CXXC motif is at the heart of the catalytic center and functions through thiol disulfide exchange. Importance of the CXXC motif in regulating BCAT activity under hypoxic conditions, a characteristic of tumours. The key active-site residues involved in substrate and PLP binding are identical between isoforms, with the exception of one residue (Val336 in BCATc is Gln in BCATm), which does not explain the catalytic or regulatory differences presented for the BCAT proteins. BCATs contain a redox active CXXC center, analysis of the functional role
additional information
the redox active CXXC motif is unique to the branched-chain aminotransferase (BCAT) proteins, the CXXC motif is at the heart of the catalytic center and functions through thiol disulfide exchange. Importance of the CXXC motif in regulating BCAT activity under hypoxic conditions, a characteristic of tumours. The key active-site residues involved in substrate and PLP binding are identical between isoforms, with the exception of one residue (Val336 in BCATc is Gln in BCATm), which does not explain the catalytic or regulatory differences presented for the BCAT proteins. BCATs contain a redox active CXXC center, analysis of the functional role
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