KEGG   ENZYME: 4.1.1.12Help
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
BRITE hierarchy
Sysname
L-aspartate 4-carboxy-lyase (L-alanine-forming)
Reaction(IUBMB)
L-aspartate = L-alanine + CO2 [RN:R00397]
Reaction(KEGG)
R00397;
(other) R00863
Show
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
PGE: LG71_16775
EBI: EbC_05500(asdA)
EGE: EM595_p0259(asD)
PAGC: BEE12_19545
VPF: M634_10470
VAG: N646_0788
VOW: A9237_22760
VBR: A6E01_18540
VSH: BSZ05_17320
POR: APT59_06490
ABX: ABK1_1281
ABH: M3Q_2677
ACC: BDGL_001724(asdA)
SPSW: Sps_02671
FTQ: RO31_0955 RO31_0956(asdP)
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)
BOK: DM82_5797(asdP)
BOC: BG90_4832
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
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
ZMO: ZMO1682
ZMN: Za10_1537
ZMM: Zmob_1458
ZMB: ZZ6_1435
ZMI: ZCP4_1480
ASZ: ASN_851
AAD: TC41_0858
LGR: LCGT_1281
LGV: LCGL_1302
LPZ: Lp16_F030
LAC: LBA1695
LAD: LA14_1696
LAF: SD55_1697
LSA: LCA_0306(aspD)
LCA: LSEI_2747
LCB: LCABL_29320(asdA)
LCS: LCBD_2960
LCE: LC2W_2934
LHL: LBHH_1710
EFA: EF1037
EFL: EF62_1474
EFS: EFS1_0865(asdA)
EFQ: DR75_96(aspD)
ENE: ENT_30620
THL: TEH_22060(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
PDC: CDIF630_02764(aspD)
CDC: CD196_2360(aspD)
CDL: CDR20291_2407(aspD)
EAC: EAL2_c09600(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
BVU: BVU_2264
BXY: BXY_02850
BOA: Bovatus_00911(asD)
BCEL: BcellWH2_01068(asD)
BCAC: CGC64_12685(aspD)
PDI: BDI_1073
FJG: BB050_04015(asD)
ABI: Aboo_0621
THA: TAM4_1721
THM: CL1_0496
 » show all
Taxonomy
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)
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)
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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