| Entry |
|
|---|
| 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] |
|---|
| Cofactor |
Pyridoxal phosphate [CPD:C00018] |
|---|
| 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. |
|---|
| Pathway |
PATH: ec00250 Alanine, aspartate and glutamate metabolism
PATH: ec00270 Cysteine and methionine metabolism
PATH: ec01100 Metabolic pathways |
|---|
| Orthology |
KO: K09758 aspartate 4-decarboxylase |
|---|
| Genes |
ABC: ACICU_02407
FTW: FTW_1358
FTL: FTL_0320
FTH: FTH_0320(aspD)
FTA: FTA_0339
FTM: FTM_0420
FTN: FTN_0343
FPH: Fphi_0481
REU: Reut_A2709
REH: H16_A3009(asdA)
RME: Rmet_1984
CTI: RALTA_A2486
BXE: Bxe_A3891
BPY: Bphyt_0790
BGL: bglu_1g10380
DAC: Daci_3914
CTT: CtCNB1_2315
MMS: mma_1084(asdA)
SUN: SUN_0877
PLA: Plav_0095
OAN: Oant_3483
BJA: blr3477
MET: M446_1557
ZMO: ZMO1682
ZMN: Za10_1537
APT: APA01_04430 APA01_15490
LAC: LBA1695
LSA: LSA0306(aspD)
LCA: LSEI_2747
LCB: LCABL_29320(asdA)
EFA: EF1037
CPE: CPE0341 CPE1001
CPF: CPF_0325 CPF_1258(aspD)
CPR: CPR_0327
CDF: CD2515(aspD)
CDC: CD196_2360(aspD)
CDL: CDR20291_2407(aspD)
CBO: CBO1166(asdA)
CBA: CLB_1197(asdA)
CBH: CLC_1209(asdA)
CBY: CLM_1317
CBL: CLK_0601(asdA)
CBB: CLD_3403(asdA)
CBI: CLJ_B1207
CBF: CLI_1247(asdA)
CBE: Cbei_1924
CKL: CKL_0699
CKR: CKR_0621
SGR: SGR_4732
CAI: Caci_1946
BTH: BT_0735
BFR: BF1517
BFS: BF1452
BVU: BVU_2264
PDI: BDI_1073
LBA: Lebu_0659
 |
|---|
| Structures |
PDB: 2ZY2 2ZY3 2ZY4 2ZY5 3FDD |
|---|
Reference
Authors
Title
Journal
Organism
|
1 [PMID:5773301]
Kakimoto T, Kato J, Shibatani T, Nishimura N, Chibata I.
Crystalline L-aspartate beta-decarboxylase of Pseudomonas dacunhae.
I. Crystallization and some physiocochemical properties.
J. Biol. Chem. 244 (1969) 353-8.
Pseudomonas dacunhae |
|---|
Reference
Authors
Title
Journal
Organism
|
2 [PMID:14154469]
NOVOGRODSKY A, MEISTER A.
CONTROL OF ASPARTATE BETA-DECARBOXYLASE ACTIVITY BY TRANSAMINATION.
J. Biol. Chem. 239 (1964) 879-88.
Pseudomonas dacunhae |
|---|
Reference
Authors
Title
Journal
Organism
|
3 [PMID:5424207]
Palekar AG, Tate SS, Meister A.
Inhibition of aspartate beta-decarboxylase by aminomalonate.
Stereospecific decarboxylation of aminomalonate to glycine.
Biochemistry. 9 (1970) 2310-5.
Alcaligenes faecalis |
|---|
Reference
Authors
Title
Journal
Organism
|
4 [PMID:14071532]
WILSON EM, KORNBERG HL.
PROPERTIES OF CRYSTALLINE L-ASPARTATE 4-CARBOXY-LYASE FROM
ACHROMOBACTER SP.
Biochem. J. 88 (1963) 578-87.
Achromobacter sp. |
|---|
| 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 |
|---|
