KEGG   ENZYME: 4.1.1.12
Entry
EC 4.1.1.12                 Enzyme                                 

Name
aspartate 4-decarboxylase;
desulfinase;
aminomalonic decarboxylase;
aspartate beta-decarboxylase;
aspartate omega-decarboxylase;
aspartic omega-decarboxylase;
aspartic beta-decarboxylase;
L-aspartate beta-decarboxylase;
cysteine sulfinic desulfinase;
L-cysteine sulfinate acid desulfinase;
L-aspartate 4-carboxy-lyase
Class
Lyases;
Carbon-carbon lyases;
Carboxy-lyases
Sysname
L-aspartate 4-carboxy-lyase (L-alanine-forming)
Reaction(IUBMB)
L-aspartate = L-alanine + CO2 [RN:R00397]
Reaction(KEGG)
R00397;
(other) R00863
Substrate
L-aspartate [CPD:C00049]
Product
L-alanine [CPD:C00041];
CO2 [CPD:C00011]
Comment
A pyridoxal-phosphate protein. Also catalyses the decarboxylation of aminomalonate (formerly listed as EC 4.1.1.10), and the desulfination of 3-sulfino-L-alanine to sulfite and alanine.
History
EC 4.1.1.12 created 1961, modified 1976 (EC 4.1.1.10 created 1961, incorporated 1972)
Pathway
ec00250  Alanine, aspartate and glutamate metabolism
ec00270  Cysteine and methionine metabolism
ec01100  Metabolic pathways
Orthology
K09758  aspartate 4-decarboxylase
Genes
DSR: 110182044
PGE: LG71_16775
SGOE: A8O29_009805
EBI: EbC_05500(asdA)
EGE: EM595_p0259(asD)
PAGC: BEE12_19545
XCZ: EBN15_14105
VPF: M634_10470
VAG: N646_0788
VOW: A9237_22760
ABX: ABK1_1281
ABH: M3Q_2677
ACC: BDGL_001724(asdA)
AGU: AS4_34620
AUG: URS_3215
SPSW: Sps_02671
FTQ: RO31_0955
FTW: FTW_1358
FTL: FTL_0320
FTH: FTH_0320(aspD)
FTA: FTA_0339
FTS: F92_01720
FTI: FTS_0320(aspD)
FTC: DA46_389(aspD)
FTV: CH67_605(aspD)
FTZ: CH68_339(aspD)
FTM: FTM_0420
FTN: FTN_0343
FTX: AW25_1696(aspD)
FTD: AS84_347(aspD)
FTY: CH70_1724(aspD)
FPH: Fphi_0481
FPT: BZ13_1555(aspD)
FPI: BF30_676(aspD)
FPM: LA56_1696(aspD)
FPX: KU46_878(aspD)
FPZ: LA55_350(aspD)
FPJ: LA02_93(aspD)
RIN: ACS15_4642(aspD)
REH: H16_A3009(asdA)
RME: Rmet_1984(asdA)
BDL: AK34_5158(aspD)
BGU: KS03_1969(aspD)
BGO: BM43_966(aspD)
BXE: Bxe_A3891
BXB: DR64_1567(aspD)
BFN: OI25_910(aspD)
PPNO: DA70_08515
PPNM: LV28_22125
PPUL: RO07_16525
PSPU: NA29_20650
PAPI: SG18_15360
CABA: SBC2_59080(asD)
AXY: AXYL_01733(asdA)
DAC: Daci_3914
CTES: O987_14975
MMS: mma_1084(asdA)
CFU: CFU_0143(asdA)
CARE: LT85_0123
CPRA: CPter91_0121(aspD)
SUN: SUN_0877
DAS: Daes_0274
PLA: Plav_0095
SMER: DU99_31685
RHL: LPU83_pLPU83c0641(asdA)
OAN: Oant_3483
OAH: DR92_3003(aspD)
BJA: blr3477
BRS: S23_35870
MET: M446_1557
RUT: FIU92_18350(asD)
ZMO: ZMO1682
ZMN: Za10_1537
ZMM: Zmob_1458
ZMB: ZZ6_1435
ZMI: ZCP4_1480
KSC: CD178_01686(asD)
ASZ: ASN_851
PRD: F7984_03280(aspD)
AAD: TC41_0858
LGR: LCGT_1281
LGV: LCGL_1302
LAC: LBA1695
LAD: LA14_1696
LAF: SD55_1697
LSA: LCA_0306(aspD)
LHL: LBHH_1710
LCA: LSEI_2747
LCS: LCBD_2960
LCE: LC2W_2934
LCB: LCABL_29320(asdA)
LPZ: Lp16_F030
EFA: EF1037
EFL: EF62_1474
EFS: EFS1_0865(asdA)
EFQ: DR75_96(aspD)
ENE: ENT_30620
THL: TEH_22060(aspD)
DPM: FNV33_08145(aspD)
CPF: CPF_0325 CPF_1258(aspD)
CPR: CPR_0327
CBO: CBO1166(asdA)
CBA: CLB_1197(asdA)
CBH: CLC_1209(asdA)
CBY: CLM_1317
CBL: CLK_0601
CBB: CLD_3403
CBI: CLJ_B1207(aspD)
CBF: CLI_1247(aspD)
CBE: Cbei_1924
CBZ: Cbs_1924
CBEI: LF65_02091
CKL: CKL_0699
CKR: CKR_0621
CBV: U729_1867(aspD)
CSQ: CSCA_1714
CLD: CLSPO_c11660(asd1)
CTYK: CTK_C07120
CSEP: CP523_01580(aspD)
CDY: F3K33_09545(aspD)
CEW: EKH84_13810(aspD)
PDC: CDIF630_02764(aspD)
CDC: CD196_2360(aspD)
CDL: CDR20291_2407(aspD)
EAC: EAL2_c09600(aspD)
ROC: HF520_07485(aspD)
PHX: KGNDJEFE_01911(asD)
AMIC: Ami3637_00175(aspD)
ABUT: Ami103574_04740(aspD)
MANA: MAMMFC1_00109(asD)
TSG: HLK68_09170(aspD) HLK68_11245(aspD)
SALB: XNR_4167
SGR: SGR_4732
SGB: WQO_11875
SVE: SVEN_2588
SFI: SFUL_2397
SFK: KY5_2946
KSK: KSE_63100
SESP: BN6_36290
CAI: Caci_1946
SNA: Snas_3840
AEQ: AEQU_1726
LBA: Lebu_0659
BTH: BT_0735
BTHO: Btheta7330_02355(asD)
BFR: BF1517
BXY: BXY_02850
BOA: Bovatus_00911(asD)
BCEL: BcellWH2_01068(asD)
BCAC: CGC64_12685(aspD)
BIS: DXK01_019955(aspD)
BVU: BVU_2264
PDI: BDI_1073
PGO: FSB84_29235(aspD)
FJG: BB050_04015(asD)
APIB: G8C43_08895(aspD)
ABI: Aboo_0621
THA: TAM4_1721
THM: CL1_0496
 » show all
Reference
1  [PMID:5773301]
  Authors
Kakimoto T, Kato J, Shibatani T, Nishimura N, Chibata I.
  Title
Crystalline L-aspartate beta-decarboxylase of Pseudomonas dacunhae. I. Crystallization and some physiocochemical properties.
  Journal
J Biol Chem 244:353-8 (1969)
Reference
2  [PMID:14154469]
  Authors
NOVOGRODSKY A, MEISTER A.
  Title
CONTROL OF ASPARTATE BETA-DECARBOXYLASE ACTIVITY BY TRANSAMINATION.
  Journal
J Biol Chem 239:879-88 (1964)
Reference
3  [PMID:5424207]
  Authors
Palekar AG, Tate SS, Meister A.
  Title
Inhibition of aspartate beta-decarboxylase by aminomalonate. Stereospecific decarboxylation of aminomalonate to glycine.
  Journal
Biochemistry 9:2310-5 (1970)
DOI:10.1021/bi00813a014
Reference
4  [PMID:14071532]
  Authors
WILSON EM, KORNBERG HL.
  Title
PROPERTIES OF CRYSTALLINE L-ASPARTATE 4-CARBOXY-LYASE FROM ACHROMOBACTER SP.
  Journal
Biochem J 88:578-87 (1963)
DOI:10.1042/bj0880578
Other DBs
ExplorEnz - The Enzyme Database: 4.1.1.12
IUBMB Enzyme Nomenclature: 4.1.1.12
ExPASy - ENZYME nomenclature database: 4.1.1.12
BRENDA, the Enzyme Database: 4.1.1.12
CAS: 9024-57-1

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