Information on EC 2.6.1.1 - aspartate transaminase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


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

EC NUMBER
COMMENTARY
2.6.1.1
-
RECOMMENDED NAME
GeneOntology No.
aspartate transaminase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate
show the reaction diagram
bi bi ping pong reaction kinetic
-
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate
show the reaction diagram
bi bi ping pong reaction kinetic
-
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate
show the reaction diagram
bi bi ping pong reaction kinetic
-
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate
show the reaction diagram
bi bi ping pong reaction kinetic
-
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate
show the reaction diagram
bi bi ping pong reaction kinetic
-
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate
show the reaction diagram
mechanism
-
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate
show the reaction diagram
bi bi ping pong reaction kinetic
-
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate
show the reaction diagram
bi bi ping pong reaction kinetic
-
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate
show the reaction diagram
bi bi ping pong reaction kinetic
-
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate
show the reaction diagram
intermediate formation; mechanism
-
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate
show the reaction diagram
bi bi ping pong reaction kinetic
-
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate
show the reaction diagram
active site structure, substrate recognition mechanism
-
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate
show the reaction diagram
active site structure, substrate recognition mechanism
Q56232
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate
show the reaction diagram
bi bi ping pong reaction kinetic
-
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate
show the reaction diagram
bi bi ping pong reaction kinetic
-
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate
show the reaction diagram
bi bi ping pong reaction kinetic
-
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate
show the reaction diagram
bi bi ping pong reaction kinetic
Chlamydomonas reinhardtii 6145c, Trichomonas vaginalis Bushby
-
-
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
amino group transfer
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
(R)-cysteate degradation
-
anaerobic energy metabolism (invertebrates, cytosol)
-
asparagine degradation III (mammalian)
-
aspartate biosynthesis
-
aspartate degradation I
-
aspartate degradation II
-
C4 photosynthetic carbon assimilation cycle, NAD-ME type
-
C4 photosynthetic carbon assimilation cycle, PEPCK type
-
coenzyme M biosynthesis II
-
glutamate degradation II
-
phenylalanine degradation IV (mammalian, via side chain)
-
sulfolactate degradation III
-
TCA cycle VI (obligate autotrophs)
-
Alanine, aspartate and glutamate metabolism
-
Cysteine and methionine metabolism
-
Arginine and proline metabolism
-
Tyrosine metabolism
-
Phenylalanine metabolism
-
Phenylalanine, tyrosine and tryptophan biosynthesis
-
Novobiocin biosynthesis
-
Carbon fixation in photosynthetic organisms
-
Isoquinoline alkaloid biosynthesis
-
Tropane, piperidine and pyridine alkaloid biosynthesis
-
Metabolic pathways
-
Biosynthesis of secondary metabolites
-
Microbial metabolism in diverse environments
-
SYSTEMATIC NAME
IUBMB Comments
L-aspartate:2-oxoglutarate aminotransferase
A pyridoxal-phosphate protein. Also acts on L-tyrosine, L-phenylalanine and L-tryptophan. Aspartate transaminase activity can be formed from the aromatic-amino-acid transaminase (EC 2.6.1.57) of Escherichia coli by controlled proteolysis [7], some EC 2.6.1.57 activity can be found in this enzyme from other sources [8]; indeed the enzymes are identical in Trichomonas vaginalis [6].
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
2-oxoglutarate-glutamate aminotransferase
-
-
-
-
AAT
-
-
-
-
AAT
Q4LDF8
-
AAT
P00509
-
AAT
Q5F4K8
-
AAT
Spirodela polyrhiza SJ
-
-
-
AAT
-
-
aatB3
Q939C9
-
aminotransferase, aspartate
-
-
-
-
AsAT
-
-
aspartate alpha-ketoglutarate transaminase
-
-
-
-
aspartate aminotransferase
-
-
-
-
aspartate aminotransferase
Q9SIE1
-
aspartate aminotransferase
-
-
aspartate aminotransferase
Q4LDF8
-
aspartate aminotransferase
-
-
aspartate aminotransferase
-
-
aspartate aminotransferase
-
-
aspartate aminotransferase
-
-
aspartate aminotransferase
-
-
aspartate aminotransferase
-
-
aspartate aminotransferase
Q5F4K8
-
aspartate aminotransferase
-
-
aspartate aminotransferase
-
-
aspartate aminotransferase
-
-
aspartate aminotransferase
-
-
aspartate aminotransferase
Spirodela polyrhiza SJ
-
-
-
aspartate aminotransferase
-
-
aspartate aminotransferase
P14909
-
aspartate aminotransferase
-
-
aspartate aminotransferase
Q7ZTK9
-
aspartate transaminase
-
-
aspartate, 2-oxoglutarate aminotransferase
-
-
aspartate-2-oxoglutarate transaminase
-
-
-
-
aspartate/(R)-cysteate:2-oxoglutarate aminotransferase
-
-
aspartate/tyrosine/phenylalanine pyridoxal-5'-phosphate-dependent aminotransferase
-
-
aspartate:2-oxoglutarate amino-transferase
-
-
aspartate:2-oxoglutarate aminotransferase
-
-
-
-
aspartic acid aminotransferase
-
-
-
-
aspartic aminotransferase
-
-
-
-
aspartyl aminotransferase
-
-
-
-
AspAT
P00509
-
AspAT
-
-
AspAT
Haloferax mediterranei R-4
-
-
-
AspAT
-
-
AspAT
O96142
-
AspAT
Pseudoalteromonas haloplanktis TAC 125
-
-
-
AspATSs
P14909
-
AspATSs
Sulfolobus solfataricus MT-4
-
-
-
AspT
-
-
-
-
AST
-
-
-
-
AST
Q4LDF8
-
AST
P00507
-
AST
-
-
AST-Bb
-
-
C-S lyase
P00507
-
EcAspAT
P00509
wild-type enzyme shows weak desulfination activity and decarboxylation activity
glutamate oxaloacetate transaminase
-
-
-
-
glutamate-oxalacetate aminotransferase
-
-
-
-
glutamate-oxalate transaminase
-
-
-
-
glutamic oxalic transaminase
-
-
-
-
glutamic oxaloacetic transaminase
-
-
glutamic-aspartic aminotransferase
-
-
-
-
glutamic-aspartic transaminase
-
-
-
-
glutamic-oxalacetic transaminase
-
-
-
-
glutamic-oxaloacetic transaminase
-
-
-
-
GOT
Q4LDF8
-
GOT
Hypocrea rufa
-
-
GOT
P00507
-
GOT
-
-
GOT (enzyme)
-
-
-
-
L-aspartate aminotransferase
-
-
L-aspartate aminotransferase
Escherichia coli TY103
-
-
-
L-aspartate transaminase
-
-
-
-
L-aspartate-2-ketoglutarate aminotransferase
-
-
-
-
L-aspartate-2-oxoglutarate aminotransferase
-
-
-
-
L-aspartate-2-oxoglutarate-transaminase
-
-
-
-
L-aspartate-alpha-ketoglutarate transaminase
-
-
-
-
L-aspartate:2-oxoglutarate aminotransferase
-
-
L-aspartateartate aminotransferase
P00509
-
L-aspartic aminotransferase
-
-
-
-
L-AspAT
D3H0F7
-
oxaloacetate transferase
-
-
-
-
oxaloacetate-aspartate aminotransferase
-
-
-
-
plastid aspartate aminotransferase
-
-
protein TT0402
-
-
SsAspAT
-, P14909
-
transaminase A
-
-
-
-
additional information
-
aspartate aminotransferases are divided into 2 subgroups: subgroup Ia, inclusive the enzyme of Escherichia coli, posses Arg292 for substrate binding and show a specificity for acidic substrates only, subgroup Ib, inclusive the enzyme of Thermus thermophilus, can utilize acidic as well as neutral substrates
additional information
-
EC 2.6.1.57 may be converted to EC 2.6.1.1 by controlled proteolysis with subtilisin, the 2 enzymes are encoded by 2 different genes with high sequence homology
additional information
-
aspartate aminotransferases are divided into 2 subgroups: subgroup Ia, inclusive the enzyme of Escherichia coli, posses Arg292 for substrate binding and show a specificity for acidic substrates only, subgroup Ib, inclusive the enzyme of Thermus thermophilus, can utilize acidic as well as neutral substrates
CAS REGISTRY NUMBER
COMMENTARY
9000-97-9
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
2 genotypes
-
-
Manually annotated by BRENDA team
3 genes encoding 3 different isozymes: asp1 is mitochondrial, asp3 is amyloplastidic and asp2 is cytosolic
-
-
Manually annotated by BRENDA team
2 major isozymes: Asp-DEAE-1 and Asp-DEAE-2
-
-
Manually annotated by BRENDA team
2 isozymes; var. Lodi
-
-
Manually annotated by BRENDA team
strain YM-2
-
-
Manually annotated by BRENDA team
strain YM-2
-
-
Manually annotated by BRENDA team
Bradyrhizobium japonicum 392
strain 392
-
-
Manually annotated by BRENDA team
cytosolic and mitochondrial isozymes; mongrel dogs
-
-
Manually annotated by BRENDA team
Chlamydomonas reinhardtii 6145c
strain 6145c
-
-
Manually annotated by BRENDA team
fragment
UniProt
Manually annotated by BRENDA team
cytosolic form I, and mitochondrial forms II and III
-
-
Manually annotated by BRENDA team
dolphin
cytosolic and mitochondrial isozyme
-
-
Manually annotated by BRENDA team
isoenzymes: AspAT-1, AspAT-2, AspAT-3
-
-
Manually annotated by BRENDA team
B; isoenzymes A and B
-
-
Manually annotated by BRENDA team
mutant K258A
-
-
Manually annotated by BRENDA team
mutant V39L
-
-
Manually annotated by BRENDA team
Escherichia coli TY103
-
-
-
Manually annotated by BRENDA team
cytosolic and mitochondrial isozymes
-
-
Manually annotated by BRENDA team
different molecular forms: alpha, beta, gamma, delta, epsilon
-
-
Manually annotated by BRENDA team
3 isozymes: 2 cytosolic, 1 mitochondrial
-
-
Manually annotated by BRENDA team
strain R-4, ATCC 33500
-
-
Manually annotated by BRENDA team
Haloferax mediterranei R-4
strain R-4, ATCC 33500
-
-
Manually annotated by BRENDA team
cytosolic isozyme
-
-
Manually annotated by BRENDA team
4 isozymes: AST I , AST II, AST III, AST IV; camel tick
-
-
Manually annotated by BRENDA team
Hypocrea rufa
-
-
-
Manually annotated by BRENDA team
Leptosphaeria michotii
2 isozymes A and B
-
-
Manually annotated by BRENDA team
grey mullet, Osteichthyes
-
-
Manually annotated by BRENDA team
2 isozymes: AAT1 and AAT2; cv. Estoril
-
-
Manually annotated by BRENDA team
2 cytosolic isozymes: AAT-P1 and AAT-P2; cv. Uniharvest
-
-
Manually annotated by BRENDA team
2 cytosolic isozymes: AAT-1 and AAT-2, the latter has the 3 forms AAT-2a, AAT-2b, AAT-2c
-
-
Manually annotated by BRENDA team
2 isozymes; Jacq. var. trichoglume Eyles
-
-
Manually annotated by BRENDA team
DSM 6457; strain SF-4; strains FTF-INRA, DSM 3012
-
-
Manually annotated by BRENDA team
Methanothermobacter thermautotrophicus SF-4
strain SF-4
-
-
Manually annotated by BRENDA team
cytosolic and mitochondrial isozyme
-
-
Manually annotated by BRENDA team
2 isoenzymes: AAT-1, AAT-2; cv. Koganemasari
-
-
Manually annotated by BRENDA team
cytosolic and mitochondrial isozymes
-
-
Manually annotated by BRENDA team
cytosolic isozyme
-
-
Manually annotated by BRENDA team
at least 3 isozymes: inducible cytosolic cAspAT and mitochondrial mAspAT, and a constitutive minor plastidic pAspAT
-
-
Manually annotated by BRENDA team
; prokaryotic-type isoform
-
-
Manually annotated by BRENDA team
Pseudoalteromonas haloplanktis TAC 125
strain TAC 125
-
-
Manually annotated by BRENDA team
strain IFO 12996
-
-
Manually annotated by BRENDA team
Pseudomonas putida IFO 12996
strain IFO 12996
-
-
Manually annotated by BRENDA team
cytosolic and mitochondrial isozyme
-
-
Manually annotated by BRENDA team
cytosolic and mitochondrial isozyme; male Wistar rats
-
-
Manually annotated by BRENDA team
male Wistar rats; purified cytosolic isozyme
-
-
Manually annotated by BRENDA team
mature mitochondrial isozyme mAAT
SwissProt
Manually annotated by BRENDA team
mitochondrial isozyme mAspAT
-
-
Manually annotated by BRENDA team
purified premature mitochondrial isozyme pmAAT
-
-
Manually annotated by BRENDA team
cytosolic and mitochondrial isozyme
-
-
Manually annotated by BRENDA team
clam, mollusca: Bivalvia
-
-
Manually annotated by BRENDA team
strain SJ
-
-
Manually annotated by BRENDA team
Spirodela polyrhiza SJ
strain SJ
-
-
Manually annotated by BRENDA team
strain MT4
SwissProt
Manually annotated by BRENDA team
Sulfolobus solfataricus MT-4
-
-
-
Manually annotated by BRENDA team
Sulfolobus solfataricus MT4
strain MT4
SwissProt
Manually annotated by BRENDA team
cytosolic and mitochondrial isozyme
-
-
Manually annotated by BRENDA team
mitochondrial isozyme
-
-
Manually annotated by BRENDA team
purified cytosolic isozyme
-
-
Manually annotated by BRENDA team
strain HB8
-
-
Manually annotated by BRENDA team
strain HB8
Uniprot
Manually annotated by BRENDA team
Torulopsis candida
cytosolic and mitochondrial isozyme
-
-
Manually annotated by BRENDA team
Bushby strain
-
-
Manually annotated by BRENDA team
Trichomonas vaginalis Bushby
Bushby strain
-
-
Manually annotated by BRENDA team
cytosolic isoform
UniProt
Manually annotated by BRENDA team
mitochondrial isoform
UniProt
Manually annotated by BRENDA team
cytosolic isoform
UniProt
Manually annotated by BRENDA team
mitochondrial isoform
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
-
a cold-sensitive mutant is generated by transposon mutagenesis. The mutated gene in CSM2 is identified as AAT. Complementation of AAT in CSM2 restores the original phenotype as in the wild-type cells
physiological function
Q7ZTK9
involved in liver glyceroneogenesis
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(2R,3R)-beta-chloroalanine + 2-mercaptoethanol
3-(2-hydroxyethyl)-cysteine + HCl
show the reaction diagram
Escherichia coli, Escherichia coli TY103
-
beta-substitution, reaction occurs with retention of stereochemistry
-
-
?
(2R,3S)-beta-chloroalanine + 2-mercaptoethanol
(2R,3S)-3-(2-hydroxyethyl)-cysteine + HCl
show the reaction diagram
Escherichia coli, Escherichia coli TY103
-
-
-
-
?
2,4-diaminobutyric acid + 2-oxoglutarate
?
show the reaction diagram
-
-
-
-
?
2-aminohexanedioic acid + 2-oxoglutarate
2-oxohexanedioic acid + L-glutamate
show the reaction diagram
-
i.e. alpha-aminoadipic acid
-
-
?
3-aminopropanesulfonate + 2-oxoglutarate
?
show the reaction diagram
-
3-aminopropanesulfonate = homotaurine, lower activity compared to L-cysteate
-
-
?
glycine + 2-oxoglutarate
glyoxylate + L-glutamate
show the reaction diagram
Hypocrea rufa
-
7.7% of the activity with aspartate
-
-
?
L-2-amino-4-methoxy-4-oxobutanoic acid + 2-oxoglutarate
4-methoxy-2,4-dioxobutanoic acid + L-glutamate
show the reaction diagram
-
isozymes AAT1 and AAT2, the latter shows lower activity
-
-
?
L-2-amino-4-methoxy-4-oxobutanoic acid + oxaloacetate
4-methoxy-2,4-dioxobutanoic acid + L-aspartate
show the reaction diagram
-
isozymes AAT1 and AAT2, low activity
-
-
?
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
show the reaction diagram
Q56232
-
-
r
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
show the reaction diagram
-
-
-
-
?
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
show the reaction diagram
Hypocrea rufa
-
7.7% of the activity with aspartate
-
-
?
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
show the reaction diagram
-
activity is not affected by the presence of formate
-
-
?
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
show the reaction diagram
-
0.7% of the activity with L-aspartate
-
-
?
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
show the reaction diagram
Trichomonas vaginalis Bushby
-
-
-
-
?
L-asparagine + 2-oxoglutarate
4-amino-2,4-dioxobutanoate + 2-glutamate
show the reaction diagram
O96142
specific activity: 0.14 micromol/min/mg
-
-
?
L-aspartate + 2-oxobutyrate
oxaloacetate + 2-aminobutyrate
show the reaction diagram
-
0.4% activity compared to 2-oxoglutarate
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
Q56232
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
r
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
P00509
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
r
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
r
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
r
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
r
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
r
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
r
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
P00509
-
-
r
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
r
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
r
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
-
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
P00507, -
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
r
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
-
r
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?, r
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?, r
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?, r
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
r
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
r
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
Leptosphaeria michotii
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
Torulopsis candida
-
-
-
?, r
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
-
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
r
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
P14909, -
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
-
r
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
Hypocrea rufa
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?, r
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?, r
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
r
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?, r
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
dolphin
-
-
-
r
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-, Q4LDF8
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
Q5F4K8
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
Q9SIE1
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
-
r
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
Q4D080, Q4D1Q4
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
Q964F0, Q964F1
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
D3H0F7
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
34% of the activity with glutamate
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
30% of the activity with glutamate
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
Q56232
enzyme can also act on neutral amino acid substrates due to a substrate-binding pocket with a more flexible conformation, Lys109 is the major determinant for the acidic substrate specificity
-
r
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
absolute specificity for aspartate and 2-oxoglutarate and for glutamate and oxaloacetate
-
r
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
P14909, -
48% of the activity with cysteine sulfinic acid
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
isozyme Asp-DEAE-1 performs preferably the reverse reaction, isozyme the forward reaction
-
r
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
25.2% of the activity with glutamate
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
2-oxoglutarate is the best acceptor substrate, 45% activity with L-aspartate compared to L-glutamate
-
r
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
Hypocrea rufa
-
best amino acid donor
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
best amino acid donor of cytosolic enzyme
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
key enzyme in assimilation of C and N compounds
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
dolphin
-
role in energy metabolism of diving animals
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
enzyme plays the most important role in amino acid metabolism
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
enzyme plays a central role in nitrogen metabolism of cells
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
enzyme plays an important role in numerous metabolic processes
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
anti-enzyme antibodies selectively inhibit the uptake of oleate in 3T3-L1 adipocytes by 31-55%, but only poorly in fibroblasts, the antibodies have no effect on uptake of 2-deoxyglucose and octanoate
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
function in C4 acid pathway
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
hyperprolinemia type II is an autosomal recessive disorder caused by severe deficiency of enzyme DELTA1-pyrroline-5-carboxylic acid dehydrogenase leading to tissue accumulation of proline. Proline has direct inhibitory effect on aspartate transaminase activity of different brain regions leading to lesser synthesis of glutamate thereby causing neurological dysfunctions
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
reaction mechanism, the strain (unfavourable interaction) of the distorted internal aldimine in the unliganded enzyme is crucial for catalysis. The true driving forces are the strain energy inherent to the respective intermediates. It is described how these strain energies are generated and are used for catalysis
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
aspartate aminotransferase from Sulfolobus solfataricus does not possess any arginine residue exposed to chemical modifications responsible for the binding of omega-carboxylate of the substrates
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
Q939C9
relative activity L-aspartate: 100%
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
O96142
specific activity: 2.67 micromol/min/mg
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
Pseudoalteromonas haloplanktis TAC 125
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
Bradyrhizobium japonicum 392
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
Spirodela polyrhiza SJ
-
-
-
-
r
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
Methanothermobacter thermautotrophicus SF-4
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
Methanothermobacter thermautotrophicus SF-4
-
-, 25.2% of the activity with glutamate
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
Chlamydomonas reinhardtii 6145c
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
Haloferax mediterranei R-4
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
Haloferax mediterranei R-4
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
Pseudomonas putida IFO 12996
-
34% of the activity with glutamate, enzyme plays the most important role in amino acid metabolism
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
Trichomonas vaginalis Bushby
-
-
-
?, r
L-aspartate + 2-oxoisocaproate
oxaloacetate + L-leucine
show the reaction diagram
-
1.0% activity compared to 2-oxoglutarate
-
-
?
L-aspartate + 4-hydroxyphenylpyruvate
oxaloacetate + L-tyrosine
show the reaction diagram
Torulopsis candida
-
1.48% of the activity with 2-oxoglutarate
-
-
?
L-aspartate + oxaloacetate
?
show the reaction diagram
Q939C9
relative activity compared to 2-oxoglutarate: 81.5%
-
-
?
L-aspartate + phenylpyruvate
oxaloacetate + L-phenylalanine
show the reaction diagram
-
-
-
-
?
L-aspartate + phenylpyruvate
oxaloacetate + L-phenylalanine
show the reaction diagram
-
no activity
-
-
-
L-aspartate + phenylpyruvate
oxaloacetate + L-phenylalanine
show the reaction diagram
Torulopsis candida
-
7.12% of the activity with 2-oxoglutarate
-
-
?
L-aspartate + pyruvate
oxaloacetate + L-alanine
show the reaction diagram
-
1.9% activity compared to 2-oxoglutarate
-
-
?
L-cysteate + 2-oxoglutarate
3-sulfopyruvate + L-glutamate
show the reaction diagram
-
L-cysteate = (R)-cysteate
-
-
?
L-cysteate + oxaloacetate
?
show the reaction diagram
-
-
-
-
?
L-cysteate + pyruvate
?
show the reaction diagram
-
-
-
-
?
L-cysteic acid + 2-oxoglutarate
2-oxo-3-sulfopropionate + L-glutamate
show the reaction diagram
-
no activity
-
-
-
L-cysteic acid + 2-oxoglutarate
2-oxo-3-sulfopropionate + L-glutamate
show the reaction diagram
-
i.e. 2-amino-2-sulfopropionate
-
-
?
L-cysteine + 2-oxoglutarate
2-oxopropionate + L-glutamate
show the reaction diagram
-
-
-
-
?
L-cysteine + 2-oxoglutarate
2-oxopropionate + L-glutamate
show the reaction diagram
Hypocrea rufa
-
26.2% of the activity with L-aspartate
-
-
?
L-cysteine + 2-oxoglutarate
2-oxopropionate + L-glutamate
show the reaction diagram
Methanothermobacter thermautotrophicus SF-4
-
-
-
-
?
L-cysteine sulfinic acid + 2-oxoglutarate
2-oxo-3-sulfinopropionic acid + L-glutamate
show the reaction diagram
-
-
-
-
?
L-cysteine sulfinic acid + 2-oxoglutarate
2-oxo-3-sulfinopropionic acid + L-glutamate
show the reaction diagram
-
-
-
-
ir
L-cysteine sulfinic acid + 2-oxoglutarate
2-oxo-3-sulfinopropionic acid + L-glutamate
show the reaction diagram
P14909, -
-
-
-
?
L-cysteine sulfinic acid + 2-oxoglutarate
2-oxo-3-sulfinopropionic acid + L-glutamate
show the reaction diagram
-
-
-
-
?
L-cysteine sulfinic acid + 2-oxoglutarate
2-oxo-3-sulfinopropionic acid + L-glutamate
show the reaction diagram
-
63% of the activity with aspartate
-
-
?
L-cysteine sulfinic acid + 2-oxoglutarate
2-oxo-3-sulfinopropionic acid + L-glutamate
show the reaction diagram
-
best amino acid donor for mitochondrial enzyme
-
-
?
L-cysteine sulfinic acid + 2-oxoglutarate
2-oxo-3-sulfinopropionic acid + L-glutamate
show the reaction diagram
-
21% of the activity with L-glutamate
-
-
?
L-cysteine sulfinic acid + 2-oxoglutarate
2-oxo-3-sulfinopropionic acid + L-glutamate
show the reaction diagram
Leptosphaeria michotii
-
only isozyme B, 27% activity compared to L-aspartate
-
-
?
L-cysteine sulfinic acid + 2-oxoglutarate
2-oxo-3-sulfinopropionic acid + L-glutamate
show the reaction diagram
-
48% of the activity with L-glutamate
-
-
?
L-cysteine sulfinic acid + 2-oxoglutarate
2-oxo-3-sulfinopropionic acid + L-glutamate
show the reaction diagram
-
27% activity compared to L-glutamate
-
-
?
L-cysteine sulfinic acid + 2-oxoglutarate
2-oxo-3-sulfinopropionic acid + L-glutamate
show the reaction diagram
Sulfolobus solfataricus MT-4
-
-
-
-
?
L-cysteine sulfinic acid + 2-oxoglutarate
2-oxo-3-sulfinopropionic acid + L-glutamate
show the reaction diagram
Methanothermobacter thermautotrophicus SF-4
-
-
-
-
?
L-cysteine sulfinic acid + 2-oxoglutarate
2-oxo-3-sulfinopropionic acid + L-glutamate
show the reaction diagram
Pseudomonas putida IFO 12996
-
21% of the activity with L-glutamate
-
-
?
L-cysteine sulfinic acid + 2-oxoglutarate
2-oxo-3-sulfinopropionic acid + L-glutamate
show the reaction diagram
-
-
-
-
ir
L-erythro-3-hydroxyaspartate + 2-oxoglutarate
erythro-3-hydroxy-2-oxoaspartate + L-glutamate
show the reaction diagram
-
high stabilization of the quinonoid intermediate formed by L-erythro-3-hydroxyaspartate and pyridoxal 5'-phosphate at the active site via Tyr70, kinetic analysis, wild-type, no activity with mutant T70F
-
-
?
L-glutamate + 2-oxoglutarate
2-oxoglutarate + L-glutamate
show the reaction diagram
-
-
-
-
?
L-glutamate + 2-oxoglutarate
2-oxoglutarate + L-glutamate
show the reaction diagram
-
-
-
-
?
L-glutamate + 2-oxoglutarate
2-oxoglutarate + L-glutamate
show the reaction diagram
-
L-glutamate is best amino acid donor
-
-
?
L-glutamate + 2-oxoglutarate
2-oxoglutarate + L-glutamate
show the reaction diagram
-
L-glutamate is best amino acid donor
-
-
?
L-glutamate + 2-oxoglutarate
2-oxoglutarate + L-glutamate
show the reaction diagram
-
L-glutamate is best amino acid donor
-
-
?
L-glutamate + 2-oxoglutarate
2-oxoglutarate + L-glutamate
show the reaction diagram
-
L-glutamate is best amino acid donor
-
-
?
L-glutamate + 2-oxoglutarate
2-oxoglutarate + L-glutamate
show the reaction diagram
-
L-glutamate is best amino acid donor
-
-
?
L-glutamate + 2-oxoglutarate
2-oxoglutarate + L-glutamate
show the reaction diagram
dolphin
-
L-glutamate is best amino acid donor
-
-
?
L-glutamate + 2-oxoglutarate
2-oxoglutarate + L-glutamate
show the reaction diagram
P14909, -
25% of the activity with cysteine sulfinic acid
-
-
?
L-glutamate + 2-oxoglutarate
2-oxoglutarate + L-glutamate
show the reaction diagram
-
binding of L-Glu to aspartate aminotransferase to form the Michaelis complex does not induce a conformational change in the enzyme. The conformational change to the closed form occurs during the transaldimination step. The hydrophobic residues of the entrance of the active site, including Tyr70, are considered to be important for promoting the transaldimination process and hence the recognition of the C5 substrate
-
-
?
L-glutamate + 2-oxoglutarate
2-oxoglutarate + L-glutamate
show the reaction diagram
-
the mechanism of the reaction at the early step of the catalysis differs significantly between the substrates L-glutamate and L-aspartate
-
-
?
L-glutamate + 2-oxoglutarate
2-oxoglutarate + L-glutamate
show the reaction diagram
Q939C9
relative activity compared to L-aspartate: 46.7%
-
-
?
L-glutamate + 2-oxoglutarate
2-oxoglutarate + L-glutamate
show the reaction diagram
Methanothermobacter thermautotrophicus SF-4
-
-
-
-
?
L-glutamate + 2-oxoglutarate
2-oxoglutarate + L-glutamate
show the reaction diagram
Methanothermobacter thermautotrophicus SF-4
-
L-glutamate is best amino acid donor
-
-
?
L-glutamate + 2-oxoglutarate
2-oxoglutarate + L-glutamate
show the reaction diagram
Pseudomonas putida IFO 12996
-
L-glutamate is best amino acid donor
-
-
?
L-kynurenine + ?
kynurenic acid + ?
show the reaction diagram
-
-
-
-
?
L-Lys + 2-oxo-4-phenyl-butanoic acid
L-homophenylalanine + 2-keto-6-aminocaproate
show the reaction diagram
-
mutant enzyme R292E/L18H shows a 12.9fold increase in specific activity towards L-Lys and 2-oxo-4-phenylbutanoic acid
2-keto-6-aminocaproate is cyclized nonenzymatically to form DELTA1-piperideine 2-carboxylic acid in the reaction mixture. The low solubility of L-homophenylalanine and spontaneous cyclization of 2-keto-6-aminocaproate drive the reaction completely towards production of L-homophenylalanine
-
?
L-methionine + 2-oxoglutarate
L-glutamate + 4-methylsulfanyl-2-oxobutyric acid
show the reaction diagram
Q4D080, Q4D1Q4
-
-
-
?
L-methionine + 2-oxoglutarate
L-glutamate + 4-methylsulfanyl-2-oxobutyric acid
show the reaction diagram
Q964F0, Q964F1
-
-
-
?
L-methionine + 2-oxoglutarate
L-glutamate + 4-methylsulfanyl-2-oxobutyric acid
show the reaction diagram
-
0.1% activity compared to L-glutamate
-
-
?
L-methionine + 2-oxoglutarate
L-glutamate + 4-methylsulfanyl-2-oxobutyric acid
show the reaction diagram
-
1.0% of the activity with glutamate
-
-
?
L-methionine + 2-oxoglutarate
L-glutamate + 4-methylsulfanyl-2-oxobutyric acid
show the reaction diagram
-
1.0% of the activity with glutamate
-
-
?
L-methionine + 2-oxoglutarate
L-glutamate + 4-methylsulfanyl-2-oxobutyric acid
show the reaction diagram
Hypocrea rufa
-
93% of the activity with aspartate
-
-
?
L-Phe + 2-oxoglutarate
2-oxo-3-phenylpropionic acid + L-glutamate
show the reaction diagram
-
-
-
-
?
L-phenylalanine + 2-oxoglutarate
2-oxo-3-phenylpropionic acid + L-glutamate
show the reaction diagram
dolphin
-
-
-
ir
L-phenylalanine + 2-oxoglutarate
2-oxo-3-phenylpropionic acid + L-glutamate
show the reaction diagram
Q4D080, Q4D1Q4
-
-
-
?
L-phenylalanine + 2-oxoglutarate
2-oxo-3-phenylpropionic acid + L-glutamate
show the reaction diagram
Q964F0, Q964F1
-
-
-
?
L-phenylalanine + 2-oxoglutarate
2-oxo-3-phenylpropionic acid + L-glutamate
show the reaction diagram
-
-
i.e. phenylpyruvate
?
L-phenylalanine + 2-oxoglutarate
2-oxo-3-phenylpropionic acid + L-glutamate
show the reaction diagram
-
-
i.e. phenylpyruvate
?
L-phenylalanine + 2-oxoglutarate
2-oxo-3-phenylpropionic acid + L-glutamate
show the reaction diagram
-
-
i.e. phenylpyruvate
?
L-phenylalanine + 2-oxoglutarate
2-oxo-3-phenylpropionic acid + L-glutamate
show the reaction diagram
-
-
i.e. phenylpyruvate
?
L-phenylalanine + 2-oxoglutarate
2-oxo-3-phenylpropionic acid + L-glutamate
show the reaction diagram
-
-
i.e. phenylpyruvate
?
L-phenylalanine + 2-oxoglutarate
2-oxo-3-phenylpropionic acid + L-glutamate
show the reaction diagram
-
low activity
-
-
?
L-phenylalanine + 2-oxoglutarate
2-oxo-3-phenylpropionic acid + L-glutamate
show the reaction diagram
-
6.9% of the activity with glutamate
i.e. phenylpyruvate
?
L-phenylalanine + 2-oxoglutarate
2-oxo-3-phenylpropionic acid + L-glutamate
show the reaction diagram
Hypocrea rufa
-
7.7% of the activity with L-aspartate
i.e. phenylpyruvate
?
L-phenylalanine + 2-oxoglutarate
2-oxo-3-phenylpropionic acid + L-glutamate
show the reaction diagram
Q939C9
relative activity compared to L-aspartate: 0.3%
-
-
?
L-phenylalanine + 2-oxoglutarate
2-oxo-3-phenylpropionic acid + L-glutamate
show the reaction diagram
-
0.07% of the activity with L-aspartate
-
-
?
L-phenylalanine + 2-oxoglutarate
2-oxo-3-phenylpropionic acid + L-glutamate
show the reaction diagram
Chlamydomonas reinhardtii 6145c
-
low activity
-
-
?
L-phenylalanine + 2-oxoglutarate
2-oxo-3-phenylpropanoate + L-glutamate
show the reaction diagram
O96142
specific activity: 0.28 micromol/min/mg
-
-
?
L-serine + 2-oxoglutarate
3-hydroxy-2-oxopropionic acid + L-glutamate
show the reaction diagram
Hypocrea rufa
-
7.7% of the activity with aspartate
-
-
?
L-tryptophan + 2-oxoglutarate
3-indole-2-oxopropionic acid + L-glutamate
show the reaction diagram
-
-
-
-
?
L-tryptophan + 2-oxoglutarate
3-indole-2-oxopropionic acid + L-glutamate
show the reaction diagram
-
-
-
-
?
L-tryptophan + 2-oxoglutarate
3-indole-2-oxopropionic acid + L-glutamate
show the reaction diagram
-
-
-
-
?
L-tryptophan + 2-oxoglutarate
3-indole-2-oxopropionic acid + L-glutamate
show the reaction diagram
-
-
-
-
-
L-tryptophan + 2-oxoglutarate
3-indole-2-oxopropionic acid + L-glutamate
show the reaction diagram
Q4D080, Q4D1Q4
-
-
-
?
L-tryptophan + 2-oxoglutarate
3-indole-2-oxopropionic acid + L-glutamate
show the reaction diagram
Q964F0, Q964F1
-
-
-
?
L-tryptophan + 2-oxoglutarate
3-indole-2-oxopropionic acid + L-glutamate
show the reaction diagram
-
0.1% of the activity with aspartate
-
-
?
L-tryptophan + 2-oxoglutarate
3-indole-2-oxopropionic acid + L-glutamate
show the reaction diagram
-
11% of the activity with glutamate
-
-
?
L-tryptophan + 2-oxoglutarate
3-indole-2-oxopropionic acid + L-glutamate
show the reaction diagram
-
0.08% of the activity with aspartate
-
-
?
L-tryptophan + 2-oxoglutarate
3-indole-2-oxopropionic acid + L-glutamate
show the reaction diagram
Q939C9
relative activity compared to L-aspartate: 1.7%
-
-
?
L-tryptophan + 2-oxoglutarate
3-indole-2-oxopropionic acid + L-glutamate
show the reaction diagram
-
0.08% of the activity with L-aspartate
-
-
?
L-tryptophan + 2-oxoglutarate
3-indole-2-oxopropionic acid + L-glutamate
show the reaction diagram
-
0.1% of the activity with aspartate
-
-
?
L-tryptophan + 2-oxoglutarate
3-(1H-indol-3-yl)-2-oxopropanoate + L-glutamate
show the reaction diagram
O96142
specific activity: 0.16 micromol/min/mg
-
-
?
L-tyrosine + 2-oxoglutarate
3-(4-hydroxyphenyl)-2-oxopropanoate + L-glutamate
show the reaction diagram
O96142
specific activity: 0.24 micromol/min/mg
-
-
?
L-tyrosine + 2-oxoglutarate
3-(4-hydroxyphenyl)-2-oxopropionic acid + L-glutamate
show the reaction diagram
dolphin
-
-
-
ir
L-tyrosine + 2-oxoglutarate
3-(4-hydroxyphenyl)-2-oxopropionic acid + L-glutamate
show the reaction diagram
Q4D080, Q4D1Q4
-
-
-
?
L-tyrosine + 2-oxoglutarate
3-(4-hydroxyphenyl)-2-oxopropionic acid + L-glutamate
show the reaction diagram
Q964F0, Q964F1
-
-
-
?
L-tyrosine + 2-oxoglutarate
3-(4-hydroxyphenyl)-2-oxopropionic acid + L-glutamate
show the reaction diagram
-
-
i.e. 4-hydroxyphenylpyruvate
?
L-tyrosine + 2-oxoglutarate
3-(4-hydroxyphenyl)-2-oxopropionic acid + L-glutamate
show the reaction diagram
-
-
i.e. 4-hydroxyphenylpyruvate
?
L-tyrosine + 2-oxoglutarate
3-(4-hydroxyphenyl)-2-oxopropionic acid + L-glutamate
show the reaction diagram
-
low activity
-
-
?
L-tyrosine + 2-oxoglutarate
3-(4-hydroxyphenyl)-2-oxopropionic acid + L-glutamate
show the reaction diagram
-
1.5 of the activity with glutamate
i.e. 4-hydroxyphenylpyruvate
?
L-tyrosine + 2-oxoglutarate
3-(4-hydroxyphenyl)-2-oxopropionic acid + L-glutamate
show the reaction diagram
-
0.04% of the activity with aspartate
i.e. 4-hydroxyphenylpyruvate
?
L-tyrosine + 2-oxoglutarate
3-(4-hydroxyphenyl)-2-oxopropionic acid + L-glutamate
show the reaction diagram
Hypocrea rufa
-
84.6% of the activity with aspartate
i.e. 4-hydroxyphenylpyruvate
?
L-tyrosine + 2-oxoglutarate
3-(4-hydroxyphenyl)-2-oxopropionic acid + L-glutamate
show the reaction diagram
-
1.2% of the activity with glutamate
i.e. 4-hydroxyphenylpyruvate
?
L-tyrosine + 2-oxoglutarate
3-(4-hydroxyphenyl)-2-oxopropionic acid + L-glutamate
show the reaction diagram
Q939C9
relative activity compared to L-aspartate: 0.4
-
-
?
L-tyrosine + 2-oxoglutarate
3-(4-hydroxyphenyl)-2-oxopropionic acid + L-glutamate
show the reaction diagram
-
0.04% of the activity with L-aspartate
-
-
?
L-tyrosine + 2-oxoglutarate
3-(4-hydroxyphenyl)-2-oxopropionic acid + L-glutamate
show the reaction diagram
Chlamydomonas reinhardtii 6145c
-
low activity
-
-
?
additional information
?
-
-
substrate specificity
-
-
-
additional information
?
-
-
substrate specificity
-
-
-
additional information
?
-
-
substrate specificity
-
-
-
additional information
?
-
-
substrate specificity
-
-
-
additional information
?
-
-
substrate specificity
-
-
-
additional information
?
-
-
substrate specificity
-
-
-
additional information
?
-
-
substrate specificity
-
-
-
additional information
?
-
-
substrate specificity
-
-
-
additional information
?
-
Torulopsis candida
-
substrate specificity
-
-
-
additional information
?
-
-
substrate specificity
-
-
-
additional information
?
-
-
substrate specificity
-
-
-
additional information
?
-
-
substrate specificity
-
-
-
additional information
?
-
-
poor substrates are: glyoxylic acid, pyruvate, succinate, maleate, L-asparagine, L-glutamine, L-alanine, glycine
-
-
-
additional information
?
-
-
indole-3-pyruvate, p-hydroxy-phenylpyruvate, and 2-oxo-n-caproate are no substrates
-
-
-
additional information
?
-
-
no activity with L-2-amino-5-methoxy-5-oxopentanoic acid, fumarate, hydroxypyruvate, glutarate, L-proline, L-arginine, and L-lysine
-
-
-
additional information
?
-
-
no activity with L-cysteine, L-isoleucine, L-leucine, L-valine, L-glutamine, glycine, L-ornithine, L-lysine, L-arginine
-
-
-
additional information
?
-
-
no enzyme activity is detectable in the presence of glutamine, asparagine, alanine, histidine, leucine, methionine, lysine, arginine, tryptophan, tyrosine, phenylalanine or kynureine
-
-
-
additional information
?
-
Q5F4K8
no enzyme activity is detectable in the presence of glutamine, asparagine, alanine, histidine, leucine, methionine, lysine, arginine, tryptophan, tyrosine, phenylalanine or kynureine
-
-
-
additional information
?
-
Q9SIE1
no enzyme activity is detectable in the presence of glutamine, asparagine, alanine, histidine, leucine, methionine, lysine, arginine, tryptophan, tyrosine, phenylalanine or kynureine
-
-
-
additional information
?
-
Q4D080, Q4D1Q4
the cytosolic isoform displays broad substrate specificity
-
-
-
additional information
?
-
Q964F0, Q964F1
the cytosolic isoform displays broad substrate specificity
-
-
-
additional information
?
-
Q964F0, Q964F1
the mitochondrial isoform is highly specific for substrates L-aspartate and 2-oxoglutarate
-
-
-
additional information
?
-
Q4D080, Q4D1Q4
the mitochondrial isoform is highly specific for substrates L-aspartate and 2-oxoglutarate
-
-
-
additional information
?
-
Methanothermobacter thermautotrophicus SF-4
-
substrate specificity
-
-
-
additional information
?
-
Chlamydomonas reinhardtii 6145c
-
substrate specificity
-
-
-
additional information
?
-
Pseudomonas putida IFO 12996
-
substrate specificity
-
-
-
additional information
?
-
Trichomonas vaginalis Bushby
-
substrate specificity, no activity with L-cysteine, L-isoleucine, L-leucine, L-valine, L-glutamine, glycine, L-ornithine, L-lysine, L-arginine
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
Q56232
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
P00509
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
P00507, -
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
Leptosphaeria michotii
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
Torulopsis candida
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
P14909, -
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
Hypocrea rufa
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
key enzyme in assimilation of C and N compounds
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
dolphin
-
role in energy metabolism of diving animals
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
enzyme plays the most important role in amino acid metabolism
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
enzyme plays a central role in nitrogen metabolism of cells
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
enzyme plays an important role in numerous metabolic processes
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
anti-enzyme antibodies selectively inhibit the uptake of oleate in 3T3-L1 adipocytes by 31-55%, but only poorly in fibroblasts, the antibodies have no effect on uptake of 2-deoxyglucose and octanoate
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
function in C4 acid pathway
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
hyperprolinemia type II is an autosomal recessive disorder caused by severe deficiency of enzyme DELTA1-pyrroline-5-carboxylic acid dehydrogenase leading to tissue accumulation of proline. Proline has direct inhibitory effect on aspartate transaminase activity of different brain regions leading to lesser synthesis of glutamate thereby causing neurological dysfunctions
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
Pseudoalteromonas haloplanktis TAC 125
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
Bradyrhizobium japonicum 392
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
Methanothermobacter thermautotrophicus SF-4
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
Methanothermobacter thermautotrophicus SF-4
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
Chlamydomonas reinhardtii 6145c
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
Haloferax mediterranei R-4
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
Haloferax mediterranei R-4
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
Pseudomonas putida IFO 12996
-
enzyme plays the most important role in amino acid metabolism
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
Trichomonas vaginalis Bushby
-
-
-
?
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
2 mol of pyridoxal phosphate per mol of enzyme; a pyridoxal 5'-phosphate protein
pyridoxal 5'-phosphate
-
a pyridoxal 5'-phosphate protein; dependent on
pyridoxal 5'-phosphate
-
a pyridoxal 5'-phosphate protein; isozyme AAT-1: 0.87 mol per mol of subunit, isozyme AAT-2: 0.93 mol per mol of subunit
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
a pyridoxal 5'-phosphate protein
pyridoxal 5'-phosphate
-
a pyridoxal 5'-phosphate protein
pyridoxal 5'-phosphate
-
1 mol of pyridoxal phosphate per mol of subunit; apoenzyme can be reconstituted with pyridoxamine 5phosphate and/or pyridoxal 5'-phosphate, each subunit binding 1 mol of coenzym; a pyridoxal 5'-phosphate protein
pyridoxal 5'-phosphate
-
a pyridoxal 5'-phosphate protein
pyridoxal 5'-phosphate
-
a pyridoxal 5'-phosphate protein
pyridoxal 5'-phosphate
Rhodotorula minuta, Torulopsis candida
-
a pyridoxal 5'-phosphate protein
pyridoxal 5'-phosphate
-
1 mol of pyridoxal phosphate per mol of subunit
pyridoxal 5'-phosphate
-
2.1 mol of pyridoxal phosphate per mol of enzyme; 2.1mol per mol of enzyme; a pyridoxal 5'-phosphate protein
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
2 mol of pyridoxal phosphate per mol of enzyme; a pyridoxal 5'-phosphate protein
pyridoxal 5'-phosphate
-
2 mol of pyridoxal phosphate per mol of enzyme; a pyridoxal 5'-phosphate protein
pyridoxal 5'-phosphate
-
1.7-1.9 mol per mol of enzyme; a pyridoxal 5'-phosphate protein
pyridoxal 5'-phosphate
-
a pyridoxal 5'-phosphate protein; bound to the active site
pyridoxal 5'-phosphate
-
a pyridoxal 5'-phosphate protein; enzyme-bound
pyridoxal 5'-phosphate
-
a pyridoxal 5'-phosphate protein
pyridoxal 5'-phosphate
-
a pyridoxal 5'-phosphate protein; bound to the active site
pyridoxal 5'-phosphate
-
a pyridoxal 5'-phosphate protein; enzyme-bound
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
a pyridoxal 5'-phosphate protein
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
binds at the intersubunit active sites and stabilizes the native enzyme form
pyridoxal 5'-phosphate
Q9SIE1
essential
pyridoxal 5'-phosphate
-
essential
pyridoxal 5'-phosphate
Q5F4K8
essential
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
Q939C9
-
pyridoxal 5'-phosphate
-
-
pyridoxamine 5'-phosphate
-
1 mol per mol of subunit; reverse reaction
pyridoxamine 5'-phosphate
-
reverse reaction
pyridoxamine 5'-phosphate
-
reverse reaction
pyridoxamine 5'-phosphate
-
-
additional information
-
active with 1-deazapyridoxal 5'-phosphate a synthetic pyridoxal 5'-phosphate analogue
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
CaCl2
Q939C9
1 mM relative activity: 115.5%
CoCl2
Q939C9
1 mM relative activity: 122.1%
CuSO4
Q939C9
1 mM relative activity: 84.3%
EDTA
Q939C9
1 mM relative activity: 106.4%
MgCl2
Q939C9
1 mM relative activity: 96.9%
Mn2+
-
activation, isozyme AST II
ZnSO4
Q939C9
1 mM relative activity: 99.7%
MnSO4
Q939C9
1 mM relative activity: 90.1%
additional information
-
cytosolic isozyme, no metal ion requirement
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(S)-4-amino-4,5-dihydro-2-furancarboxylic acid
D3H0F7
crystal structures of the Escherichi coli aspartate aminotransferase with (S)-4-amino-4,5-dihydro-2-furancarboxylic acid bound to the active site are obtained via cocrystallization at pH 7.5 and 8. The complex structures suggest that (S)-4-amino-4,5-dihydro-2-furancarboxylic acid inhibits the transamination reaction by forming adducts with the catalytic lysine 246 via a covalent bond while producing 1 equivalent of pyridoxamine 5'-phosphate
-
2-methyl-DL-aspartate
Q56232
binds to the pyridoxal 5'-phosphate form of the enzyme, formation of an external aldimine complex
2-oxoglutaconate
-
injection into mice leads to inhibition of the kidney enzyme
2-oxoglutaconate
-
2-oxoglutarate protects against inhibition, L-glutamate enhances the inhibitory effect; 30% inhibition at 25C, pH 7.2, 10 mM, after 2 h; cytosolic and mitochondrial isozymes
2-oxoglutaconate
-
2-oxoglutarate protects against inhibition, L-glutamate enhances the inhibitory effect; 30% inhibition at 25C, pH 7.2, 10 mM, after 2 h; binds the active site of the pyridoxal 5'-phosphate enzyme form, cytosolic isozyme
2-oxoglutaconic acid dimethyl ester
-
15% inhibition at 25C, pH 7.0, 10 mM, after 2 h; pyridoxal 5'-phosphate enzyme form, cytosolic isozyme
2-oxoglutarate
-
in cell extracts, alanine activity is inhibited by 50% by about 2.5 mM 2-oxoglutarate, while the aspartate activity is unaffected at this concentration. The highly purified enzyme is also inhibited by 2-oxoglutarate, but the extent of inhibition is slightly more than that in extracts. Thus, alanine activity is completely inhibited by 10 mM 2-oxoglutarate, and 36% of the aspartate activity is inhibited
2-oxoglutarate
dolphin
-
oxoglutarate production; substrate inhibition at high concentration
2-oxoglutarate
-
substrate inhibition at high concentration
2-oxoglutarate
-
competitive to cysteine sulfinic acid or aspartate
2-oxoglutarate
-
1-3 mM, at pH 6.0, not at pH 8.0
2-oxoglutarate
-
cytoplasmic enzyme inhibited above 0.25 mM, mitochondrial enzyme not
2-oxoglutarate
-
competitive to L-aspartate
2-oxoglutarate
-
product and substrate inhibition
Adipate
-
no inhibition
alpha-aminoadipate
-
IC50: 1.5 mM
Aminoguanidine
-
competes with the enzyme for pyridoxal 5'-phosphate, forms complexes with pyridoxal 5'-phosphate, 70% enzyme inhibition at 1 mM
aminooxyacetic acid hemihydrochloride
-
inhibitor of C-S lyase, reduces renal injuries due to cisplatin in rats. On day 5 following a bolus cisplatin injection, in vivo nephrotoxic potentials are in the decreasing order of species rats > mice, rabbits, based on body surface. The levels of renal Pt residue at the nephrotoxic dose are in order of rabbits > rats > mice. The activity of endogenous basal mitochondrial aspartate aminotransferase, one of the C-S lyases, in the renal cortex of naive animals is rats > mice, rabbits. Expression of mitochondrial C-S lyase in the kidney is observed at approximately 37 kDa in all five species used. In in vitro studies, the cytotoxicity of cisplatin is dependent on the expression level of C-S lyase mRNA in the respective renal cells
-
aminooxyacetic acid hemihydrochloride
P00507
inhibitor of C-S lyase, reduces renal injuries due to cisplatin in rats. On day 5 following a bolus cisplatin injection, in vivo nephrotoxic potentials are in the decreasing order of species rats > mice, rabbits, based on body surface. The levels of renal Pt residue at the nephrotoxic dose are in order of rabbits > rats > mice. The activity of endogenous basal mitochondrial aspartate aminotransferase, one of the C-S lyases, in the renal cortex of naive animals is rats > mice, rabbits. Expression of mitochondrial C-S lyase in the kidney is observed at approximately 37 kDa in all five species used. In in vitro studies, the cytotoxicity of cisplatin is dependent on the expression level of C-S lyase mRNA in the respective renal cells
-
aspartate
-
IC50: 0.3 mM
chymoptrypsin
-
cytosolic isozyme at 1 mg/ml, no inhibition of mitochondrial isozyme
-
CN-
-
cytosolic isoform, at 5 mM
fumarate
-
competitive
gamma-Acetylenic GABA
-
-
glutamate
-
IC50: 0.9 mM
Glutarate
-
isozyme AAT1: competitive
Hadacidin
-
i.e. N-formylhydroxyaminoacetic acid
Hg2+
Hypocrea rufa
-
-
hydroxylamine
O96142
inhibition of PfAspAT abolishes all glutamate oxaloacetate transamination activity in the cytoplasm of cultured parasites, demonstrating that no other enzyme within the cytoplasm can complement PfAspAT activity
isonicotinic acid hydrazine
-
complete inhibition at 0.3 mM, partially reversible by pyridoxyl 5'-phosphate
isonicotinic acid hydrazine
-
cytosolic isozyme, only after 24 h incubation, 1 mM
L-2-amino-5-methoxy-5-oxopentanoic acid
-
only isozyme AAT2, competitive against L-asparate
L-aspartate
-
inhibits tyrosine transamination
L-aspartate
-
weak, competitive against 2-oxoglutarate
L-Cycloserine
-
cytosolic isozyme, weak inhibition only after 24 h incubation, 1 mM
L-cysteic acid
-
competitive
L-cysteine
-
10 mM, 30% inactivation
L-cysteine sulfinic acid
-
weak, competitive to 2-oxoglutarate
L-cysteinic acid
-
-
L-glutamate
dolphin
-
forward reaction, substrate L-aspartate
L-glutamate
-
competitive
L-glutamate
-
product inhibition, noncompetitive to 2-oxoglutarate and competitive against aspartate
L-glutamate
-
isozyme AAT1 and AAT2, product inhibition
L-glutamate
-
5 mM, significant inhibition
L-histidine
-
; inhibition is relieved by high concentrations of substrates
L-serine O-sulfate
-
inhibition of cytosolic enzyme, no inhibition of mitochondrial enzyme
malate
dolphin
-
isozymes Asp-DEAE-1 and Asp-DEAE-2
malate
-
oxoglutarate production, oxaloacetate production
malate
-
competitive
Maleate
-
78% inhibition of cytosolic isozyme at 4 mM, competitive to 2-oxoglutarate
Maleate
Q56232
binds noncovalently to the pyridoxal 5'-phosphate form of the enzyme
Methylacetimidate
-
complete inhibition at 50 mM
N-5'-phosphopyridoxyl L-aspartate
-
cofactor analogue binds covalently to the enzyme
N-ethylmaleimide
-
alkylation of cysteine residues
oxaloacetate
dolphin
-
substrate inhibition
oxaloacetate
-
isozymes AAT-P1 and AAT-P2; substrate inhibition
oxaloacetate
-
isozyme AAT1 and AAT2, product inhibition
p-chloromercuribenzoate
-
complete inhibition at 0.15 mM
p-chloromercuribenzoate
-
cytosolic isozyme, 50% inhibition after 10 min at 30C, 1 mM
p-hydroxymercuribenzoate
-
-
palmitate
-
0.1 mM
phosphate
-
inhibition of cofactor binding to the apoenzyme, cytosolic and mitochondrial isozymes
potassium phosphate
-
-
Pro
-
hyperprolinemia type II is an autosomal recessive disorder caused by severe deficiency of enzyme DELTA1-pyrroline-5-carboxylic acid dehydrogenase leading to tissue accumulation of proline. Proline has direct inhibitory effect on aspartate transaminase activity of different brain regions leading to lesser synthesis of glutamate thereby causing neurological dysfunctions
proteinase K
-
both cytosolic and mitochondrial isozymes
-
quisqualate
-
6 mM, 90% inhibition
Sodium mersalyl
-
cytosolic isozyme, 40% inhibition after 60 min at 5 mM and 30C
Subtilisin
-
only cytosolic isozyme
-
succinate
dolphin
-
forward reaction
succinate
Hypocrea rufa
-
-
succinate
-
competitive
Thiosemicarbazide
-
-
Trypsin
-
weak inhibition of mitochondrial isozyme
-
additional information
-
the activities with 2 mM aspartate or alanine are not inhibited by 10 mM isoleucine, phenylalanine, arginine, asparagine, glutamine, glycine, lysine, methionine, proline, serine, and threonine
-
additional information
-
no inhibition by Cd2+, Pb2+ and Cu2+
-
additional information
-
no inhibition by dipropylacetic acid, vinyl-GABA
-
additional information
-
no inhibition by 4-aminobutyric acid
-
additional information
-
cytosolic isozyme, no inhibition by L-cysteine and EDTA
-
additional information
-
no substrate inhibition
-
additional information
-
acarbose causes no changes in the specific and total activities of AST
-
additional information
-
insensitive to glutamine
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
aconitate
-
activating effect on the activity of the cytoplasmic enzyme form
ethanol
-
binge ethanol treatment causes significant increase in blood plasma AST activity
rosiglitazone
-
10 nM, stimulates activity
additional information
-
intramitochondrial chaperone homologues GroEL and GroES can facilitate the folding of nascent premature mitochondrial isoform pmAspAT in rabbit reticulocyte lysate under conditions where it otherwise would not, GroEL alone inhibits the import into mitochondria, which is reversed by GroES
-
additional information
P00507, -
cytosolic Hsp70, from bovine brain, protein exclusively binds to the mitochondrial isozyme, regulatory function; cytosolic Hsp70, from bovine brain, protein exclusively binds to the mitochondrial isozyme, regulatory function
-
additional information
-
carnosine treatment alone does not alter blood plasma AST activity
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.77
-
2-oxo-4-phenyl-butanoic acid
-
wild-type enzyme
0.86
-
2-oxo-4-phenyl-butanoic acid
-
mutant enzyme R292E/L18H
0.007
-
2-oxoglutarate
-
recombinant deletion mutant, pH 7.5, 25C
0.062
-
2-oxoglutarate
-
30C
0.07
-
2-oxoglutarate
-
isozyme pAspAT, gamma-form, pH 8.0, 25C
0.071
-
2-oxoglutarate
-
pH 7.6, 25C
0.075
-
2-oxoglutarate
-
isozyme pAspAT, beta-form, pH 8.0, 25C
0.08
-
2-oxoglutarate
-
isozyme Asp-DEAE-1, pH 8.0
0.08
-
2-oxoglutarate
-
recombinant mutant C166S, pH 7.5, 25C
0.087
-
2-oxoglutarate
-
isozyme pAspAT, alpha-form, pH 8.0, 25C
0.088
0.095
2-oxoglutarate
-
pH 7.4, 30C
0.093
-
2-oxoglutarate
-
cytosolic isozyme, pH 7.4, 25C
0.098
-
2-oxoglutarate
-
mitochondrial isozyme, pH 7.4, 25C
0.105
-
2-oxoglutarate
-
isoenzyme AAT-2, pH 7.8, 37C
0.11
-
2-oxoglutarate
-
isoenzyme AAT-1, pH 7.8, 37C
0.11
-
2-oxoglutarate
-
pH 8.3, 25C
0.12
-
2-oxoglutarate
-
isozyme Asp-DEAE-2, pH 8.0
0.13
-
2-oxoglutarate
-
isozyme mAspAT, pH 8.0, 25C
0.14
-
2-oxoglutarate
-
isozyme cAspAT, beta-form, pH 8.0, 25C
0.17
-
2-oxoglutarate
-
pH 7.4, 25C
0.17
-
2-oxoglutarate
-
isozyme cAspAT, alpha-form, pH 8.0, 25C
0.2
-
2-oxoglutarate
-
pH 7.5, 37C
0.2
-
2-oxoglutarate
-
isozyme AspAT-3, 25C, pH 8.0
0.2
-
2-oxoglutarate
-
isozyme AAT-P2, pH 7.6, 25C
0.2
-
2-oxoglutarate
-
isozyme cAspAT, gamma-form, pH 8.0, 25C
0.2
-
2-oxoglutarate
-
pH 8.0, 45C
0.22
-
2-oxoglutarate
-
pH 8.5, 60C, recombinant enzyme
0.23
-
2-oxoglutarate
-
isozyme AspAT-1, 25C, pH 8.0
0.24
-
2-oxoglutarate
-
25C, pH 8.0
0.26
-
2-oxoglutarate
-
isozyme AAT-P1, pH 7.6, 25C
0.3
-
2-oxoglutarate
-
cytosolic isozyme, pH 8.0, 37C
0.3
-
2-oxoglutarate
-
recombinant isozyme mAspAT, pH 7.5, 25C
0.3
-
2-oxoglutarate
Q939C9
pH 8.0, 45C
0.33
-
2-oxoglutarate
-
recombinant premature isozyme pmAspAT, pH 7.5, 25C
0.39
-
2-oxoglutarate
-
isozyme AAT-2, including forms 2a, 2b and 2c, pH 8.0
0.48
-
2-oxoglutarate
-
pH 8, cosubstrate: L-Phe, mutant enzyme A12T/P13T/N34D/T109S/G261A/S285G/A293D/N297S
0.5
-
2-oxoglutarate
-
pH 7.5, 37C
0.55
-
2-oxoglutarate
-
isozyme AAT-1, pH 8.0
0.55
-
2-oxoglutarate
-
pH 7.8, 25C
0.59
-
2-oxoglutarate
-
wild-type, pH 8.4, 25C
0.67
-
2-oxoglutarate
-
isozyme AST II, 37C, pH 7.5
0.8
-
2-oxoglutarate
-
recombinant mutant C166A, pH 7.5, 25C
1.25
-
2-oxoglutarate
-
cytoplasmic enzyme
1.33
-
2-oxoglutarate
-
cytoplasmic enzyme, in 0.05 M potassium phosphate buffer (pH 7.5) containing 0.9 mM L-aspartate, 2.7 mM 2-oxoglutarate, 0.1 mM NADH, and 1 U/ml malate dehydrogenase
1.4
-
2-oxoglutarate
-
pH 7.5, 35C
1.47
-
2-oxoglutarate
-
enzyme from nonsynaptic mitochondrion, pH 7.8, 30C
1.5
-
2-oxoglutarate
Q964F0, Q964F1
pH 7.5, 37C
1.7
-
2-oxoglutarate
-
cytosolic isozyme
1.75
-
2-oxoglutarate
-
mitochondrial enzyme
1.95
-
2-oxoglutarate
-
mitochondrial enzyme, in 0.05 M potassium phosphate buffer (pH 7.5) containing 1.6 mM L-aspartate, 4 mM 2-oxoglutarate, 0.1 mM NADH, and 1 U/ml malate dehydrogenase
1.95
-
2-oxoglutarate
-
enzyme from synaptic mitochondrion, pH 7.8, 30C
2.06
-
2-oxoglutarate
-
cytosolic isozyme, pH 6.8, 37C
2.2
-
2-oxoglutarate
-
mitochondrial isozyme
2.4
-
2-oxoglutarate
Q56232
wild-type, pH 8.0, 25C
2.6
-
2-oxoglutarate
-
pH 8.0, 50C
2.6
-
2-oxoglutarate
-
pH 8, cosubstrate: L-Asp, mutant enzyme A12T/P13T/N34D/T109S/G261A/S285G/A293D/N297S
3.2
-
2-oxoglutarate
Q4D080, Q4D1Q4
pH 7.5, 37C
6.9
-
2-oxoglutarate
-
mitochondrial isozyme, pH 8.0, 37C
4.1
-
L-2-amino-4-methoxy-4-oxobutanoic acid
-
isozyme AAT2, 25C
20.3
-
L-2-amino-4-methoxy-4-oxobutanoic acid
-
isozyme AAT1, 25C
3.5
-
L-alanine
-
pH 7.5, 37C
140
-
L-alanine
-
60C
29
-
L-Asp
-
pH 8, mutant enzyme A12T/P13T/N34D/T109S/G261A/S285G/A293D/N297S
0.09
-
L-aspartate
-
recombinant deletion mutant, pH 7.5, 25C
0.25
-
L-aspartate
-
recombinant premature isozyme pmAspAT, pH 7.5, 25C
0.25
-
L-aspartate
-
60C
0.29
-
L-aspartate
-
recombinant mutant C166A, pH 7.5, 25C
0.33
-
L-aspartate
-
recombinant mutant C166S, pH 7.5, 25C
0.35
-
L-aspartate
-
cytoplasmic enzyme
0.36
-
L-aspartate
-
recombinant isozyme mAspAT, pH 7.5, 25C
0.4
-
L-aspartate
-
mitochondrial isozyme, pH 7.4, 25C
0.43
-
L-aspartate
-
cytoplasmic enzyme, in 0.05 M potassium phosphate buffer (pH 7.5) containing 0.9 mM L-aspartate, 2.7 mM 2-oxoglutarate, 0.1 mM NADH, and 1 U/ml malate dehydrogenase
0.5
-
L-aspartate
-
isozyme Asp-DEAE-2, pH 8.0
0.51
-
L-aspartate
-
mitochondrial isozyme
0.75
-
L-aspartate
-
mitochondrial enzyme
0.78
-
L-aspartate
-
mitochondrial enzyme, in 0.05 M potassium phosphate buffer (pH 7.5) containing 1.6 mM L-aspartate, 4 mM 2-oxoglutarate, 0.1 mM NADH, and 1 U/ml malate dehydrogenase
0.85
-
L-aspartate
-
isozyme Asp-DEAE-1, pH 8.0
0.96
-
L-aspartate
-
30C
1.2
-
L-aspartate
-
isozyme AAT-1, pH 8.0
1.3
-
L-aspartate
-
25C, pH 8.0
1.3
-
L-aspartate
-
isozyme mAspAT, pH 8.0, 25C
1.5
-
L-aspartate
-
isozyme AAT-2, including forms 2a, 2b and 2c, pH 8.0
1.7
-
L-aspartate
-
isozyme AspAT-3, 25C, pH 8.0
1.7
-
L-aspartate
Q56232
wild-type, pH 8.0, 25C
1.9
-
L-aspartate
-
mitochondrial isozyme, pH 8.0, 37C
1.9
-
L-aspartate
-
wild-type, pH 8.4, 25C
2
-
L-aspartate
-
pH 7.4, 25C
2.1
2.9
L-aspartate
-
pH 7.4, 30C
2.1
-
L-aspartate
Q4D080, Q4D1Q4
pH 7.5, 37C
2.2
-
L-aspartate
-
isozyme AAT-P1, pH 7.6, 25C
2.2
-
L-aspartate
-
isozyme pAsp-AT, beta-form, pH 8.0, 25C
2.3
-
L-aspartate
-
pH 8.3, 25C
2.3
-
L-aspartate
-
isozyme pAsp-AT, gamma-form, pH 8.0, 25C
2.4
-
L-aspartate
-
isoenzyme AAT-1, pH 7.8, 37C
2.53
-
L-aspartate
-
pH 7.8, 25C
2.6
-
L-aspartate
-
isozyme AAT-P2, pH 7.6, 25C
2.6
-
L-aspartate
-
isozyme pAsp-AT and cAspAT, alpha-form, pH 8.0, 25C
3
-
L-aspartate
-
cytosolic isozyme, pH 7.4, 25C
3
-
L-aspartate
-
pH 8.0, 50C
3
-
L-aspartate
-
isozyme cAspAT, gamma-form, pH 8.0, 25C
3.1
-
L-aspartate
-
pH 7.5, 25C, mutant I33Q/Y214Q/R280Y
3.2
-
L-aspartate
-
isozyme cAspAT, beta-form, pH 8.0, 25C
3.7
-
L-aspartate
-
pH 7.5, 37C
3.7
-
L-aspartate
-
isoenzyme AAT-2, pH 7.8, 37C
3.9
-
L-aspartate
-
cytosolic isozyme, pH 8.0, 37C
4
-
L-aspartate
-
pH 7.5, 25C, wild-type
4.4
-
L-aspartate
-
-
4.6
-
L-aspartate
-
pH 7.5, 35C
5
-
L-aspartate
-
pH 8.0, 45C
6.5
-
L-aspartate
-
cytosolic isozyme
6.7
-
L-aspartate
Q939C9
pH 8.0, 45C
6.8
-
L-aspartate
Q964F0, Q964F1
pH 7.5, 37C
7.5
-
L-aspartate
-
isozyme AspAT-1, 25C, pH 8.0
15.1
-
L-aspartate
-
isozyme AST II, 37C, pH 7.5
22.5
-
L-aspartate
-
cytosolic isozyme, pH 6.8, 37C
26
-
L-aspartate
Q964F0, Q964F1
pH 7.5, 37C
37
-
L-aspartate
Q4D080, Q4D1Q4
pH 7.5, 37C
2.05
-
L-cysteine sulfinic acid
-
pH 8.5, 60C, recombinant enzyme
0.5
-
L-glutamate
-
cytoplasmic enzyme, in 0.05 M potassium phosphate buffer (pH 7.5) containing 0.9 mM L-aspartate, 2.7 mM 2-oxoglutarate, 0.1 mM NADH, and 1 U/ml malate dehydrogenase
0.58
-
L-glutamate
-
mitochondrial enzyme, in 0.05 M potassium phosphate buffer (pH 7.5) containing 1.6 mM L-aspartate, 4 mM 2-oxoglutarate, 0.1 mM NADH, and 1 U/ml malate dehydrogenase
0.75
-
L-glutamate
-
isozyme Asp-DEAE-2, pH 8.0
1.6
-
L-glutamate
-
isozyme Asp-DEAE-1, pH 8.0
3.88
-
L-glutamate
-
pH 7.8, 25C
5.2
-
L-glutamate
-
pH 7.5, 25C, mutant I33Q/Y214Q/R280Y
5.7
-
L-glutamate
-
pH 8.0, 45C
7.5
-
L-glutamate
-
isozyme mAspAT, pH 8.0, 25C
8
-
L-glutamate
Q939C9
pH 8.0, 45C
12
-
L-glutamate
-
isozyme AAT-P2, pH 7.6, 25C
12.2
-
L-glutamate
-
isozyme AspAT-3, 25C, pH 8.0
13
-
L-glutamate
-
pH 8.0, 25C
13
-
L-glutamate
-
isozyme cAspAT, gamma-form, pH 8.0, 25C
13.2
-
L-glutamate
-
isoenzyme AAT-2
14
-
L-glutamate
-
isozyme cAspAT, beta-form, pH 8.0, 25C
15
-
L-glutamate
-
25C, pH 8.0
17
-
L-glutamate
-
isozyme cAspAT, alpha-form, pH 8.0, 25C
17.4
-
L-glutamate
-
isozyme AspAT-1, 25C, pH 8.0
18
-
L-glutamate
-
isozyme pAspAT, gamma-form, pH 8.0, 25C
18.5
-
L-glutamate
-
isozyme AAT-1, pH 8.0
19.4
-
L-glutamate
-
isozyme AAT-2, including forms 2a, 2b and 2c, pH 8.0
20
-
L-glutamate
-
isozyme pAspAT, beta-form, pH 8.0, 25C
22
-
L-glutamate
-
isozyme AAT-P1, pH 7.6, 25C
32
-
L-glutamate
-
isozyme pAspAT, alpha-form, pH 8.0, 25C
37
-
L-glutamate
-
pH 7.5, 25C, wild-type
0.724
-
L-kynurenine
-
at pH 7.4
105
-
L-Lys
-
mutant enzyme R292E/L18H
189
-
L-Lys
-
wild-type enzyme
6.9
-
L-methionine
Q4D080, Q4D1Q4
pH 7.5, 37C
56
-
L-methionine
Q964F0, Q964F1
pH 7.5, 37C
0.3
-
L-Phe
-
pH 8, mutant enzyme A12T/P13T/N34D/T109S/G261A/S285G/A293D/N297S
1.1
-
L-phenylalanine
Q4D080, Q4D1Q4
pH 7.5, 37C
2.17
-
L-phenylalanine
-
-
6.6
-
L-phenylalanine
Q964F0, Q964F1
pH 7.5, 37C
2.3
-
L-tryptophan
Q4D080, Q4D1Q4
pH 7.5, 37C
5
-
L-tryptophan
-
pH 7.6, 25C
5
-
L-tryptophan
-
L-glutamate, isoenzyme AAT-1
1.43
-
L-tyrosine
-
pH 7.6, 25C
1.5
-
L-tyrosine
Q4D080, Q4D1Q4
pH 7.5, 37C
0.01
-
oxaloacetate
-
25C, pH 8.0
0.02
-
oxaloacetate
-
isozyme AAT-P2, pH 7.6, 25C
0.023
-
oxaloacetate
-
isozyme pAspAT, gamma-form, pH 8.0, 25C
0.027
-
oxaloacetate
-
isozyme AAT-2, including forms 2a, 2b and 2c, pH 8.0
0.03
-
oxaloacetate
-
isozyme pAspAT, alpha-form, pH 8.0, 25C
0.031
-
oxaloacetate
-
isozyme AAT-1, pH 8.0
0.032
-
oxaloacetate
-
pH 8.0, 45C
0.033
-
oxaloacetate
-
isozyme pAspAT, beta-form, pH 8.0, 25C
0.043
-
oxaloacetate
-
isoenzyme AAT-1
0.044
-
oxaloacetate
-
pH 7.8, 25C
0.045
-
oxaloacetate
-
isozyme Asp-DEAE-2, pH 8.0
0.048
-
oxaloacetate
-
isoenzyme AAT-2
0.049
-
oxaloacetate
-
pH 8.0, 25C
0.056
-
oxaloacetate
-
isozyme mAspAT, pH 8.0, 25C
0.065
-
oxaloacetate
-
isozyme cAspAT, alpha-form, pH 8.0, 25C
0.08
-
oxaloacetate
-
isozyme cAspAT, gamma-form, pH 8.0, 25C
0.085
-
oxaloacetate
-
isozyme cAspAT, beta-form, pH 8.0, 25C
0.1
-
oxaloacetate
-
isozyme Asp-DEAE-1, pH 8.0
0.1
-
oxaloacetate
-
isozyme AAT-P1, pH 7.6, 25C
0.2
-
oxaloacetate
-
isozyme AspAT-1, 25C, pH 8.0
0.32
-
oxaloacetate
-
isozyme AspAT-3, 25C, pH 8.0
0.37
-
oxaloacetate
-
pH 7.6, 25C
0.6
-
oxaloacetate
Q939C9
pH 8.0, 45C
2.04
-
oxaloacetate
-
mitochondrial enzyme, in 0.05 M potassium phosphate buffer (pH 7.5) containing 1.6 mM L-aspartate, 4 mM 2-oxoglutarate, 0.1 mM NADH, and 1 U/ml malate dehydrogenase
2.45
-
oxaloacetate
-
cytoplasmic enzyme, in 0.05 M potassium phosphate buffer (pH 7.5) containing 0.9 mM L-aspartate, 2.7 mM 2-oxoglutarate, 0.1 mM NADH, and 1 U/ml malate dehydrogenase
0.00025
-
pyridoxyl 5'-phosphate
-
pH 7.6, 25C
1.6
-
L-tyrosine
Q964F0, Q964F1
pH 7.5, 37C
additional information
-
additional information
dolphin
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
Leptosphaeria michotii
-
-
-
additional information
-
additional information
-
kinetics
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
kinetics
-
additional information
-
additional information
-
kinetics
-
additional information
-
additional information
-
kinetics; wild-type and mutants
-
additional information
-
additional information
-
kinetics; recombinant enzyme
-
additional information
-
additional information
-
kinetics; wild-type and mutants
-
additional information
-
additional information
Q56232
kinetics; wild-type and mutants
-
additional information
-
additional information
-
kinetics
-
additional information
-
additional information
-
recombinant enzyme, high temperature dependence of Km
-
additional information
-
additional information
-
kinetics; mutants
-
additional information
-
additional information
-
-
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.35
-
2-oxo-4-phenyl-butanoic acid
-
wild-type enzyme
0.38
-
2-oxo-4-phenyl-butanoic acid
-
mutant enzyme R292E/L18H
4
-
2-oxoglutarate
-
recombinant deletion mutant, pH 7.5, 25C
27
-
2-oxoglutarate
Q939C9
pH 8.0, 45C
89
-
2-oxoglutarate
-
recombinant C166S mutant, pH 7.5, 25C
90
-
2-oxoglutarate
-
recombinant premature isozyme pmAspAT, pH 7.5, 25C
96
-
2-oxoglutarate
-
recombinant C166A mutant, pH 7.5, 25C
120
-
2-oxoglutarate
Q56232
wild-type, pH 8.0, 25C
176
-
2-oxoglutarate
-
isozyme AAT5, pH 8.0, 25C
187
-
2-oxoglutarate
-
recombinant isozyme mAspAT, pH 7.5, 25C
205
-
2-oxoglutarate
-
isozyme AAT1, pH 8.0, 25C
217
-
2-oxoglutarate
-
isozyme AAT2, pH 8.0, 25C
322
-
2-oxoglutarate
-
pH 7.4, 25C
43
-
L-Asp
-
pH 8, mutant enzyme A12T/P13T/N34D/T109S/G261A/S285G/A293D/N297S
0.13
-
L-aspartate
-
pH 7.5, 25C, mutant I33Q/Y214Q/R280Y
4
-
L-aspartate
-
recombinant deletion mutant, pH 7.5, 25C
30
-
L-aspartate
Q939C9
pH 8.0, 45C
89
-
L-aspartate
-
recombinant C166S mutant, pH 7.5, 25C
90
-
L-aspartate
-
recombinant premature isozyme pmAspAT, pH 7.5, 25C
96
-
L-aspartate
-
recombinant C166A mutant, pH 7.5, 25C
120
-
L-aspartate
Q56232
wild-type, pH 8.0, 25C
187
-
L-aspartate
-
pH 8.0, 45C
187
-
L-aspartate
-
recombinant isozyme mAspAT, pH 7.5, 25C
259
-
L-aspartate
-
wild-type, pH 8.4, 25C
322
-
L-aspartate
-
pH 7.4, 25C
352
-
L-aspartate
-
pH 7.5, 35C
530
-
L-aspartate
-
pH 7.5, 25C, wild-type
0.03
-
L-glutamate
-
pH 7.5, 25C, mutant I33Q/Y214Q/R280Y
14
-
L-glutamate
Q939C9
pH 8.0, 45C
101
-
L-glutamate
-
pH 8.0, 45C
670
-
L-glutamate
-
pH 7.5, 25C, wild-type
0.305
-
L-Lys
-
wild-type enzyme
5.55
-
L-Lys
-
mutant enzyme R292E/L18H
22
-
oxaloacetate
Q939C9
pH 8.0, 45C
279
-
oxaloacetate
-
isozyme AAT5, pH 8.0, 25C
319
-
oxaloacetate
-
isozyme AAT1, pH 8.0, 25C
574
-
oxaloacetate
-
isozyme AAT2, pH 8.0, 25C
10
-
L-Phe
-
pH 8, mutant enzyme A12T/P13T/N34D/T109S/G261A/S285G/A293D/N297S
additional information
-
additional information
-
mutants
-
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
84.38
-
2-oxoglutarate
Q939C9
pH 8.0, 45C
34
251.4
-
2-oxoglutarate
-
pH 7.5, 35C
34
0.042
-
L-aspartate
-
pH 7.5, 25C, mutant I33Q/Y214Q/R280Y
97
4.5
-
L-aspartate
Q939C9
pH 8.0, 45C
97
76.5
-
L-aspartate
-
pH 7.5, 35C
97
133
-
L-aspartate
-
pH 7.5, 25C, wild-type
97
0.006
-
L-glutamate
-
pH 7.5, 25C, mutant I33Q/Y214Q/R280Y
41
1.75
-
L-glutamate
Q939C9
pH 8.0, 45C
41
18
-
L-glutamate
-
pH 7.5, 25C, wild-type
41
36.67
-
oxaloacetate
Q939C9
pH 8.0, 45C
57
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2
-
2-oxoglutaconate
-
cytosolic isozyme, 25C, pH 7.2
0.96
-
2-oxoglutarate
-
cytosolic isozyme, pH 8.6, versus cysteinic acid
1.9
-
2-oxoglutarate
-
mitochondrial isozyme, pH 8.6, versus L-aspartate
2.5
-
2-oxoglutarate
-
mitochondrial isozyme, pH 8.6, versus cysteinic acid
17
-
2-oxoglutarate
-
cytosolic isozyme, pH 8.6, versus L-aspartate
30
-
2-oxoglutarate
-
30C, substrate inhibition
21
-
aspartate
-
cytosolic isozyme, pH 8.6, versus 2-oxoglutarate
263
-
aspartate
-
mitochondrial isozyme, pH 8.6, versus 2-oxoglutarate
6.78
-
fumarate
-
isozyme AAT2, 25C, versus 2-oxoglutarate
8.4
-
fumarate
-
cytoplasmic enzyme
24.59
-
fumarate
-
isozyme AAT1, 25C, versus 2-oxoglutarate
33.72
-
fumarate
-
isozyme AAT2, 25C, versus L-aspartate
44.12
-
fumarate
-
isozyme AAT1, 25C, versus L-aspartate
15.05
-
Glutarate
-
isozyme AAT1, 25C, versus 2-oxoglutarate
26.55
-
Glutarate
-
isozyme AAT1, 25C, versus L-aspartate
6.6
-
Isocitrate
-
cytoplasmic enzyme
25.85
-
L-2-amino-5-methoxy-5-oxopentanoic acid
-
isozyme AAT2, 25C, versus 2-oxoglutarate
1.6
-
L-aspartate
-
cytoplasmic enzyme
1.9
-
L-aspartate
-
mitochondrial enzyme
5.1
-
L-cysteinic acid
-
cytosolic isozyme, pH 8.6, versus 2-oxoglutarate
16.29
-
L-cysteinic acid
-
isozyme AAT1, 25C, versus 2-oxoglutarate
20.73
-
L-cysteinic acid
-
isozyme AAT2, 25C, versus 2-oxoglutarate
26
-
L-cysteinic acid
-
mitochondrial isozyme, pH 8.6, versus 2-oxoglutarate
97.63
-
L-cysteinic acid
-
isozyme AAT1, 25C, versus L-aspartate
150.8
-
L-cysteinic acid
-
isozyme AAT2, 25C, versus L-aspartate
1.8
-
L-glutamate
-
mitochondrial enzyme
2.4
-
L-glutamate
-
cytoplasmic enzyme
2.8
-
L-glutamate
-
30C, competitive versus L-aspartate
6.8
-
L-glutamate
-
30C, competitive versus 2-oxoglutrate
10.5
-
L-glutamate
-
isozyme AAT1, competitive versus L-aspartate
11.1
-
L-glutamate
-
isozyme AAT1, noncompetitive versus 2-oxoglutarate
16
-
L-glutamate
-
isozyme AAT2, noncompetitive versus 2-oxoglutarate
30
-
L-glutamate
-
isozyme AAT2, competitive versus L-aspartate
2.6
-
L-glutamine
-
mitochondrial enzyme
3.7
-
L-glutamine
-
cytoplasmic enzyme
1.21
-
Maleate
-
isozyme AAT2, versus 2-oxoglutarate, 25C
1.4
-
Maleate
-
isozyme AAT1, versus 2-oxoglutarate, 25C
1.72
-
Maleate
-
cytosolic isozyme, pH 6.8, 37C
8.5
-
Maleate
-
isozyme AAT2, versus L-aspartate, 25C
10.58
-
Maleate
-
AAT1, versus L-aspartate, 25C
0.005
-
oxaloacetate
-
isozyme AAT1, competitive versus 2-oxoglutarate
0.024
-
oxaloacetate
-
isozyme AAT2, noncompetitive versus L-aspartate
0.026
-
oxaloacetate
-
isozyme AAT2, competitive versus 2-oxoglutarate
0.03
-
oxaloacetate
-
isozyme AAT1, noncompetitive versus L-aspartate
0.0195
-
phosphate
-
mitochondrial isozyme, pH 7.4, 37C
0.032
-
phosphate
-
cytosolic isozyme, pH 7.4, 37C
4.1
-
succinate
-
mitochondrial enzyme
5.7
-
succinate
-
cytoplasmic enzyme
8.86
-
succinate
-
isozyme AAT2, 25C, versus 2-oxoglutarate
10.66
-
succinate
-
isozyme AAT1, 25C, versus 2-oxoglutarate
16.84
-
succinate
-
isozyme AAT2, 25C, versus L-aspartate
36.89
-
succinate
-
isozyme AAT1, 25C, versus L-aspartate
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1.5
-
alpha-aminoadipate
-
IC50: 1.5 mM
0.3
-
aspartate
-
IC50: 0.3 mM
0.9
-
glutamate
-
IC50: 0.9 mM
0.069
-
hydroxylamine
O96142
pH 8, 37C
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.00000967
-
-
enzyme from homogenate
0.00875
-
-
after 905fold purification
0.015
-
-
homogenate, mitochondrial enzyme
0.04
-
-
homogenate, cytoplasmic enzyme
0.06
-
-
wild type enzyme, at 37C
0.061
-
-
partially purified isozyme AST II
0.11
-
-
cell extract
0.14
-
O96142
substrates: L-asparagine + 2-oxoglutarate, pH 8, 37C
0.16
-
O96142
substrates: L-tryptophan + 2-oxoglutarate, pH 8, 37C
0.186
-
Q5F4K8
-
0.24
-
Torulopsis candida
-
-
0.24
-
O96142
substrates: L-tyrosine + 2-oxoglutarate, pH 8, 37C
0.28
-
O96142
substrates: L-phenylalanine + 2-oxoglutarate, pH 8, 37C
0.3
-
-
pH 7.5, 37C, enzyme in crude extract
0.459
-
-
after 30fold purification, mitochondrial enzyme
0.576
-
-
partially purified cytosolic isozyme
1.41
-
-
after 35fold purification, cytoplasmic enzyme
1.53
-
-
purified enzyme
2.5
-
Torulopsis candida
-
purified enzyme
2.67
-
O96142
substrates: L-aspartate + 2-oxoglutarate, pH 8, 37C
12.92
-
-
recombinant enzyme in Escherichia coli cells
16.87
-
-
in 50 mM Tris-HCl pH 7.8
18.8
-
-
purified mitochondrial isozyme from liver
22.37
-
-
mitochondrial enzyme
22.6
-
-
purified mitochondrial isozyme from heart
25.3
-
-
pH 7.5, 37C, partiall purified enzyme
45.15
-
-
purified enzyme
48.45
-
-
cytoplasmic enzyme
69.4
-
-
partially purified enzyme
74
-
-
purified cytosolic isozyme from liver
83.5
-
-
purified cytosolic isozyme from heart
84
-
-
purified enzyme
84
-
-
purified enzyme
93
-
-
pH 8.5, 60C, recombinant enzyme
100
-
dolphin
-
purified cytosolic isozyme
105
-
-
purified enzyme
105
-
-
partially purified enzyme
108
-
-
mutant V39L
112.1
-
-
purified recombinant enzyme
120
-
-
-
130
-
-
purified cytosolic isozyme AAT-2 form 2a
136
-
-
partially purified enzyme
137.7
-
-
purified recombinant enzyme
140
-
-
purified cytosolic isozyme AAT-2 form 2c
150
-
-
purified, mitochondrial isozyme
151.5
-
-
mitochondrial isozyme
156
-
-
mitochondrial fraction
165
-
-
synthesis of aspartate
165
-
-
purified recombinant isozyme AAT5
170
-
-
purified enzyme
172
-
-
purified enzyme
178
-
-
purified pAspAT, gamma-form
182
-
-
forward reaction
200
-
-
purified enzyme
202
-
-
purified mitochondrial isozyme
210
-
-
purified apoenzyme
215
-
-
purified cytosolic isozyme
217
-
-
purified enzyme
220
-
-
-
221
-
-
purified enzyme
228
-
dolphin
-
purified mitochondrial isozyme
231
-
-
purified mitochondrial isozyme
232
-
-
purified recombinant enyme
240
-
-
purified cytosolic isozyme AAT-2 form 2b
252
-
-
purified pAspAT, alpha-form
292.3
-
Torulopsis candida
-
-
322
-
-
purified pAspAT, beta-form
341
-
-
supernatant fraction
390
-
-
purified isozyme AAT-1
403.4
-
-
purified enzyme
443
-
-
purified cytosolic isozyme
450
-
-
purified isozyme AAT-2
454
-
-
recombinant purified isozyme AAT1
512
-
-
purified mAspAT
546.5
-
Leptosphaeria michotii
-
purified isozyme B
671
-
-
purified cAspAT, alpha-form
805.6
-
Leptosphaeria michotii
-
purified isozyme A
953
-
-
purified cAspAT, gamma-form
1035
-
-
purified cAspAT, beta-form
2934
-
-
recombinant purified isozyme AAT2
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
activity of recombinant isozymes from different E. coli host strains
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
889 units/g protein
additional information
-
-
33 units/mg
additional information
-
-
15.25 units/l
additional information
-
-
1.7 units/ml
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.3
7.3
dolphin
-
mitochondrial enzyme
6.5
8.5
-
-
6.8
8.3
-
formation of oxaloacetate, isoenzyme Asp-DEAE-1
6.8
-
-
cytosolic isozyme
6.8
-
-
enzyme from eggs
6.8
-
-
mitochondrial form
7
8
-
forward reaction, isoenzymes AAT-1 and AAT-2
7
-
P00507, -
assay at; assay at
7
-
-
enzyme from larva
7.2
-
-
-
7.3
8.3
dolphin
-
cytosolic enzyme
7.4
7.6
-
-
7.4
-
-
assay at
7.4
-
D3H0F7
assay at
7.5
8.5
-
isozyme AAT1
7.5
-
-
assay at
7.5
-
-
cytosolic isozyme
7.5
-
Leptosphaeria michotii
-
isozymes A and B
7.5
-
-
-
7.5
-
-
recombinant enzyme, assay at
7.5
-
-
isozyme AST II
7.5
-
-
cytoplasmic form
7.5
-
-
assay at
7.5
-
-
assay at
7.6
-
-
-
7.8
-
-
assay at
8
8.3
-
2 reaction methods
8
8.5
-
reverse reaction, isoenzyme AAT-1
8
8.8
-
reverse reaction, isoenzyme AAT-2
8
8.9
-
-
8
-
-
formation of aspartate
8
-
-
oxaloacetate formation, isoenzyme Asp-DEAE-2
8
-
-
assay at
8
-
-
reverse reaction
8
-
-
formation of glutamate
8
-
-
isoenzyme AAT-1, isoenzyme AAT-2
8
-
-
assay at
8
-
-
assay at
8
-
-
assay at
8
-
-
assay at
8
-
-
assay at
8
-
-
assay at
8
-
-
highest activity
8
-
Q939C9
-
8
-
O96142
assay at
8.3
-
-
forward reaction
8.5
10
-
cytosolic enzyme
8.5
9.5
-
isozyme AAT2
8.5
-
-
substrates L-phenylalanine or L-tryptophan
8.5
-
-
assay at
8.5
-
-
L-aspartate formation
8.7
-
-
mitochondrial enzyme
9
-
-
substrate L-tyrosine
9
-
Hypocrea rufa
-
-
additional information
-
-
succession of enzymes with different pH-optima takes place during ontogenesis, as well as stage specific changes in their activity
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
-
-
40% of maximal activity
5.5
10
Leptosphaeria michotii
-
isozyme B
5.5
9
Leptosphaeria michotii
-
isozyme A
5.5
9.5
-
no definite pH optimum
6.3
9
-
about 60% of activity maximum at pH 6.3 and pH 9.0
6.4
7.2
-
cytosolic isozyme
6.5
8
-
pH 6.5: 63% of activity maximum of oxaloacetate formation, 50% of activity maximum of aspartate formation, pH 8.0: activity maximum
6.8
8.3
dolphin
-
pH 6.8: 76% of activity maximum, pH 7.3-8.3: activity maximum, supernatant enzyme
7
9
-
pH 7.0: about 45% of activity maximum, pH 9.0: about 40% of activity maximum
7
9
Q939C9
relatively high activity in alkaline range
7.4
10
-
pH 7.4: 60% of activity maximum, pH 8.5-10.0: activity maximum, cytosolic enzyme
7.4
8.7
-
pH 7.4: 95% of activity maximum, pH 8.7: activity maximum, mitochondrial enzyme
10
-
-
40% of maximal activity
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
-
assay at
25
-
-
assay at
25
-
-
assay at
25
-
-
assay at
25
-
-
assay at
25
-
-
-
25
-
-
assay at
25
-
-
assay at
25
-
-
assay at
25
-
-
assay at
25
-
-
assay at
25
-
-
assay at
25
-
-
assay at
25
-
-
assay at
30
-
-
assay at
30
-
Leptosphaeria michotii
-
assay at
30
-
-
assay at
30
-
-
assay at
34
-
-
optimal temperature of recombinant enzyme in Escherichia coli in vivo
37
-
-
assay at
37
-
-
assay at
37
-
-
assay at
37
-
-
assay at
37
-
P00507, -
assay at; assay at
37
-
-
assay at
37
-
O96142
assay at
40
-
-
highest activity
45
-
Q939C9
-
50
60
-
highest catalytic activity
55
-
-
0.7 M KCl
65
-
-
1.6-3.4 M KCl
65
-
-
3.5 M KCl
70
-
-
-
95
-
-
above; above
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
15
-
-
30% activity
35
63
-
half-maximal activity at 35C and 63C
40
80
-
40C: about 40% of activity maximum, 80C: about 65% of activity maximum
45
85
-
44% of maximum activity at 45C, 80% of maximum activity at 85C
60
-
-
30% activity
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.1
-
-
2 forms differing in isoelectric point: form I has a pI at pH 4.1, form II at pH 4.2, kinetic mechanism
4.2
-
-
2 forms differing in isoelectric point: form I has a pI at pH 4.1, form II at pH 4.2, kinetic mechanism
4.4
-
-
isoelectric focusing
5
-
-
isozyme AAT-2
5.54
-
-
isozyme AAT1
5.7
-
-
cytoslic isozyme
5.79
-
-
isozyme AAT2
6.3
6.8
-
microheterogenity of purified enzyme
6.3
-
-
microheterogeneity when submitted to chromatofocusing and/or isoelectric focusing analysis. Two main bands having pI = 6.8 and 6.3 are observed
6.3
-
-
isoelectric focusing, pH range 4.0-7.5, recombinant enzyme
6.5
-
-
isozyme AAT-1
6.8
-
-
microheterogeneity when submitted to chromatofocusing and/or isoelectric focusing analysis. Two main bands having pI = 6.8 and 6.3 are observed
6.8
-
-
theoretical value. The enzyme undergoes glycation when incubated with D-fructose leading to a shift down of pI
7
-
Leptosphaeria michotii
-
isozyme B
7.1
-
Leptosphaeria michotii
-
isozyme A
7.5
-
Q5F4K8
calculated from amino acid sequence
9.1
-
-
mitochondrial isozyme
9.6
-
-
pmAspAT
additional information
-
-
multiple forms/pIs of cytosolic isozyme
additional information
-
-
multiple forms of isozyme cAspAT and pAspAT have different isolelectric points, pI mAspAT: pH 4.93, pI cAspATs: pH 5.54-5.76, pI pAspATs: pH 4.94-5.13
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
differentiated from 3T3-L1 fibroblasts
Manually annotated by BRENDA team
-
isozyme Asp-DEAE-2
Manually annotated by BRENDA team
-
3T3-L1 cells, low activity
Manually annotated by BRENDA team
Leptosphaeria michotii
-
-
Manually annotated by BRENDA team
-
low activity
Manually annotated by BRENDA team
-
green, greening and etiolated: all isozymes, low content in etiolated leaves
Manually annotated by BRENDA team
-
cytosolic, mitochondrial and amyloplastidic isozymes
Manually annotated by BRENDA team
-
isozymes AAT1 and AAT2
Manually annotated by BRENDA team
P00507, -
premature and mature mitochondrial isozyme; premature and mature mitochondrial isozyme
Manually annotated by BRENDA team
-
cytosolic and mitochondrial isozymes, low content
Manually annotated by BRENDA team
-
isozyme Asp-DEAE-1
Manually annotated by BRENDA team
dolphin
-
-
Manually annotated by BRENDA team
Hypocrea rufa
-
-
Manually annotated by BRENDA team
Leptosphaeria michotii
-
-
Manually annotated by BRENDA team
Q7ZTK9
pronephric duct
Manually annotated by BRENDA team
-
low activity
Manually annotated by BRENDA team
-
cytosolic isozyme, low content
Manually annotated by BRENDA team
-
low activity
Manually annotated by BRENDA team
Spirodela polyrhiza SJ
-
-
-
Manually annotated by BRENDA team
-
3-days-old eggs
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Leptosphaeria michotii
-
isozymes A and B, major part
Manually annotated by BRENDA team
-
only form I occurs in chloroplast enriched fraction
Manually annotated by BRENDA team
-
isozyme pAspAT, multiple forms
Manually annotated by BRENDA team
-
24% activity is localized in chloroplasts
Manually annotated by BRENDA team
Spirodela polyrhiza SJ
-
24% activity is localized in chloroplasts
-
Manually annotated by BRENDA team
-
73% of total cellular content is localized in the cytoplasm
Manually annotated by BRENDA team
Spirodela polyrhiza SJ
-
73% of total cellular content is localized in the cytoplasm
-
Manually annotated by BRENDA team
dolphin
-
cytosolic isoenzyme
Manually annotated by BRENDA team
-
isoenzyme AAT-1 mainly in cytosol
Manually annotated by BRENDA team
-
cytosolic isoenzyme
Manually annotated by BRENDA team
-
multiple catalytically active forms of the cytosolic enzyme
Manually annotated by BRENDA team
Leptosphaeria michotii
-
isoenzyme A; isozymes A and B
Manually annotated by BRENDA team
-
cytosolic isoenzyme
Manually annotated by BRENDA team
Rhodotorula minuta, Torulopsis candida
-
cytosolic isoenzyme
Manually annotated by BRENDA team
-
multiple catalytically active forms of the cytosolic enzyme
Manually annotated by BRENDA team
-
cytosolic isoenzyme
Manually annotated by BRENDA team
-
multiple catalytically active forms of the cytosolic enzyme
Manually annotated by BRENDA team
-
cytosolic isoenzyme; multiple catalytically active forms of the cytosolic enzyme
Manually annotated by BRENDA team
-
multiple catalytically active forms of the cytosolic enzyme
Manually annotated by BRENDA team
-
cytosolic isoenzyme
Manually annotated by BRENDA team
-
cytosolic isoenzyme
Manually annotated by BRENDA team
-
cytosolic isoenzyme
Manually annotated by BRENDA team
-
cytosolic isoenzyme
Manually annotated by BRENDA team
-
cytosolic isoenzyme
Manually annotated by BRENDA team
Q964F0, Q964F1
enzyme is constitutively expressed
Manually annotated by BRENDA team
Q4D080, Q4D1Q4
enzyme is specifically induced in the mammalian stages of Trypanosoma cruzi
Manually annotated by BRENDA team
Bradyrhizobium japonicum 392
-
-
-
Manually annotated by BRENDA team
-
isozyme AAT-2, very low activity of isoenzyme AAT-1
Manually annotated by BRENDA team
dolphin
-
mitochondrial isoenzyme
Manually annotated by BRENDA team
-
isoenzyme AAT-2: major isoenzyme in mitochondria and peroxisomes
Manually annotated by BRENDA team
-
mitochondrial isoenzyme
Manually annotated by BRENDA team
-
mitochondrial isoenzyme
Manually annotated by BRENDA team
-
mitochondrial isoenzyme
Manually annotated by BRENDA team
Leptosphaeria michotii
-
isozyme B
Manually annotated by BRENDA team
-
mitochondrial isoenzyme
Manually annotated by BRENDA team
-
mitochondrial isoenzyme
Manually annotated by BRENDA team
Torulopsis candida
-
-
Manually annotated by BRENDA team
-
form II and III in poorly resolved plastid and mitochondrial fraction; mitochondrial isoenzyme
Manually annotated by BRENDA team
-
form I and II occurs in chloroplast-enriched fraction
Manually annotated by BRENDA team
-
mitochondrial isoenzyme; multiple catalytically active forms of mitochondrial isozyme
Manually annotated by BRENDA team
-
multiple catalytically active forms of mitochondrial isozyme
Manually annotated by BRENDA team
-
mitochondrial isoenzyme
Manually annotated by BRENDA team
-
mature mAspAT and premature pmAspAT forms of the isozyme
Manually annotated by BRENDA team
-
mitochondrial isoenzyme
Manually annotated by BRENDA team
-
mature mAspAT and premature pmAspAT forms of the isozyme
Manually annotated by BRENDA team
P00507, -
mature isozyme mAAT; mitochondrial isoenzyme
Manually annotated by BRENDA team
-
2.8% activity is localized in mitochondria
Manually annotated by BRENDA team
Q964F0, Q964F1
enzyme is down-regulated in bloddstream forms of Trypanosoma brucei
Manually annotated by BRENDA team
Q4D080, Q4D1Q4
enzyme is constitutively expressed
Manually annotated by BRENDA team
-
AAT-2: major isoenzyme in mitochondria and peroxisomes, very low activity of AAT-1
Manually annotated by BRENDA team
-
form II and III in poorly resolved plastid and mitochondrial fraction
Manually annotated by BRENDA team
-
nuclear-encoded protein that is translated on cytosolic ribosomes and subsequently imported into plastids
Manually annotated by BRENDA team
Spirodela polyrhiza SJ
-
2.8% activity is localized in mitochondria
-
Manually annotated by BRENDA team
additional information
P00507, -
cytosolic and mitochondrial isozymes bind differently to the 70 kDa heat shock protein Hsp70, which regulates the folding and aggregation process of polypeptides, sequence and distribution of Hsp70-binding regions allow the classification of isozymes into a phylogenetic tree, overview; cytosolic and mitochondrial isozymes bind differently to the 70 kDa heat shock protein Hsp70, which regulates the folding and aggregation process of polypeptides, sequence and distribution of Hsp70-binding regions allow the classification of isozymes into a phylogenetic tree, overview
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli O44:H18 (strain 042 / EAEC)
Escherichia coli O44:H18 (strain 042 / EAEC)
Giardia intestinalis (strain ATCC 50803 / WB clone C6)
Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Staphylococcus aureus (strain NCTC 8325)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
40000
-
-
SDS-PAGE
43000
-
-
SDS-PAGE
44600
-
-
SDS-PAGE
45300
-
-, Q4LDF8
calculated from sequence of cDNA
45620
-
-
electrospray mass spectrometry
46410
-
-
deduced from cDNA
49100
-
Q939C9
calculated from cDNA
52000
-
-
isozyme AST II, gel filtration
52800
-
Q9SIE1
calculated from amino acid sequence
52800
-
-
calculated from amino acid sequence
52800
-
Q5F4K8
calculated from amino acid sequence
53000
-
Q9SIE1
SDS-PAGE
53000
-
-
SDS-PAGE
53000
-
Q5F4K8
SDS-PAGE
55000
-
Q939C9
SDS-PAGE
57000
-
-
gel filtration, gradient PAGE
64200
68200
-
gel filtration, PAGE, diffusion and sedimentation equilibrium
80000
84000
-
gel filtration, meniscus depletion sedimentation equilibrium method
80000
-
-
meniscus depletion sedimentation equilibrium method
80000
-
-
gel filtration
80000
-
-
isozymes AAT-2a, 2b and 2c, gel filtration
82000
-
-
PAGE
84000
-
-
meniscus depletion sedimentation equilibrium method
84000
-
-
cytosolic isozyme, gel filtration
85000
-
-
gel filtration
86000
-
-
mitochondrial isozyme, gel filtration
86000
-
-
cytosolic isozyme, gel filtration
87000
-
-
SDS-PAGE
87100
-
-
sedimentation equilibrium analysis
88000
-
-
gel filtration; isozyme AAT-1
88000
-
-
gel filtration; mitochondrial isozyme
88000
-
-
isozyme AAT1, gel filtration
88900
-
-
cytosolic isozyme, sedimentation equilibrium
90000
92000
-
gel filtration, sedimentation equilibrium analysis
90000
-
-
analytical ultracentrifugation
91000
-
-
mitochondrial isozyme, sedimentation equilibrium analysis
92000
-
Leptosphaeria michotii
-
isozymes A and B, PAGE, gel filtration
92000
-
-
isozyme AAT2, gel filtration
92000
-
-
mitochondrial form, SDS-PAGE
93150
-
-
amino acid sequence
94000
-
-
isozyme AAT-2, gel filtration
94000
-
-
cytosolic isozyme, sedimentation equilibrium analysis
95000
-
Torulopsis candida
-
cytosol, gel filtration
96000
-
-
isozyme AAT-P2, gel filtration
97000
98000
-
gel filtration, sedimentation equilibrium
98000
-
-
cytoplasmic form, SDS-PAGE
100000
-
-
gel filtration
100000
-
-
gel filtration
100000
-
-
gel filtration
100000
-
-
gel filtration
103000
-
-
gel filtration
105000
-
-
gel filtration, isozyme AAT-P2
108000
-
-
gel filtration
111000
-
-
native PAGE
112000
-
-
isozyme AAT1, native PAGE
120000
-
Q5F4K8
gel filtration
120000
-
-
gel filtration
130000
-
-
sedimentation equilibrium centrifugation
136000
-
-
isozyme AAT2, native PAGE
138000
-
-
gel filtration
162000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 43000, SDS-PAGE
?
-
x * 44000-45000, isoymes AAT1, AAT2 and AAT5, SDS-PAGE
?
-
x * 47000, premature mitochondrial isozyme pmAspAT, SDS-PAGE
?
-
x * 43776, recombinant enzyme, DNA sequence determination and mass spectrometry
?
P14909
x * 45705, calculated from sequence
?
-
x * 53000, SDS-PAGE
?
Pseudoalteromonas haloplanktis TAC 125
-
x * 43776, recombinant enzyme, DNA sequence determination and mass spectrometry
-
?
Sulfolobus solfataricus MT4
-
x * 45705, calculated from sequence
-
?
Sulfolobus solfataricus MT-4
-
x * 53000, SDS-PAGE
-
dimer
-
2 * 44000, mitochondria, SDS-PAGE
dimer
-
2 * 46344, amino acid sequence
dimer
-
2 * 44000, isozyme AAT-1, SDS-PAGE; 2 * 47000, AAT-2, SDS-PAGE
dimer
-
2 * 42000-45000, SDS-PAGE
dimer
-
2 * 45400, mitochondrial isozyme, SDS-PAGE; 2 * 46300, cytosolic isozyme
dimer
-
2 * 41000, cytosolic isozyme, SDS-PAGE; 2 * 43400, mitochondrial isozyme, SDS-PAGE
dimer
-
2 * 46500, SDS-PAGE
dimer
-
2 * 42000, SDS-PAGE
dimer
-
2 * 53000; 2 * 53000, SDS-PAGE
dimer
-
2 * 44000, mitochondria, SDS-PAGE; 2 * 46000, cytosol, SDS-PAGE
dimer
Torulopsis candida
-
2 * 46000, cytosol, SDS-PAGE
dimer
-
2 * 40000, SDS-PAGE
dimer
-
2 * 42000, SDS-PAGE
dimer
-
2 * 46470, SDS-PAGE
dimer
-
-
dimer
-
2 * 43000, SDS-PAGE
dimer
-
2 * 40000, isozymes AAT-2a, 2b and 3c, SDS-PAGE
dimer
-
2 * 65000, SDS-PAGE
dimer
-
2 * 32500, SDS-PAGE
dimer
-
AAT-P2 und AAT-P2
dimer
-
2 * 45000, SDS-PAGE
dimer
-
2 * 42000, SDS-PAGE
dimer
-
2 * 52200, isozyme AAT1, SDS-PAGE; 2 * 54800, isozyme AAT2, SDS-PAGE
dimer
-
2 * 43500, SDS-PAGE
dimer
D3H0F7
-
dimer
-
2 * 42000, SDS-PAGE
-
dimer
Chlamydomonas reinhardtii 6145c
-
2 * 65000, SDS-PAGE
-
dimer
Haloferax mediterranei R-4
-
2 * 32500, SDS-PAGE
-
dimer
Pseudomonas putida IFO 12996
-
-
-
dimer
Trichomonas vaginalis Bushby
-
2 * 44000, mitochondria, SDS-PAGE
-
homodimer
-
-
homodimer
O96142
-
monomer
-
1 * 50000, SDS-PAGE
monomer
-
1 * 50000, SDS-PAGE
monomer
Q939C9
-
tetramer
-
4 * 43000, SDS-PAGE
tetramer
Methanothermobacter thermautotrophicus SF-4
-
4 * 43000, SDS-PAGE
-
monomer
Methanothermobacter thermautotrophicus SF-4
-
1 * 50000, SDS-PAGE
-
additional information
-
structure modeling, subunit organization
additional information
Pseudoalteromonas haloplanktis TAC 125
-
structure modeling, subunit organization
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
side-chain modification
-
two partially modified lysine residues at positions 202 and 384 converted to their N-epsilon-methyl derivatives
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
vapour diffusion method, 10 mM NaOH-glycine, pH 9.1, polyethylene glycol 4000 18% w/v, 1 week, X-ray analysis
-
crystallization of V39F AspAT is performed by the hanging drop vapor diffusion method
-
crystals are grown at 19C by the hanging-drop technique, unliganded and hydrocinnamate complex of V39L/K41Y/T47I/N69L/T109S/A293D/N297S, hydrocinnamate complex and maleate complexes of A12T/P13T/N34D/T109S/G261A/S285G/N297S and the hydrocinnamate complex of A12T/P13T/N34D/T109S/G261A/S285G/A293D/N297S
-
hanging drop vapour diffusion, crystals of mutants P195A and P138A/P195A in complex with maleate, protein solution: 20 mg/ml, 10 mM potassium phosphate, 0.01 mM pyridoxal 5'-phosphate, 2 mM EDTA, 0.5 mM DTT, reservoir solution: 1.9-2.1 M ammonium sulfate, 0.2 M 2-methylmorpholine, 2% polyethylene glycol 400, mutant P138A/P195A is also crystallized in complex with maleate, 20 mM, X-ray diffraction structure analysis
-
purified mutant K258A, batch method, protein solution: 5.2 mg/ml, 50 mM potassium phosphate, pH 7.5, 53% ammonium sulfate, room temperature, 1 week, preparation of crystals with heavy atom derivatives by soaking crystals for 24 or 48 h, structure analysis
-
purified mutant V39L, hanging drop method, room temperature, protein solution: 12.5 mg/ml, 20 mM sodium phosphate, pH 7.5, 30 mM maleate, 0.4 M sodium chloride, 12.5% w/v polyethylene glycol 4000, reservoir solution: 23-25% w/v polyethylene glycol 4000, 0.8 M sodium chloride, 20 mM sodium phosphate, pH 7.5, X-ray diffraction structure determination
-
sitting drop method, protein solution: 30 mg/ml, 10 mM potassium phosphate, pH 7.0, 0.01 mM pyridoxal 5'-phosphate, 1 mM EDTA, 2 mM succinate, 0.3 mM azide, reservoir solution: same composition as protein solution, contains no protein but polyethylene glycol 4000, 11-17% w/v, 20C, stepwise addition of protein solution, X-ray diffraction analysis
-
the crystal triple mutant I33Q/Y214Q/R280Y is determined to relate the observed changes in reaction kinetics to the changes in active-site structure
-
the crystals of AspATs reconstituted with phosphopyridoxyl-L-Glu, phosphopyridoxyl-D-Glu, and phosphopyridoxal-2-methyl-L-glutamate are obtained by the hanging drop vapor diffusion method using ammonium sulfate as the precipitant. Crystals of suitable size for diffraction experiments are obtained within a week. The crystal structures of the complexes of aspartate aminotransferase with phosphopyridoxyl derivatives of L-glutamate, D-glutamate, and 2-methyl-L-glutamate are solved as the models for the external aldimine and ketimine complexes of L-glutamate. All the structures are in the closed form, and the two carboxylate groups and the arginine residues binding them are superimposable on the external aldimine complex with 2-methyl-L-aspartate
-
two nearly identical crystal structures of the complexes between (S)-4-amino-4,5-dihydro-2-furancarboxylic acid and L-AspAT obtained at pH 7.5 and 8 are shown. The inhibitor forms only one adduct with the enzyme, with active site lysine 246, thus irreversibly inactivating the L-AspAT transamination reaction
D3H0F7
vapour diffusion technique, protein solution: 10 mg/ml, 10 mM potassium phosphate,pH 7.0, 2.5 mM pyridoxal 5'-phosphate, 2.5% polyethylene glycol w/v, 4C, 7-10 days
-
purified cytosolic enzyme, variation of crystallization conditions resulting in different crystal types, influence of various divalent metal ions, dioxane and non-ionic detergent beta-octylglucoside, structure analysis
-
vapour diffusion method with hanging drops, protein solution: 10 mg/ml, 50mM sodium phosphate, pH 7.5, 8-24% polyethylene glycol 2000-20000, reservoir solution: 8-24% polyethylene glycol 2000-20000, equal amounts, room temperature, X-ray structure analysis
-
concentrated isoenzyme AAT-1 solution, 10 mM Tris-HCl, pH 8.0, 1 mM 2-oxoglutarate, 2 mM KOH, 0.01 pyridoxal 5'-phosphate, 0.01% 2-mercaptoethanol, polyethylene glycol 6000 8% w/v, 4C, 6 days; concentrated isoenzyme AAT-2 solution, 10 mM potassium phosphate, pH 7.0, 1 mM 2-oxoglutarate, 2 mM KOH, 0.001 mM pyridoxal 5'-phosphate, 0.01% 2-mercaptoethanol, dialysis against distilled water at 4C for 3 days
-
crystalized to a maximum resolution of 2.8 A
-
the X-ray structure of the PfAspAT homodimer at a resolution of 2.8 A is reported. While the overall fold is similar to the currently available structures of other AspATs, the structure presented shows a significant divergence in the conformation of the N-terminal residues
O96142
concentrated protein solution, potassium phosphate 0,01 M, pH 7.2, 0.01 mM pyridoxal 5'-phosphate, ammonium sulfate
-
hanging drop vapour diffusion and sitting drop vapour diffusion using 23.6% (w/v) PEG 4000, 0.1 M HEPES pH 8.0
-
crystals of cytosolic enzyme, or enzyme in complex with substrates, N-methylpyridoxal, and inhibitors, depression-plate and sandwich-box techniques, protein solution: 35-40 mg/ml, pH 5.4, 40 mM sodium acetate, 4% polyethylene glycol 4000-6000, with or without substrate, cofactor or inhibitor compounds, reservoir solution: 40 mM sodium acetate, pH 5.4, 8% polyethylene glycol 4000-6000, crystals appear within 1 week, spectroscopic analysis
-
crystals of enzyme-inhibitor complex, sitting drop vapour diffusion method, 4C, protein solution: 7 mg/ml, polyethylene glycol 4000 11% w/v, 50 mM potassium phosphate, pH 7.5, reservoir solution: polyethylene glycol 4000 22% w/v, 50 mM potassium phosphate, pH 7.5, X-ray structure analysis
-
forced dialysis lead to crystal formation or pure protein, 8.5 mg/ml, in solution for microdiffusion, 53% (NH4)2SO4 and pH 6.0-7.0, 4C, 2 months
-
vapour diffusion method with hanging drops, crystals from solution: 10 mg/ml protein, polyethylene glycol 4000 16-17% w/v, 10 mM sodium phosphate, pH 7.5, injection of seed crystal into the hanging drop of chicken mitochondrial aspartate aminotransferase
-
vapour diffusion method with hanging drops, crystals from solution: polyethylene glycol 4000 17% w/v, 10 mM glycine/NaOH, pH 9.1, microspectrophotometric equilibrium and kinetic analysis
-
native and selenomethionine-substituted TT0402 proteins are crystallized in hanging drops at 4C
-
equilibrium diffusion in a sitting drop, ammonium sulfate solution
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
2
-
-
irreversibly destroyed below
3.3
-
-
1 h, 10% loss of activity of cytoplasmic enzyme, 40% loss of activity of mitochondrial enzyme
5
-
-
irreversible inactivation
6
11
-
37C, 1 h, stable
12
-
-
irreversibly destroyed above
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
37
-
Hypocrea rufa
-
relatively stable
37
-
-
1 h, pH 6.0-11.0, stable
40
-
-
pH 7.5, 1 h, gradual loss of activity above
50
65
-
recombinant enzyme, transition temperature
50
-
Hypocrea rufa
-
30 min, 20% loss of activity
50
-
-
under physiological or nearly physiological conditions, 3.5 M KCl, pH 7.8, stable for several h
50
-
-
15 min, 10% loss of activity for the mitochondrial isozyme, 80% loss of activity with aspartate for the cytosolic isozyme
50
-
-
t1/2: 6.8 min
50
-
-
isozyme AST II, 15 min, stable
50
-
-
isozyme AAT1 t1/2: 3.6 min, isozyme AAT2 t1/2: 41.2 min
50
-
Q939C9
enzyme stable up to 50C
55
-
-
10 min, 48% loss of activity with tyrosine, 36% loss of activity with phenylalanine
55
-
-
30 min, isoenzyme I: completely stable, isoenzyme II: 31% loss of activity, isoenzyme III: 67% loss of activity
60
-
Hypocrea rufa
-
30 min, 75% loss of activity
60
-
-
15 min, stable
60
-
-
5 min, more than 90% loss of activity
65
-
-
inactivation, isozymes AAT 1 and 2
65.5
-
-
recombinant enzyme, melting temperature
70
-
Hypocrea rufa
-
30 min, 80% loss of activity
70
-
-
15 min, mitochondrial enzyme completely destroyed
70
-
-
pH 7.5, 1 h, enzyme loses 65% of activity; pH 7.5, 1 h, stable up to
70
-
-
pH 7.5, 1 h, stable up to
70
-
-
t1/2 wild-type of mature mitochondrial isozyme: 2.7 min
70
-
-
5-10 min, 50% residual activity; moderately thermostable, retaining about 50% of its activity after incubation at 70C for 5-10 min
75
-
-
stable up to
75
-
-
no significant decrease in the enzyme activity even after 30 min of incubation at 75C
78.5
-
-
denaturation
80
-
-
20 min, 35% loss of activity
80
-
-
10 min, 75% remaining activity
80
-
-
isozyme AST II, loss of 89% activity
90
-
-
6 h, stable; 6 h, stable
100
-
-
2 h, 50% inactivation; t1/2: 2 h
100
-
-
the enzyme retains its structure at 100C
100
-
-
enzymes starts to precipitate at temperatures above 100C
additional information
-
-
2-oxoglutarate protects against thermal inactivation
additional information
-
-
cysteine sulfinic acid protects against heat inactivation
additional information
-
-
-
additional information
-
-
no difference in thermostability between plants of genotypes acclimated at 4 different thermoperiods
additional information
-
-
thermal denaturation is not reversible, denaturation temperature of holoenzyme is 78.5C
additional information
-
-
high thermostability, extra prolyl residues, located at the surface of the protein, are involved; thermal denaturation is irreversible
additional information
-
-
2-oxoglutarate protects against thermal inactivation
additional information
-
-
the premature form of the mitochondrial isozyme is more thermostable than the mature form
additional information
-
-
presence of pyridoxal 5'-phosphate significantly increases the thermostability
additional information
-
-
structural stability of the enzyme is investigated by coupling isothermally and thermally induced denaturation studies to molecular modeling. Gel filtration analysis indicates that the enzyme unfolds with an N2 reversible 2D mechanism. In the molecular model, a cluster of hydrophobic residues is shown at the interface between the subunits of the enzyme and suggests this cluster as a structural feature stabilizing the enzyme quaternary structure
additional information
-
-
thermophilicity, short-term and long-term thermostability of isoenzymes are independently evaluated and the influence of a cysteine residue on the three properties is assessed
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
labile enzyme is stabilized by pyridoxyl 5'-phosphate and L-aspartate
-
2-oxoglutarate does not protect against heat inactivation
-
addition of glycerol, DTT and pyridoxal 5'-phosphate to buffers, required for stabilization during purification
-
aspartate, 10 mM, or pyridoxal 5'-phosphate, 0.2 mM protects against heat inactivation
-
2-oxoglutarate stabilizes against thermal inactivation
-
inactivation at 1.3 M NaCl and KCl
-
complete loss of activity after freezing and thawing
-
2-oxoglutarate stabilizes against thermal inactivation
-
cysteinic acid protects the cytosolic isoform against thermal denaturation, not aspartate or 2-oxoglutarate
-
enzyme is stabilized by the intramitochondrial chaperone homologues GroEL and GroES
-
AspATSs, when incubated at 37C in the presence of trypsin, is cleaved after Lys32 and Lys33 and looses its activity. At 37C, substrates are not able to protect the enzyme from proteolysis, while at 75C the presence of substrates lowers the inactivation rate about 4fold
-
presence of substrates renders AspATSs less sensitive to thermolysin, possibly by inducing a conformational transition
-
35% decrease in activity after 5 days under the influence of 50 mM D-fructose, 46% decrease in activity under the influence of 500 mM D-fructose.The enzyme undergoes glycation when incubated with D-fructose leading to a shift down of pI. Uric acid has a protective effect against late glycation
-
ORGANIC SOLVENT
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
guanidine-HCl
-
4.0-6.0 M, 1 h, complete denaturation. SsAspAT is fully unfolded in the presence of denaturant concentrations higher than 3.5 M; at 25C, the enzyme from Sulfolobus solfataricus is less resistant to guanidinium chloride-induced denaturation than the cytosolic mesophilic aspartate aminotransferase from pig heart
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
0C, stable for at least several h in solution
-
-20C, protein concentration above 10 mg/ml
-
enriched enzyme is stable and can be stored at 4C or -20C for many weeks
-
-70C, 0.7-0.9 mg/ml protein in 20 to 40 mM sodium phosphate buffer, pH 7.0, 0.01 mM pyridoxal phosphate, 1 mM 2-oxoglutarate
-
4C, 0.01 M potassium phosphate buffer, pH 7.0, 0.001 mM pyridoxal 5'-phosphate, 75% ammonium sulfate, stable for several months
-
4C, stable for several weeks
-
4C, partially purified cytosolic isozyme, stable for 1 month, gradual decrease of activity afterwards
-
-80C, stable for at least 1 year
-
-20C or 4C, stable for at least 2 weeks
-
-20C, protein concentration up to 2 mg/ml, 30-40% loss of activity per month
-
0-4C, 50% glycerol, 1 day, remains active, (cytoplasmic enzyme)
-
0-4C, 50% glycerol, 3-5 h, remains active, (mitochondrial enzyme)
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
recombinant isozymes AAT1, AAT2 and AAT5 from Escherichia coli
-
isoenzymes: Asp-DEAE-1 and Asp-DEAE-2
-
isoenzyme I and II
-
380fold
-
partial, 92fold
-
partial, cytosolic, 171fold, and mitochondrial, 78fold, isozymes
-
by anion-exchange chromatography
-
cytosolic form I, and mitochondrial forms II and III
-
cytosolic and mitochondrial isozymes
dolphin
-
isoenzymes: AspAT-1, AspAT-2, AspAT-3
-
crystal structures of the internal aldimine and the stable L-aspartate external aldimine of Escherichia coli AAT reconstituted with deazaPLP at 1.8 A resolution is reported. Crystals are obtained by the hanging drop method
-
EcAspAT is purified by anion exchange chromatography in a Fractogel EMD DEAE 650-S column, pooled fractions are dialyzed against 20 mM sodium phosphate, pH 7.5, and loaded onto a ceramic hydroxyapatite column
-
isoenzymes A and B
-
mutant V39L
-
Ni-NTA Superflow resin chromatography
-
recombinant wild-type and mutants from overexpressing strain MG204
-
recombinantly overexpressed enzyme
-
cytosolic isozyme; mitochondrial isozyme
-
mitochondrial isozyme
-
recombinant mAspAT, pmAspAT and mutants from Escherichia coli
-
1 cytosolic isozyme, partial, 120fold
-
isoenzyme mitAAT DEAE-Sepharose column chromatography
-
partial, 404fold, cytosolic isozyme
-
isozyme AST II, 30.25fold
-
partial
Hypocrea rufa
-
2 forms: A and B
Leptosphaeria michotii
-
isozymes AAT1 and AAT2
-
isoenzymes: AAT-P1 and AAT-P2, partial
-
cytosolic isozyme: multiple forms AAT-2a, AAT-2b, AAT-2c
-
DEAE-Sepharose column chromatography and Phenyl-Sepharose column chromatography
-
mitochondrial and cytosolic isozymes
-
2 isoenzymes: AAT-1, AAT-2
-
cytosolic isozyme
-
mitochondrial isozyme, 57.3fold
-
isozymes mAsp-AT, cAsp-AT, and pAspAT from young green leaves
-
His-tag affinity chromatography and gel filtration
Q5F4K8
Ni-NTA affinity chromatography and DEAE Sephacel column chromatography; recombinant protein, rapid protocol for purification
-
using Ni-NTA chromatography, anion-exchange chromatography and gel filtration
-
partial purification of native enzyme, purification of recombinant enzyme from Escherichia coli
-
DEAE-Sepharose column chromatography and Phenyl-Sepharose column chromatography
-
differential centrifugation, Sephadex G-25 gel filtration, DEAE cellulose ion exchange chromatography, and Sephadex G-150 gel filtration
-
mitochondrial and cytosolic isozymes
-
mitochondrial isozyme
-
2 isozymes
-
Sephadex G-25 gel filtration and DEAE-Toyopearl column chromatography
-
nickel Sepharose 6 fast flow chromatography and S-75 gel filtration
-
; recombinant protein
-
large-scale
-
recombinant from overproducing Escherichia coli AB1157 cells, 66fold
-
mitochondrial isoform
Torulopsis candida
-
200-1000fold, copurification with the aromatic amino acid aminotransferase 2.6.1.57
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
AAT1, AAT2, and AAT5, overexpression in Escherichia coli strains
-
aspartate aminotransferase construct consists of the Arabidopsis thaliana ASP5 coding region followed by mGFP5. This construct is designated SP5:GFP. GFP is fused to the carboxy-terminus of ASP5 to preserve the cleavage site between the ASP5 transit peptide and mature protein, thus ensuring proper plastid import and processing. A five amino acid linker peptide (GSGGG) is inserted between ASP5 and GFP to promote proper folding and activity of both proteins. The constructs are introduced into Nicotiana tabacum cv. Samsun NN via Agrobacterium-mediated transformation of leaf strips. ASP5:GFP is present in stromules of Nicotiana tabacum. Arabidopsis thaliana ASP5, with GFP fused to its carboxy-terminus, can interact with itself and with the Nicotiana tabacum AAT3 to form enzymes that are functional in vitro
-
expressed in Escherichia coli as a His-tagged fusion protein
Q939C9
overexpressed in Escherichia coli
-
expressed in Escherichia coli
-
expressed in Escherichia coli strain MG204
-
overexpression from plasmid in strain JM103
-
overexpression of wild-type enzyme and mutants from plasmid in Escherichia coli strain MG204, which lacks endogenous enzyme activity
-
expression of wild-type mAspAT and pmAspAT and mutants in Escherichia coli
-
cloning and DNA-sequencing of cDNA encoding the plastidic isozyme pAspAT, DNA and amino acid sequence analysis
-
expressed in Escherichia coli
Q5F4K8
expressed in Escherichia coli; expression in Escherichia coli
-
expressed in Escherichia coli as a His-tagged fusion protein
-
isolation of genomic DNA and construction of a genetic library, cloning of gene PhaspC, DNA and amino acid sequence determination, overexpression in Escherichia coli strain TY103
-
cloning of a liver cDNA fragment, nucleotides 1-419, into a plasmid for production of cRNA probes
-
expressed in Escherichia coli BL21 (DE3) cells
-
expression in Escherichia coli
-
cloning, DNA and amino acid sequence determination and analysis, overexpression in Escherichia coli AB1157
-
expression in Escherichia coli
-
gene aspC, expression of wild-type and K109 mutants in Escherichia coli BL21(DE3)
Q56232
expression in Escherichia coli, His-tagged protein; expression in Escherichia coli, His-tagged protein
Q964F0, Q964F1
expression in Escherichia coli, His-tagged protein; expression in Escherichia coli, His-tagged protein
Q4D080, Q4D1Q4
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
circulating osteocalcin concentration is negatively associated with aspartate transaminase levels
-
expression of AAT in Pseudomonas syringae is transiently enhanced when cells are shifted from 22 to 4C
-
no expression at gastruala and neurula stage, low expression in somites at end of neurulation or early tail-bud stage
Q7ZTK9
high expression after neurulation in somites
Q7ZTK9
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
D232N
Q939C9
mutant shows no activity
K270H
Q939C9
mutant shows no activity
R403Y
Q939C9
mutant shows no activity
A12T/P13T/N34D/T109S/G261A/S285G/A293D/N297S
-
mutant enzyme has nearly the same ratio of kcat/Km(Phe) to kcat/Km(Asp) as that of wild-type enzyme. The additional mutation A293D compared to mutant enzyme A12T/P13T/N34D/T109S/G261A/S285G/N297S holds the Arg292 side chain away from the active site to allow increased specificity for phenylalanine over aspartate
E265K
-
site-directed mutagenesis, reduced kcat, reduced Km for L-aspartate and 2-oxoglutarate
E265Q
-
site-directed mutagenesis, reduced kcat, reduced Km for L-aspartate and 2-oxoglutarate
I33Q/Y214Q/R280Y
-
substitution of three active-site residues in Escherichia coli L-aspartateartate aminotransferase highly reduces kcat for transamination reaction. Ratio of L-cysteine sulfinate desulfinase to transaminase activity is increased by 100000fold in mutant. kcat for desulfination of L-cysteine sulfinate increases to 0.5/sec (from 0.05/sec in wild-type enzyme). kcat for beta-decarboxylation of L-aspartateartate increases from below 0.0001/sec to 0.07/sec
K258A
-
exchange of active site lysine for alanine, binds still pyridoxal 5'-phosphate or pyridoxamine 5'-phosphate, but not covalently, the latter forms when bound to the enzyme a covalent stable ketimine with 2-oxoglutarate and effects a beta-decarboxylation of oxaloacetate, followed by transamination to give the pyridoxal 5'-phosphate aldimine of alanine as a final product
K68E
-
site-directed mutagenesis, reduced kcat, reduced Km for L-aspartate and increased Km for 2-oxoglutarate
K68E/E265K
-
site-directed mutagenesis, charge exchange in the conserved intrasubunit salt bridge, reduced kcat, reduced Km for L-aspartate and 2-oxoglutarate
K68M
-
site-directed mutagenesis, reduced kcat, reduced Km for L-aspartate and increased Km for 2-oxoglutarate
K68M/E265Q
-
site-directed mutagenesis, introduction of a neutral amino acid pair in the conserved intrasubunit salt bridge, reduced kcat, reduced Km for L-aspartate and 2-oxoglutarate
P138A
-
oligonucleotide-directed mutagenesis, no significant effect, unaltered compared to the wild-type
P138A/P195A
-
oligonucleotide-directed mutagenesis
P195A
-
oligonucleotide-directed mutagenesis, no significant effect, unaltered compared to the wild-type
R292E/L18H
-
12.9fold increase in specific activity towards L-Lys and 2-oxo-4-phenylbutanoic acid
T70F
-
nearly no activity with L-erythro-3-hydroxyaspartate, in opposite to the wild-type, altered reaction kinetics due to inability to stabilize the reaction quinonoid intermediate
V39F
-
mutant enzyme shows a more open conformation, and the aldimine pKa is lowered by 0.7 unit compared with the wild-type enzyme. The maleate-bound V39F enzyme shows the aldimine pKa 0.9 unit lower than that of the maleate-bound wild-type enzyme. The maleate-bound V39F enzyme shows an altered side-chain packing pattern in the 3739 region, and the lack of repulsion between Gly38 carbonyl O and Tyr225 seems to be the cause of the reduced pKa value
V39F/N194A
-
mutation does not decrease the aldimine pKa, showing that the domain rotation controls the aldimine pKa via the Arg386-Asn194 pyridoxal 5'-phosphate linkage system
V39L
-
crystal structure analysis
V39L/K41Y/T47I/N69L/T109S/A293D/N297S
-
the additional mutation A293D compared to mutant enzyme V39L/K41Y/T47I/N69L/T109S/N297S holds the Arg292 side chain away from the active site to allow increased specificity for phenylalanine over aspartate
Y225R/R292K/R386A
-
the mutation converts its activity into an aspartate 4-decarboxylase
C166A
-
site-directed mutagenesis of isozyme mAspAT, decreased ability to undergo transition from the open to the closed conformation essential for the reaction mechanism, reduced reactivity with DTNB
DELTA1-13
O96142
truncation of these noncatalytic residues reduces enzyme activity and a peptide containing these amino acids inhibits PfAspAT in vitro and in the lysate of cultured parasites
DELTA1-7
O96142
truncation of the first seven amino acids only minorly reduces enzymatic activity
K109S
Q56232
site-directed mutagenesis, loss of activity towards acidic substrates, increased activity towards the neutral substrate alanine, increase in pKa value
K109V
Q56232
site-directed mutagenesis, loss of activity towards acidic substrates, increased activity towards the neutral substrate alanine
C166S
-
site-directed mutagenesis of isozyme mAspAT, decreased ability to undergo transition from the open to the closed conformation essential for the reaction mechanism, reduced reactivity with DTNB
additional information
-
construction of deletion mutant DELTA3-11mAspAT of isozyme mAspAT, enhanced thermostability, reduced kcat and Km, enhanced reactivity of Cys166 with DTNB
Renatured/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
at 7 M urea and 25C
-
in the presence of 0.01 mM pyridoxal 5'-phosphate
-
reversible dissociation and unfolding of the dimeric enzyme by guanidine hydrochloride
-
wild-type and mutants, unfolding by guanidinium hydrochloride and renaturing kinetics, fluorescent spectrometric analysis
-
reconstitution of holoenzyme after purification of apoenzyme with pyridoxal 5'-phosphate; thermal denaturation is not reversible
-
thermal denaturation is not reversible
-
guanidinium hydrochloride denatured premature form pmAspAT cannot refold at 30C, but refolds rapidly in presence of the intramitochondrial chaperone homologues GroEL and GroES
-
unfolding in 6 M guanidine hydrochloride for different periods of time. Reactivation of equilibrium-unfolded mAAT is sigmoidal, reactivation of the short term unfolded protein displays a double exponential behavior consistent with the presence of fast and slow refolding species. The presence of coenzyme does not perturb the kinetics or pathway of refolding. Covalently attached PLP slows down the interconversion between fast and slow folding populations of unfolded states. Additional structural rearrangements occurring both in the unfolded state and in populations of folding intermediates along the folding pathway
-
reconstitution of holoenzyme with pyridoxal 5'-phosphate or pyridoxamine 5'-phosphate
-
refolding of SsAspAT can be accelerated by increasing the temperature from 25 to 50C. Although refolding is faster at 50C (35% of native enzyme) the highest yield of renaturation is obtained at 37C (70% reactivation), similar to the yield of 65% of initial activity that is obtained at 25C
-
reconstitution of holoenzyme after purification of apoenzyme with the inhibitor N-5'-phosphopyridoxyl L-aspartate
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
synthesis
-
mutant enzyme R292E/L18H can use L-lysine as inexpensive amino donor for the production of L-homophenylalanine. The low solubility of product L-homophenylalanine and spontaneous cyclization of 2-keto-6-aminocaproate drive the reaction completely towards production of L-homophenylalanine
medicine
-
the inhibitor of C-S lyase, aminooxyacetic acid hemihydrochloride, reduces renal injuries due to cisplatin in rats. On day 5 following a bolus cisplatin injection, in vivo nephrotoxic potentials are in the decreasing order of species rats > mice, rabbits, based on body surface. The levels of renal Pt residue at the nephrotoxic dose are in order of rabbits > rats > mice. The activity of endogenous basal mitochondrial aspartate aminotransferase, one of the C-S lyases, in the renal cortex of naive animals is rats > mice, rabbits. Expression of mitochondrial C-S lyase in the kidney is observed at approximately 37 kDa in all five species used. In in vitro studies, the cytotoxicity of cisplatin is dependent on the expression level of C-S lyase mRNA in the respective renal cells
medicine
P00507
the inhibitor of C-S lyase, aminooxyacetic acid hemihydrochloride, reduces renal injuries due to cisplatin in rats. On day 5 following a bolus cisplatin injection, in vivo nephrotoxic potentials are in the decreasing order of species rats > mice, rabbits, based on body surface. The levels of renal Pt residue at the nephrotoxic dose are in order of rabbits > rats > mice. The activity of endogenous basal mitochondrial aspartate aminotransferase, one of the C-S lyases, in the renal cortex of naive animals is rats > mice, rabbits. Expression of mitochondrial C-S lyase in the kidney is observed at approximately 37 kDa in all five species used. In in vitro studies, the cytotoxicity of cisplatin is dependent on the expression level of C-S lyase mRNA in the respective renal cells
biotechnology
-
an enzymatic method for the synthesis of the amino acid Phe is developed. AAT from porcine heart is immobilized by covalent attachment and entrapment, and the resulting immobilized preparations are compared to the soluble enzyme both in terms of stability and reaction efficiency