Entry
Name
N-succinylarginine dihydrolase;
N2-succinylarginine dihydrolase;
arginine succinylhydrolase;
SADH;
AruB;
AstB;
2-N-succinyl-L-arginine iminohydrolase (decarboxylating)
Class
Hydrolases;
Acting on carbon-nitrogen bonds, other than peptide bonds;
In linear amidines
BRITE hierarchy
Sysname
N2-succinyl-L-arginine iminohydrolase (decarboxylating)
Reaction(IUBMB)
N2-succinyl-L-arginine + 2 H2O = N2-succinyl-L-ornithine + 2 NH3 + CO2 [RN:
R04189 ]
Reaction(KEGG)
Substrate
Product
Comment
Arginine, N2-acetylarginine and N2-glutamylarginine do not act as substrates [3]. This is the second 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).
History
EC 3.5.3.23 created 2006
Pathway
ec00330 Arginine and proline metabolism
Orthology
K01484 succinylarginine dihydrolase
Genes
ECW : EcE24377A_1967(astB)
EDJ : ECDH1ME8569_1689(astB)
ECOI : ECOPMV1_01843(astB)
KPN : KPN_01224(astB) KPN_01496
KPU : KP1_2254(astB) KP1_2502
KPM : KPHS_21210 KPHS_23980
KPH : KPNIH24_16230 KPNIH24_18010
KPZ : KPNIH27_10325 KPNIH27_11690
KPV : KPNIH29_10830 KPNIH29_11915
KPW : KPNIH30_11075 KPNIH30_12455
KPY : KPNIH31_10455 KPNIH31_11540
KPG : KPNIH32_10915 KPNIH32_12295
KPC : KPNIH10_10520 KPNIH10_12000
KPQ : KPR0928_10690 KPR0928_12010
KPT : VK055_1013(astB) VK055_1234(astB2)
KPO : KPN2242_09240 KPN2242_10265
KPR : KPR_2271(astB) KPR_2847(astB)
KPI : D364_06345 D364_07335
KPA : KPNJ1_02999 KPNJ1_03286
KPS : KPNJ2_02999 KPNJ2_03277
KPX : PMK1_03603(astB_1) PMK1_03814(astB_2)
KPB : FH42_01985 FH42_03380
KPNE : KU54_014205 KU54_015585
KPNU : LI86_14140 LI86_15895
KPNK : BN49_2359(astB) BN49_2558(astB2)
KPE : KPK_2965 KPK_3219(astB)
KPK : A593_20850 A593_22030
KVD : KR75_18695 KR75_19850
KVQ : SP68_00885 SP68_25140
KQU : AVR78_15505 AVR78_16570
KQV : B8P98_15120(astB) B8P98_16220(astB)
KAR : LGL98_13820(astB) LGL98_14875(astB)
REE : electrica_03007(astB)
ROR : RORB6_07415 RORB6_08545
RON : TE10_12245 TE10_13120
RPLN : B1209_14545 B1209_15890 B1209_27425
RAO : DSD31_14040(astB) DSD31_15125(astB)
RTG : NCTC13098_04212(astB_4)
CLAP : NCTC11466_02669(astB)
KIE : NCTC12125_01663(astB)
AHN : NCTC12129_02270(astB)
METY : MRY16398_22360(astB)
PSHI : SAMEA2665130_1893(astB)
EBU : CUC76_03535(astB) CUC76_04575(astB)
YPG : YpAngola_A2517(astB)
YPI : YpsIP31758_2118(astB)
SMW : SMWW4_v1c28590(astB)
SMAF : D781_1034 D781_2660
SRZ : AXX16_2392 AXX16_4066
SERM : CLM71_05045(astB) CLM71_13750(astB)
SFJ : SAMEA4384070_2884(astB)
SOF : NCTC11214_03938(astB_2)
SRHZ : FO014_04735(astB) FO014_19910(astB)
SSAR : SSARUM_002773(astB)
SERA : Ser39006_004535(astB)
KPIE : N5580_10000(astB) N5580_21295(astB)
TPTY : NCTC11468_01715(astB)
PAEB : NCGM1900_1823(aruB)
PVD : CFBP1590__3553(astB)
PPRC : PFLCHA0_c45830(astB)
PMUD : NCTC8068_03950(astB)
PFW : PF1751_v1c42580(astB)
PPUU : PputUW4_04171(astB)
PTRT : HU722_0022690(astB)
PTW : TUM18999_42550(astB)
PTAE : NCTC10697_03318(astB)
MSHE : MAALD49_32710(astB)
ASOL : BEN76_09755 BEN76_16540
SCAA : TUM17387_15300(astB)
PPIS : B1L02_09290(astB) B1L02_18245(astB)
SALH : HMF8227_01295(astB)
LLG : 44548918_01288(astB)
LJR : NCTC11533_01647(astB)
LCJ : NCTC11976_02336(astB)
LWA : SAMEA4504053_1638(astB)
LSS : NCTC12082_00833(astB)
LADL : NCTC12735_01939(astB)
LANT : TUM19329_17880(astB)
HAAH : HALA3H3_700053(astB)
AEL : NCTC12917_01209(astB)
CDIZ : CEDIAZO_02152(astB)
BMV : BMASAVP1_A2421(astB)
BML : BMA10229_A2870(astB)
BPM : BURPS1710b_2842(astB)
BPL : BURPS1106A_2781(astB)
BUE : BRPE67_ACDS10010(astB)
PLG : NCTC10937_03868(astB)
BUO : BRPE64_ACDS10880(astB)
CCS : CCNA_00619 CCNA_01680
BVY : NCTC9239_01101(astB)
TSV : DSM104635_02380(astB)
SBIN : SBA_ch1_25360(astB1)
SPAG : sphantq_00114(astB)
SFLA : SPHFLASMR4Y_01347(astB)
SLAA : EUU25_05855 EUU25_08725
POT : E2E27_04565 E2E27_08640
» show all
Taxonomy
Reference
Authors
Schneider BL, Kiupakis AK, Reitzer LJ
Title
Arginine catabolism and the arginine succinyltransferase pathway in Escherichia coli.
Journal
Sequence
Reference
Authors
Tocilj A, Schrag JD, Li Y, Schneider BL, Reitzer L, Matte A, Cygler M.
Title
Crystal structure of N-succinylarginine dihydrolase AstB, bound to substrate and product, an enzyme from the arginine catabolic pathway of Escherichia coli.
Journal
Sequence
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
Itoh Y
Title
Cloning and characterization of the aru genes encoding enzymes of the catabolic arginine succinyltransferase pathway in Pseudomonas aeruginosa.
Journal
Sequence
Other DBs
ExplorEnz - The Enzyme Database: 3.5.3.23
ExPASy - ENZYME nomenclature database: 3.5.3.23
LinkDB
All DBs