KEGG   ENZYME: 4.8.1.2
Entry
EC 4.8.1.2                  Enzyme                                 
Name
aliphatic aldoxime dehydratase;
OxdA;
aliphatic aldoxime hydro-lyase
Class
Lyases;
Nitrogen-oxygen lyases;
Hydro-lyases
Sysname
aliphatic aldoxime hydro-lyase (aliphatic-nitrile-forming)
Reaction(IUBMB)
an aliphatic aldoxime = an aliphatic nitrile + H2O [RN:R02827]
Reaction(KEGG)
R02827
Substrate
aliphatic aldoxime [CPD:C02658]
Product
aliphatic nitrile [CPD:C16072];
H2O [CPD:C00001]
Comment
The enzyme from Pseudomonas chlororaphis contains Ca2+ and protoheme IX, the iron of which must be in the form iron(II) for activity. The enzyme exhibits a strong preference for aliphatic aldoximes, such as butyraldoxime and acetaldoxime, over aromatic aldoximes, such as pyridine-2-aldoxime, which is a poor substrate. No activity was found with the aromatic aldoximes benzaldoxime and pyridine-4-aldoxime.
History
EC 4.8.1.2 created 2004 as EC 4.99.1.5, transferred 2021 to EC 4.8.1.2
Orthology
K13028  aliphatic aldoxime dehydratase
Genes
KPASLUW96_26075
KRDA3780_03605
SRYM621_16765
ROXBV494_24265
GQUAWC35_07535
PACBM9782_00380 M9782_01890
BRBEH207_13150
LPOPI6N93_12970
EBIEbC_pEb17201260
PVAPvag_pPag20172(oxd)
PAOPat9b_4157
PPHOCTZ24_25680
GKDK6Q96_19040
PPFPput_2724
PPBPPUBIRD1_2719
PPIYSA_10164
PSBPsyr_0006
PAVLBKM03_00075
PSYIMME58_26435
PFSPFLU_3206
POIBOP93_15040
PFWPF1751_v1c35540
PFFPFLUOLIPICF718125
PFXA7318_17655
PPUUPputUW4_03348
PSKU771_17940
PSWLK03_13745
PPVNJ69_09910
PFKPFAS1_24125
PPSLBJP27_22315
PSETTHL1_3212
PVKEPZ47_15365
PEZHWQ56_17275
PBZGN234_03640
PSEPC4K39_4246
PPIIQL104_27475
PXAKSS93_13700
PSAMHU731_001400
PASGKSS96_12085
PTAIICN73_20670
PHYGJTY93_12630
PPAELDL65_27515
PSKUKUIN1_00060
ACIACIAD1620(oxd)
SWDSwoo_0211
MICTFIU95_19905(oxd)
MICZGL2_16030
MVBMJO52_20075
KIMG3T16_03195
GAIIMCC3135_05130(oxd)
HAAA5892_00345
RPJN234_09734
BCMBcenmc03_3231
BCHBcen2424_4286
BAMBamb_6546
BACBamMC406_6260
BCEPAPZ15_17540
BCONNL30_05545
BSEMWJ12_26915
BMECWJ16_18455
BGDbgla_2g08590
BUMAXG89_29840
BURKDM992_39525
PTERC2L65_36345
BHZACR54_04419(oxd)
BPDZBBN53_00995
BGVCAL12_21035
PIGEGT29_10530
AAAAcav_2428
VAPVapar_0670 Vapar_2540
VPEVarpa_3386
VPDVAPA_1c30120
VBOCKY39_15760
VAMC4F17_06950
HYRBSY239_4027
HSEHsero_0929(oxdA)
HSZACP92_04650
HRBHrubri_2880(oxdA) Hrubri_3579(oxdA)
AMISAmn_pd00460
SFHSFHH103_06512(oxd)
OCHCES85_3266
BJUBJ6T_45640
BJPRN69_22155
BBTBBta_4765
BRSS23_30650
BRCBCCGELA001_21810
BRADBF49_6425
BICLMTR13_22140
BRKCWS35_21575
BOTCIT37_28410
BRQCIT40_18020
BGQX265_22005
BGZXH91_15375
BSYMCIT39_17370
BELBE61_49650
BDGLPJ38_27700
BSEPHAP48_0042040
BQBJ4P68_0002280
BBANJ4G43_031100
BCANBcanWSM471_22975
BAUTQA635_19805
BBRAQA636_20180
BGKIC762_21090
BCOUIC761_15570
BPAHQA639_25190
BXNI3J27_22260
BRAZLRP30_23255
TALZRPMA_26245
XAUXaut_1560
MLGCWB41_11900
BBARRHAL1_03168
HMCHYPMC_0479(Adase)
METGHT051_03750
PSINCAK95_03820 CAK95_28650
PPRUFDP22_16910
SWISwit_0988
SPHDHY78_21570
SPHRBSY17_2187(oxd)
SPYGYGS_C1P2765
GOHB932_2217
NTND5366_08300
SNEANBZ79_14860 NBZ79_17720
MTYMTOK_06480
RHARHA1_ro00358
RERRER_59190
REYO5Y_28495
REBXU06_28825
RQIC1M55_30310
ROAPd630_LPD04519
RHODAOT96_09960
RKOJWS14_00645 JWS14_16535
RGOKYT97_19110
ROZCBI38_29980
RPSKJWS13_28105
SALBXNR_1370
SKYD0C37_08395
SLKSLUN_04645
SVIOHWN34_07530
AARCG127AT_03890
ARRARUE_c20310(oxd)
AAUAAur_1899(oxdA)
NAROCFH99_05010
PSIMKR76_24340
ARHDVSH64_05650
PDXPsed_2832
PSEEFRP1_16645
PSEHXF36_16225
PSEQAD006_30930
PECQAD017_30305
PBROHOP40_02675
APRECNX65_00410
AMIAmir_0081
KUTJJ691_09670(oxd)
ACTYOG774_07450
UMERM788_11175
EKEEK0264_14185
 » show all
Reference
1  [PMID:12773527]
  Authors
Oinuma K, Hashimoto Y, Konishi K, Goda M, Noguchi T, Higashibata H, Kobayashi M
  Title
Novel aldoxime dehydratase involved in carbon-nitrogen triple bond synthesis of Pseudomonas chlororaphis B23. Sequencing, gene expression, purification, and characterization.
  Journal
J Biol Chem 278:29600-8 (2003)
DOI:10.1074/jbc.M211832200
  Sequence
Reference
2  [PMID:14556637]
  Authors
Xie SX, Kato Y, Komeda H, Yoshida S, Asano Y
  Title
A gene cluster responsible for alkylaldoxime metabolism coexisting with nitrile hydratase and amidase in Rhodococcus globerulus A-4.
  Journal
Biochemistry 42:12056-66 (2003)
DOI:10.1021/bi035092u
  Sequence
Reference
3  [PMID:16233624]
  Authors
Kato Y, Yoshida S, Xie SX, Asano Y.
  Title
Aldoxime dehydratase co-existing with nitrile hydratase and amidase in the iron-type nitrile hydratase-producer Rhodococcus sp. N-771.
  Journal
J Biosci Bioeng 97:250-9 (2004)
DOI:10.1016/S1389-1723(04)70200-5
  Sequence
[rer:RER_59190]
Other DBs
ExplorEnz - The Enzyme Database: 4.8.1.2
IUBMB Enzyme Nomenclature: 4.8.1.2
ExPASy - ENZYME nomenclature database: 4.8.1.2
BRENDA, the Enzyme Database: 4.8.1.2

DBGET integrated database retrieval system