| Entry |
|
| Name |
succinylornithine transaminase;
succinylornithine aminotransferase;
N2-succinylornithine 5-aminotransferase;
AstC;
SOAT;
2-N-succinyl-L-ornithine:2-oxoglutarate 5-aminotransferase |
| Class |
Transferases;
Transferring nitrogenous groups;
Transaminases
 |
| Sysname |
N2-succinyl-L-ornithine:2-oxoglutarate 5-aminotransferase |
| Reaction(IUBMB) |
N2-succinyl-L-ornithine + 2-oxoglutarate = N-succinyl-L-glutamate
5-semialdehyde + L-glutamate [RN:R04217] |
| Reaction(KEGG) |
R04217
 |
| Substrate |
N2-succinyl-L-ornithine [CPD:C03415];
2-oxoglutarate [CPD:C00026] |
| Product |
N-succinyl-L-glutamate 5-semialdehyde [CPD:C05932];
L-glutamate [CPD:C00025] |
| Comment |
A pyridoxal-phosphate protein. Also acts on N2-acetyl-L-ornithine
and L-ornithine, but more slowly [3]. In Pseudomonas aeruginosa, the
arginine-inducible succinylornithine transaminase, acetylornithine
transaminase (EC 2.6.1.11) and ornithine aminotransferase (EC
2.6.1.13) activities are catalysed by the same enzyme, but this is
not the case in all species [5]. This is the third enzyme in the
arginine succinyltransferase (AST) pathway for the catabolism of
arginine [1]. This pathway converts the carbon skeleton of arginine
into glutamate, with the concomitant production of ammonia and
conversion of succinyl-CoA into succinate and CoA. The five enzymes
involved in this pathway are EC 2.3.1.109 (arginine
N-succinyltransferase), EC 3.5.3.23 (N-succinylarginine
dihydrolase), EC 2.6.1.81 (succinylornithine transaminase), EC
1.2.1.71 (succinylglutamate-semialdehyde dehydrogenase) and EC
3.5.1.96 (succinylglutamate desuccinylase) [3, 6]. |
| Pathway |
PATH: ec00330 Arginine and proline metabolism |
| Orthology |
KO: K00840 succinylornithine aminotransferase |
| Genes |
ECO: b1748(astC)
ECJ: JW1737(astC)
ECD: ECDH10B_1886(astC)
EBW: BWG_1561(astC)
ECE: Z2780(argD)
ECS: ECs2454(argD)
ECF: ECH74115_2466(astC)
ETW: ECSP_2316(astC)
ECG: E2348C_1876(astC)
ECC: c2148(argD)
ECI: UTI89_C1943(astC)
ECP: ECP_1694
ECV: APECO1_817(cstC)
ECW: EcE24377A_1970(astC)
ECX: EcHS_A1831(astC)
ECM: EcSMS35_1443(astC)
ECY: ECSE_1918
ECL: EcolC_1884
ECK: EC55989_1916(astC)
ECQ: ECED1_1950(astC)
ECR: ECIAI1_1809(astC)
ECT: ECIAI39_1306(astC)
ECZ: ECS88_1800(astC)
EUM: ECUMN_2037(astC)
ELF: LF82_0182(astC)
EBL: B21_01705(astC)
EBD: ECBD_1897
EBR: ECB_01717(astC)
EOH: ECO103_1941(astC)
EOI: ECO111_2259(astC)
EOJ: ECO26_2523(astC)
EFE: EFER_1317(astC)
STY: STY1811(argD)
STT: t1182(argD)
SPT: SPA1541(argD)
SEK: SSPA1432
SPQ: SPAB_02040
SEI: SPC_2428(argD)
SEC: SC1326(argD)
SEH: SeHA_C1430(astC)
SEE: SNSL254_A1415
SEW: SeSA_A1398
SEA: SeAg_B1871(astC)
SED: SeD_A2043
SEG: SG1813(astC)
SET: SEN1740(astC)
SES: SARI_01676
STM: STM1303(argD)
YPE: YPO1962(argD)
YPK: y2349(argD)
YPM: YP_1707(argD)
YPA: YPA_1344
YPG: YpAngola_A2520(argM)
YPP: YPDSF_1161
YPS: YPTB1959(argD)
YPI: YpsIP31758_2121(argM)
YPY: YPK_2229
YPB: YPTS_2011
YEN: YE2469(argM)
SSN: SSON_1409(cstC)
SBO: SBO_1342(cstC)
SBC: SbBS512_E1995(astC)
ETA: ETA_18590(argM)
PLU: plu3110(argD)
PAY: PAU_01497(argM)
ENT: Ent638_1696
ESA: ESA_02157
CTU: Ctu_18160(astC)
KPN: KPN_01493
KPE: KPK_2968 KPK_3222(astC)
KPU: KP1_2251(argD) KP1_2498
CKO: CKO_01774
SPE: Spro_2844
DDA: Dd703_0484
ACI: ACIAD1284(argD)
ACB: A1S_3132
ABM: ABSDF0355(astC)
ABY: ABAYE0352(astC)
ABC: ACICU_01135 ACICU_03334
ABN: AB57_1173 AB57_3587
ABB: ABBFA_000377 ABBFA_002455
 |
Reference Authors Title
Journal Organism
|
1 [PMID:2865249]
Vander Wauven C, Stalon V.
Occurrence of succinyl derivatives in the catabolism of arginine in
Pseudomonas cepacia.
J. Bacteriol. 164 (1985) 882-6.
Pseudomonas cepacia |
Reference Authors Title
Journal Organism
|
2 [PMID:9696779]
Schneider BL, Kiupakis AK, Reitzer LJ.
Arginine catabolism and the arginine succinyltransferase pathway in
Escherichia coli.
J. Bacteriol. 180 (1998) 4278-86.
Escherichia coli [GN:eco] |
Reference Authors Title Journal Organism
|
3 [PMID:3534538]
Cunin R, Glansdorff N, Pierard A, Stalon V.
Biosynthesis and metabolism of arginine in bacteria.
Microbiol. Rev. 50 (1986) 314-52.
Pseudomonas spp. |
Reference Authors Title
Journal Organism
|
4 [PMID:9393691]
Itoh Y.
Cloning and characterization of the aru genes encoding enzymes of
the catabolic arginine succinyltransferase pathway in Pseudomonas
aeruginosa.
J. Bacteriol. 179 (1997) 7280-90.
Pseudomonas aeruginosa [GN:pae] |
Reference Authors Title
Journal Organism
|
5 [PMID:3129535]
Stalon V, Vander Wauven C, Momin P, Legrain C.
Catabolism of arginine, citrulline and ornithine by Pseudomonas and
related bacteria.
J. Gen. Microbiol. 133 (1987) 2487-95.
Pseudomonas cepacia, Pseudomonas putida, Pseudomonas indigofera |
| Other DBs |
ExplorEnz - The Enzyme Database: 2.6.1.81
IUBMB Enzyme Nomenclature: 2.6.1.81
ExPASy - ENZYME nomenclature database: 2.6.1.81
BRENDA, the Enzyme Database: 2.6.1.81 |