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Literature summary for 4.8.1.2 extracted from

  • Kobayashi, K.; Pal, B.; Yoshioka, S.; Kato, Y.; Asano, Y.; Kitagawa, T.; Aono, S.
    Spectroscopic and substrate binding properties of heme-containing aldoxime dehydratases, OxdB and OxdRE (2006), J. Inorg. Biochem., 100, 1069-1074.
    View publication on PubMed
Search for more literature for 4.8.1.2

Cloned(Commentary)

Cloned (Comment) Organism
overexpression in Escherichia coli as his tagged fusion protein at the N-terminus Bacillus sp. (in: Bacteria)
overexpression in Escherichia coli as his tagged fusion protein at the N-terminus Rhodococcus sp.

Organism

Organism UniProt Comment Textmining
Bacillus sp. (in: Bacteria)
-
-
-
Bacillus sp. (in: Bacteria) OxB-1
-
-
-
Rhodococcus sp.
-
-
-

Purification (Commentary)

Purification (Comment) Organism
by using a Co2+-loaded metal-ion chelating TALON column Bacillus sp. (in: Bacteria)
by using a Co2+-loaded metal-ion chelating TALON column Rhodococcus sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
an aliphatic aldoxime
-
 Bacillus sp. (in: Bacteria) an aliphatic nitrile + H2O
-
 ?
an aliphatic aldoxime
-
 Rhodococcus sp. an aliphatic nitrile + H2O
-
 ?
an aliphatic aldoxime
-
 Bacillus sp. (in: Bacteria) OxB-1 an aliphatic nitrile + H2O
-
 ?

Synonyms

Synonyms Comment Organism
aliphatic aldoxime dehydratase
-
 Bacillus sp. (in: Bacteria)
aliphatic aldoxime dehydratase
-
 Rhodococcus sp.
OXD
-
 Bacillus sp. (in: Bacteria)
OXD
-
 Rhodococcus sp.
OxdB
-
 Bacillus sp. (in: Bacteria)
OxdRE
-
 Rhodococcus sp.