Entry
Name
succinylglutamate desuccinylase;
N2-succinylglutamate desuccinylase;
SGDS;
AstE
Class
Hydrolases;
Acting on carbon-nitrogen bonds, other than peptide bonds;
In linear amides
BRITE hierarchy
Sysname
N-succinyl-L-glutamate amidohydrolase
Reaction(IUBMB)
N-succinyl-L-glutamate + H2O = succinate + L-glutamate [RN:
R00411 ]
Reaction(KEGG)
Substrate
Product
Comment
Requires Co2+ for maximal activity [1]. N2-Acetylglutamate is not a substrate. This is the final 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
2.6.1.11 (acetylornithine transaminase), EC
1.2.1.71 (succinylglutamate-semialdehyde dehydrogenase) and EC
3.5.1.96 (succinylglutamate desuccinylase).
History
EC 3.5.1.96 created 2006
Pathway
ec00330 Arginine and proline metabolism
Orthology
K05526 succinylglutamate desuccinylase
Genes
ECOO : ECRM13514_2241(ydjS)
ECOH : ECRM13516_2146(ydjS)
ECW : EcE24377A_1966(astE)
EDJ : ECDH1ME8569_1688(astE)
ECOI : ECOPMV1_01842(astE)
KPN : KPN_01225(astE) KPN_01497
KPU : KP1_2256(astE) KP1_2504
KPM : KPHS_21220 KPHS_23990
KPH : KPNIH24_16225 KPNIH24_18005
KPZ : KPNIH27_10330 KPNIH27_11695
KPV : KPNIH29_10835 KPNIH29_11920
KPW : KPNIH30_11080 KPNIH30_12460
KPY : KPNIH31_10460 KPNIH31_11545
KPG : KPNIH32_10920 KPNIH32_12300
KPC : KPNIH10_10525 KPNIH10_12005
KPQ : KPR0928_10695 KPR0928_12015
KPT : VK055_1012(astE) VK055_1233(astE2)
KPO : KPN2242_09245 KPN2242_10270
KPR : KPR_2272 KPR_2846(astE)
KPI : D364_06350 D364_07340
KPA : KPNJ1_02998 KPNJ1_03285
KPS : KPNJ2_02998 KPNJ2_03276
KPX : PMK1_03604(astE_1) PMK1_03815(astE_2)
KPB : FH42_01990 FH42_03385
KPNE : KU54_014200 KU54_015580
KPNU : LI86_14135 LI86_15890
KPNK : BN49_2360 BN49_2559(astE)
KPE : KPK_2964 KPK_3217(astE)
KPK : A593_20855 A593_22035
KVD : KR75_18700 KR75_19855
KVQ : SP68_00890 SP68_25145
KQU : AVR78_15510 AVR78_16575
KQV : B8P98_15115(astE) B8P98_16215(astE)
KAR : LGL98_13815(astE) LGL98_14870(astE)
KPAS : LUW96_18530(astE) LUW96_28475(astE)
REE : electrica_03006(astE)
ROR : RORB6_07410 RORB6_08540
RON : TE10_12250 TE10_13125
RPLN : B1209_14540 B1209_15885 B1209_27430
RAO : DSD31_14035(astE) DSD31_15120(astE)
RTG : NCTC13098_04211(astE_2)
CLAP : NCTC11466_02668(astE)
KIE : NCTC12125_01662(astE)
BAGE : BADSM9389_24680(astE)
AHN : NCTC12129_02271(astE)
METY : MRY16398_22370(astE)
PSHI : SAMEA2665130_1517(astE)
YPG : YpAngola_A2516(astE)
YPI : YpsIP31758_2117(astE)
SMW : SMWW4_v1c28580(astE)
SFJ : SAMEA4384070_2883(astE)
SOF : NCTC11214_03939(astE)
SERA : Ser39006_004540(astE)
TPTY : NCTC11468_01716(astE)
VFU : vfu_A02107 vfu_B00706
VAU : VANGNB10_cI1524c(astE)
VFL : AL536_06430(astE) AL536_14285
VGA : BSQ33_02210 BSQ33_16445
VSR : Vspart_01987(astE_1) Vspart_03791(astE_2)
VZI : G5S32_06050 G5S32_18275(astE)
VPL : SA104470976_00989(astE)
VRU : RND59_12720 RND59_18965(astE)
PMAI : CF386_07245 CF386_07250
PAEB : NCGM1900_1821(aruE)
PVD : CFBP1590__3551(astE)
PPRC : PFLCHA0_c45810(astE)
PMUD : NCTC8068_03948(astE)
PFW : PF1751_v1c42560(astE)
PPUU : PputUW4_04169(astE)
PTRT : HU722_0022680(astE)
PTW : TUM18999_42530(astE)
PTAE : NCTC10697_03316(astE)
MSHE : MAALD49_32670(astE)
ABAD : ABD1_05450(astE) ABD1_30160(astE)
ASOL : BEN76_09750 BEN76_16535
SCAA : TUM17387_19730(astE)
PRR : AT705_01700 AT705_02425
SALH : HMF8227_01651(astE)
AEL : NCTC12917_02803(astE)
CDIZ : CEDIAZO_01652(astE)
IOD : EJO50_01935(astE) EJO50_07710(astE)
IFL : C1H71_03270(astE) C1H71_19310(astE)
BMV : BMASAVP1_A2420(astE)
BML : BMA10229_A2871(astE)
BPM : BURPS1710b_2841(astE)
BPL : BURPS1106A_2780(astE)
BAC : BamMC406_1066 BamMC406_5816
BSTG : WT74_05945 WT74_20040
BUE : BRPE67_ACDS10020(astE)
PLG : NCTC10937_03866(astE)
BUO : BRPE64_ACDS10890(astE)
JAB : VN23_01665 VN23_05125
MVAR : MasN3_48870(astE_2)
SAQI : AXG55_06635 AXG55_07580
» show all
Taxonomy
Reference
Authors
Vander Wauven C, Stalon V.
Title
Occurrence of succinyl derivatives in the catabolism of arginine in Pseudomonas cepacia.
Journal
Reference
Authors
Cunin R, Glansdorff N, Pierard A, Stalon V.
Title
Biosynthesis and metabolism of arginine in bacteria.
Journal
Microbiol Rev 50:314-52 (1986)
Reference
Authors
Biosynthesis and metabolism of arginine in bacteria.
Title
Microbiol Rev 51:178 (1987)
Reference
Authors
Itoh Y
Title
Cloning and characterization of the aru genes encoding enzymes of the catabolic arginine succinyltransferase pathway in Pseudomonas aeruginosa.
Journal
Sequence
Reference
Authors
Schneider BL, Kiupakis AK, Reitzer LJ
Title
Arginine catabolism and the arginine succinyltransferase pathway in Escherichia coli.
Journal
Sequence
Other DBs
ExplorEnz - The Enzyme Database: 3.5.1.96
ExPASy - ENZYME nomenclature database: 3.5.1.96