KEGG   ENZYME: 4.1.3.41Help
Entry
EC 4.1.3.41                 Enzyme                                 

Name
3-hydroxy-D-aspartate aldolase;
D-3-hydroxyaspartate aldolase
Class
Lyases;
Carbon-carbon lyases;
Oxo-acid-lyases
BRITE hierarchy
Sysname
3-hydroxy-D-aspartate glyoxylate-lyase (glycine-forming)
Reaction(IUBMB)
(1) threo-3-hydroxy-D-aspartate = glycine + glyoxylate [RN:R09717];
(2) D-erythro-3-hydroxyaspartate = glycine + glyoxylate [RN:R09718]
Reaction(KEGG)
Substrate
threo-3-hydroxy-D-aspartate [CPD:C19813];
D-erythro-3-hydroxyaspartate [CPD:C19838]
Product
glycine [CPD:C00037];
glyoxylate [CPD:C00048]
Comment
A pyridoxal-phosphate protein. The enzyme, purified from the bacterium Paracoccus denitrificans IFO 13301, is strictly D-specific as to the alpha-position of the substrate, but accepts both the threo and erythro forms at the beta-position. The erythro form is a far better substrate (about 100-fold). The enzyme can also accept D-allothreonine, D-threonine, erythro-3-phenyl-D-serine and threo-3-phenyl-D-serine. Different from EC 4.1.3.14, erythro-3-hydroxy-L-aspartate aldolase. Requires a divalent cation, such as Mg2+, Mn2+ or Co2+.
History
EC 4.1.3.41 created 2011
Orthology
K18425  3-hydroxy-D-aspartate aldolase
Genes
PMAI: CF386_11945
PAR: Psyc_1390(dhaa)
PCR: Pcryo_0979
PSO: PSYCG_05135
PUR: AOC03_11535
PSYC: DABAL43B_1129(dhaA)
SPSW: Sps_01098 Sps_05249
CPS: CPS_4887
COM: CMT41_17630
COLW: A3Q33_19535
GAI: IMCC3135_14580(dhaa)
ODI: ODI_R0236
PACA: ID47_01710
MES: Meso_4367
AMIH: CO731_00754(dhaa)
BOS: BSY19_202
VGO: GJW-30_1_01043(dhaa)
SNO: Snov_2637
MOR: MOC_1918
SIL: SPOA0146
JAN: Jann_2604
RDE: RD1_2890
PDE: Pden_3919
DSH: Dshi_0889
KVL: KVU_0190
PSF: PSE_p0085
OTM: OSB_04160(dhaa)
MALG: MALG_04359
RSU: NHU_00511
RHC: RGUI_2046
SPSE: SULPSESMR1_04893(dhaa)
AHT: ANTHELSMS3_04164(dhaa)
SPHD: HY78_29915
 » show all
Taxonomy
Reference
1  [PMID:12835921]
  Authors
Liu JQ, Dairi T, Itoh N, Kataoka M, Shimizu S
  Title
A novel enzyme, D-3-hydroxyaspartate aldolase from Paracoccus denitrificans IFO 13301: purification, characterization, and gene cloning.
  Journal
Appl Microbiol Biotechnol 62:53-60 (2003)
DOI:10.1007/s00253-003-1238-2
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 4.1.3.41
IUBMB Enzyme Nomenclature: 4.1.3.41
ExPASy - ENZYME nomenclature database: 4.1.3.41
BRENDA, the Enzyme Database: 4.1.3.41

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