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Literature summary for 4.8.1.2 extracted from

  • Konishi, K.; Ishida, K.; Oinuma, K.; Ohta, T.; Hashimoto, Y.; Higashibata, H.; Kitagawa, T.; Kobayashi, M.
    Identification of crucial histidines involved in carbon-nitrogen triple bond synthesis by aldoxime dehydratase (2004), J. Biol. Chem., 279, 47619-47625.
    View publication on PubMed
Search for more literature for 4.8.1.2

Protein Variants

Protein Variants Comment Organism
H169A the heme content and CD spectra in the far-UV region are almost identical to that of wild-type enzyme Pseudomonas chlororaphis
H296A the heme content and CD spectra in the far-UV region are almost identical to that of wild-type enzyme Pseudomonas chlororaphis
H299A mutant is unable to bind heme Pseudomonas chlororaphis
H299A the heme content and CD spectra in the far-UV region are almost identical to that of wild-type enzyme Pseudomonas chlororaphis
H320A mutation does not affect the overall structure of OxdA but causes loss of its ability of carbon-nitrogen triple bond synthesis and a lower shift of the Fe-C stretching band in the Raman spectrum for the CO-bound form Pseudomonas chlororaphis
H320A the heme content and CD spectra in the far-UV region are almost identical to that of wild-type enzyme Pseudomonas chlororaphis
H338A the heme content and CD spectra in the far-UV region are almost identical to that of wild-type enzyme Pseudomonas chlororaphis

Organism

Organism UniProt Comment Textmining
Pseudomonas chlororaphis
-
 B23
-
Pseudomonas chlororaphis B23
-
 B23
-

Purification (Commentary)

Purification (Comment) Organism
-
 Pseudomonas chlororaphis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
butyraldoxime
-
 Pseudomonas chlororaphis butyronitrile + H2O
-
 ?
butyraldoxime
-
 Pseudomonas chlororaphis B23 butyronitrile + H2O
-
 ?

Synonyms

Synonyms Comment Organism
OxdA
-
 Pseudomonas chlororaphis

Cofactor

Cofactor Comment Organism Structure
heme
-
 Pseudomonas chlororaphis