| Entry |
|
|---|
| Name |
alanine transaminase;
glutamic-pyruvic transaminase;
glutamic-alanine transaminase;
GPT;
beta-alanine aminotransferase;
alanine aminotransferase;
alanine-alpha-ketoglutarate aminotransferase;
alanine-pyruvate aminotransferase;
ALT;
glutamic acid-pyruvic acid transaminase;
glutamic-pyruvic aminotransferase;
L-alanine aminotransferase;
L-alanine transaminase;
L-alanine-alpha-ketoglutarate aminotransferase;
pyruvate transaminase;
pyruvate-alanine aminotransferase;
pyruvate-glutamate transaminase |
|---|
| Class |
Transferases;
Transferring nitrogenous groups;
Transaminases
 |
|---|
| Sysname |
L-alanine:2-oxoglutarate aminotransferase |
|---|
| Reaction(IUBMB) |
L-alanine + 2-oxoglutarate = pyruvate + L-glutamate [RN:R00258] |
|---|
| Reaction(KEGG) |
R00258
 |
|---|
| Substrate |
L-alanine [CPD:C00041];
2-oxoglutarate [CPD:C00026] |
|---|
| Product |
pyruvate [CPD:C00022];
L-glutamate [CPD:C00025] |
|---|
| Cofactor |
Pyridoxal phosphate [CPD:C00018] |
|---|
| Comment |
A pyridoxal-phosphate protein. 2-Aminobutanoate can act slowly
instead of alanine. |
|---|
| Pathway |
PATH: ec00250 Alanine, aspartate and glutamate metabolism
PATH: ec00710 Carbon fixation in photosynthetic organisms
PATH: ec01064 Biosynthesis of alkaloids derived from ornithine,
lysine and nicotinic acid
PATH: ec01100 Metabolic pathways |
|---|
| Orthology |
KO: K00814 alanine transaminase |
|---|
| Genes |
HSA: 2875(GPT) 84706(GPT2)
MCC: 703122(GPT) 716305
MMU: 108682(Gpt2) 76282(Gpt)
RNO: 307759(Gpt2) 81670(Gpt)
CFA: 609510 609914(GPT)
BTA: 539188(GPT) 618400(GPT2)
ECB: 100056741(GPT2)
MDO: 100012906 100019438
OAA: 100079939
GGA: 415746(GPT2)
TGU: 100225697
XLA: 444533(gpt2)
XTR: 549559(gpt2)
DRE: 100148522 403086(gpt2l) 799963(gpt2)
BFO: BRAFLDRAFT_99414
CIN: 100181336
DME: Dmel_CG1640
DPO: Dpse_GA22670
DAN: Dana_GF19406
DER: Dere_GG17777
DPE: Dper_GL18066
DSE: Dsec_GM11628
DSI: Dsim_GD17120
DYA: Dyak_GE17071
DGR: Dgri_GH24493
DMO: Dmoj_GI15248
AGA: AgaP_AGAP000901
AAG: AaeL_AAEL009872 AaeL_AAEL009875
CQU: CpipJ_CPIJ014256
AME: 409196
NVI: 100116238
TCA: 660331
API: 100164899
ISC: IscW_ISCW013629
CEL: C32F10.8
CBR: CBG04059
SMM: Smp_007760
NVE: NEMVE_v1g236165
HMG: 100200489
TAD: TRIADDRAFT_50189
ATH: AT1G17290(AlaAT1) AT1G23310(GGT1) AT1G70580(AOAT2)
POP: POPTR_1073568 POPTR_565169 POPTR_833470
RCU: RCOM_0024660
VVI: 100241156 100261274(GSVIVT00009478001)
OSA: 4331850(Os03g0183600) 4342210(Os07g0108300)
4347138(Os09g0433900) 4348524(Os10g0390500)
SBI: SORBI_02g039340(SORBIDRAFT_02g039340)
ZMA: 100280822 100282849(uaz158(alt)) 100284842
PPP: PHYPADRAFT_106172 PHYPADRAFT_108003 PHYPADRAFT_113688
PHYPADRAFT_135465 PHYPADRAFT_226033
CRE: CHLREDRAFT_191703(AAT2) CHLREDRAFT_206184(AAT1)
OLU: OSTLU_30612
CME: CMM066C
SCE: YDR111C(ALT2) YLR089C(ALT1)
AGO: AGOS_AGR085W
KLA: KLLA0F19162g
LTH: KLTH0G13662g
DHA: DEHA0B08393g
PIC: PICST_70108(ALA2)
PPA: PAS_chr3_0482
VPO: Kpol_392p5 Kpol_543p39
LEL: LELG_02633
ZRO: ZYRO0C01628g
CAL: CaO19.346 CaO19.7979
CTP: CTRG_02333
CDU: CD36_83480
CGR: CAGL0L12254g
YLI: YALI0D06325g
SPO: SPBC582.08
NCR: NCU03973
PAN: PODANSg3195
MGR: MGG_06503
FGR: FG08443.1
ANI: AN1923.2
AFM: AFUA_6G07770
AOR: AO090003000164
ANG: An11g02620
AFV: AFLA_036440
PCS: Pc12g09430
NFI: NFIA_053440
CIM: CIMG_01266
URE: UREG_01197
SSL: SS1G_02202
BFU: BC1G_04300
CNE: CNG01490
CNB: CNBG3290
LBC: LACBIDRAFT_178543
MPR: MPER_08419
MGL: MGL_3609
MBR: MONBRDRAFT_16434 MONBRDRAFT_31676
DDI: DDB_0232139
EHI: EHI_096750 EHI_159710
EDI: EDI_092730 EDI_325280
TGO: TGME49_064030
TET: TTHERM_00302100
PTM: GSPATT00022590001 GSPATT00033336001 GSPATT00036698001
TBR: Tb927.1.3950
TCR: 506529.420 506529.430 510889.120 510889.140
LMA: LmjF12.0630
LIF: LinJ12.0580
LBZ: LbrM12_V2.0630
GLA: GL50803_12150 GL50803_16363
TVA: TVAG_074600 TVAG_088220 TVAG_098820 TVAG_132440 TVAG_136210
TVAG_379550
PTI: PHATRDRAFT_34010 PHATRDRAFT_bd475
TPS: THAPSDRAFT_412(ALAT_1) THAPS_35402(ALAT_2)
AFW: Anae109_2006
 |
|---|
| Structures |
PDB: 3IHJ |
|---|
Reference
Authors
Title
Journal
Organism
|
1 [PMID:5452003]
Dumitru IF, Iordachescu D, Niculescu S.
Chromatographic purification, crystallization and study of vegetable
L-alanine: 2-oxoglutarate-aminotransferase properties.
Experientia. 26 (1970) 837-8.
Glycine hispida |
|---|
Reference
Authors
Title
Journal
|
2
Dumitru, I.F., Iordachescu, D. and Niculescu, S.
L-Alanine: 2-oxoglutarate-aminotransferase chromatographic
purification and crystallization of the enzyme from seeds of Glycine
hispida var Cheepeura.
Rev. Roum. Biochim. 7 (1970) 31-44. |
|---|
Reference
Authors
Title
Journal
|
3
Green, D.E., Leloir, L.F. and Nocito, W.
Transaminases.
J. Biol. Chem. 161 (1945) 559-582. |
|---|
Reference
Authors
Title
Journal
|
4
Iordachescu, D., Dumitru, I.F. and Corniciuc, M.-T.
Comparative biochemical studies concerning L-alanine:
2-oxoglutarate-aminotransferase from the liver and the bile of
swines.
Rev. Roum. Biochim. 20 (1983) 173-179. |
|---|
Reference
Authors
Title
Journal
Organism
|
5 [PMID:13174595]
WILSON DG, KING KW, BURRIS RH.
Transamination reactions in plants.
J. Biol. Chem. 208 (1954) 863-74.
Lupinus albus, Hordeum vulgare [GN:ehvu] |
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| Other DBs |
ExplorEnz - The Enzyme Database: 2.6.1.2
IUBMB Enzyme Nomenclature: 2.6.1.2
ExPASy - ENZYME nomenclature database: 2.6.1.2
BRENDA, the Enzyme Database: 2.6.1.2
CAS: 9000-86-6 |
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