KEGG   ENZYME: 4.99.1.5Help
Entry
EC 4.99.1.5                 Enzyme                                 

Name aliphatic aldoxime dehydratase;
OxdA;
aliphatic aldoxime hydro-lyase
Class Lyases;
Other lyases;
Sole sub-subclass for lyases that do not belong in the other
subclasses
BRITE hierarchy
Sysname aliphatic aldoxime hydro-lyase (aliphatic-nitrile-forming)
Reaction(IUBMB) an aliphatic aldoxime = an aliphatic nitrile + H2O [RN:R02827]
Reaction(KEGG) R02827
Show
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 Fe(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.
Pathway ec00460  Cyanoamino acid metabolism
ec01100  Metabolic pathways
ec01110  Biosynthesis of secondary metabolites
Orthology K13028  aldoxime dehydratase
Genes PPF: Pput_2724
PSB: Psyr_0006
PFS: PFLU3206
ACI: ACIAD1620
SWD: Swoo_0211
BCN: Bcen_4080
BCH: Bcen2424_4286
BCM: Bcenmc03_3231
BAM: Bamb_6546
BAC: BamMC406_6260
VAP: Vapar_2540
HSE: Hsero_0929(oxdA)
BBT: BBta_4765
XAU: Xaut_1560
SWI: Swit_0988
RHA: RHA1_ro00358
RER: RER_59190
AAU: AAur_1899(oxdA)
AMI: Amir_0081
Taxonomy
Reference
  Authors

  Title


  Journal
  Organism
  Sequence
1  [PMID:12773527]
Oinuma K, Hashimoto Y, Konishi K, Goda M, Noguchi T, Higashibata H,
Kobayashi M.
Novel aldoxime dehydratase involved in carbon-nitrogen triple bond
synthesis of Pseudomonas chlororaphis B23. Sequencing, gene
expression, purification, and characterization.
J. Biol. Chem. 278 (2003) 29600-8.
Pseudomonas chlororaphis
NCBI-GI: 33456984
Reference
  Authors
  Title

  Journal
  Organism
  Sequence
2  [PMID:14556637]
Xie SX, Kato Y, Komeda H, Yoshida S, Asano Y.
A gene cluster responsible for alkylaldoxime metabolism coexisting
with nitrile hydratase and amidase in Rhodococcus globerulus A-4.
Biochemistry. 42 (2003) 12056-66.
Rhodococcus globerulus
NCBI-GI: 37718700
Reference
  Authors
  Title

  Journal
  Organism
3  [PMID:16233624]
Kato Y, Yoshida S, Xie SX, Asano Y.
Aldoxime dehydratase co-existing with nitrile hydratase and amidase
in the iron-type nitrile hydratase-producer Rhodococcus sp. N-771.
J. Biosci. Bioeng. 97 (2004) 250-9.
Rhodococcus sp.
Other DBs ExplorEnz - The Enzyme Database: 4.99.1.5
IUBMB Enzyme Nomenclature: 4.99.1.5
ExPASy - ENZYME nomenclature database: 4.99.1.5
BRENDA, the Enzyme Database: 4.99.1.5

DBGET integrated database retrieval system