KEGG   ENZYME: 4.1.3.41
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
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)
R09717 R09718
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
Pathway
ec00630  Glyoxylate and dicarboxylate metabolism
ec01100  Metabolic pathways
Orthology
K18425  3-hydroxy-D-aspartate aldolase
Genes
DTLH8F01_09325
DTADYST_03239
MPQABA45_01630
MSQBKP64_01000
PARPsyc_1390(dhaa)
PCRPcryo_0979
PSOPSYCG_05135
PURAOC03_11535
PSYCDABAL43B_1129(dhaA)
SPSWSps_01098
SPSHFM037_15100
SEURFM038_011510
SHEMHWQ47_14040
CPSCPS_4887
COMCMT41_17630
COLWA3Q33_19535
COLADBO93_08415
CBERB5D82_18810
TPSYRGQ13_01585
TNNRI845_17445
TFTRI844_11720
SHAILMH63_09555
GAIIMCC3135_14580(dhaa)
EEINX720_02160
NIYFQ775_00515
NTUNTH_00113(dhaa)
MESMeso_3310 Meso_4367
AAKAA2016_6017 AA2016_6438
AMIHCO731_00754(dhaa)
OSTABWH87_09975(bhcC)
AMAXABWH92_01440(bhcC)
KMNHW532_14250
SMIBN406_06800
RHINGR_b19530
SFDUSDA257_c17700
SAMESAMCFNEI73_pC1568
AGRCGSF67_26235
RELREMIM1_PF00833
REPIE4803_CH03645
NGLRG1141_CH33030
NGGRG540_CH33840
VGOGJW-30_1_01043(dhaa)
SNOSnov_2637
APRAG3A50_08360
AQIJ5J86_05410
MRDMrad2831_1540 Mrad2831_6208
MORMOC_1918
MPHYMCBMB27_01184
METXA3862_23150
METIDK427_04595
MMESMMSR116_01770 MMSR116_17135
MTEADK419_09675
MTADM6G65_08405
MFUJABC766_01375
MENSLOK46_08295 LOK46_30735
CMETK6K41_18880
AALAIGS74_11750
AALMLUX29_12900
JIEOH818_25035
PSFPSE_p0085
LAPACP90_23560
LABRCHH27_20580
LABPFJ695_09280
LABTFIU93_01315(dhaa)
LAGGB0E33_07020
ACUTMRB58_05965
SILSPOA0146
SITTM1040_2701
RUAD1823_21190
RUTFIU92_20550(dhaa)
RCONK3740_13110
RUYNOR97_19270
JANJann_2604
RDERD1_2890
RLIRLO149_c015460
RPONG3256_11505
RFUROLI_016910(dhaa)
DSHDshi_0889
OATOAN307_c10710
OAROA238_c05550
OTMOSB_04160(dhaa)
OCTFTO60_12295
LMDMETH_23270
LEJETW24_21905
LAQUR2C4_20915
LEVETW23_24090
LCAEK3721_21100
MALGMALG_04359
YPACCEW88_20000
YANAYJ57_16085
SULIC1J05_15620
SULDB5M07_04180
SFAVPL335_16920
SPSESULPSESMR1_04893(dhaa)
TOMBWR18_19320
RMMROSMUCSMR3_02249(dhaa) ROSMUCSMR3_04226(dhaa)
ROKRAK1035_0938
RIDRIdsm_04289(dhaa)
ROMEI983_03805
ROHFIU89_00860(dhaa)
RPHCRZ517_05565(bhcC)
RRLRZS32_001845(bhcC)
AHTANTHELSMS3_04164(dhaa)
SAGUCDO87_02405
SSTLABFK29_15645(bhcC)
THAACFI11_05050
OCDFHY55_04770
ROTFIV09_12730(dhaa)
MALUKU6B_33590
PALXGQA70_00110
TRYQF118_19080
RMAIMACH21_06330
REDroselon_00137
ASCAQEZ52_02975
ACLDACIRQ6_06795(bhcC)
SEOHACMUJL_04315(bhcC)
FYTQF092_10350
PDEPden_3919
PAMIJCM7686_1649 JCM7686_1733
PYEA6J80_18880
PZHCX676_03985
PAROCUV01_11725
PARUCYR75_05570
PAMNJCM7685_1474
PMUTDPM13_17980
PARREOJ32_18375
PAAKFIU66_05605
PKDF8A10_04345
PPANESD82_04855
PMAUCP157_03283(dhaa)
PMEHJWJ88_04575
PSAPJHX88_05850
PFISJHX87_04025
PSTLJHW45_12710
PALPJHW40_15335
PVERE3U25_05150
PAEZPAE61_09535
PALSPAF20_08445
PDIMPAF18_05895
PFEOE3U26_20780
RSUNHU_00511
RHMB5V46_15385
RHCRGUI_2046
RMBK529_013205
TSCOR1T40_17875
DAAAKL17_0565
LVSLOKVESSMR4R_00359(dhaa) LOKVESSMR4R_02474(dhaa) LOKVESSMR4R_03892(dhaa)
YAGAABB28_17250(bhcC)
YRHAABB31_06230(bhcC)
GEHHYN69_00875
GFUKM031_14105
TAWEI545_14140
PPSOQPJ95_11155
BOOE2K80_10425
PSEBEOK75_08135
LITFPZ52_03800
POZI0K15_09135
MONG8E03_01825
THASC6Y53_14005
HDHG5B40_18740
GCEKYE46_06295
GYJAADW23_13080(bhcC)
NSMJO391_09170
AALKLGT41_0011725
AMAQGO499_17965
PBAEP8S53_15810
RBGBG454_15055
LVRT8T21_18630
BOSGGKR98_17180
MANHLA6_001770(dhaa)
FAQG5B39_13615
RBXI3V23_01540
SPHDHY78_29915
AALUABWI00_01395
NACINUH88_11800 NUH88_13860
SNEANBZ79_16015
 » show all
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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