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Literature summary for 1.14.14.1 extracted from

  • Chen, C.K.; Berry, R.E.; Shokhireva, T.K.; Murataliev, M.B.; Zhang, H.; Walker, F.A.
    Scanning chimeragenesis: the approach used to change the substrate selectivity of fatty acid monooxygenase CYP102A1 to that of terpene omega-hydroxylase CYP4C7 (2010), J. Biol. Inorg. Chem., 15, 159-174.
    View publication on PubMed
Search for more literature for 1.14.14.1

Application

Application Comment Organism
biotechnology scanning chimeragenesis can be a useful method for producing new enzymatic products from CYP102A1 and may be used as a new systematic tool for changing substrate selectivity and regiospecificity among any two cytochromes P450 that have a common substrate, to study the interaction between enzymes and the substrate or to create new chimeric proteins for pharmaceutical and industrial uses Priestia megaterium

Cloned(Commentary)

Cloned (Comment) Organism
homologous peptide fragments of terpene omega-hydroxylase CYP4C7 from Diploptera punctata inserted into CYP102A1 Priestia megaterium

Organism

Organism UniProt Comment Textmining
Priestia megaterium P14779
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-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3,7-dimethyl-1-octanol + [reduced NADPH-hemoprotein reductase] + O2
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 Priestia megaterium 6-hydroxy-3,7-dimethyl-1-octanol + [oxidized NADPH-hemoprotein reductase] + H2O
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 ?
farnesol + [reduced NADPH-hemoprotein reductase] + O2 CYP102A1 oxidizes farnesol to three products (2,3-epoxyfarnesol, 10,11-epoxyfarnesol, and 9-hydroxyfarnesol), whereas CYP4C7 produces 12-hydroxyfarnesol as the major product. Chimeric proteins C(78-82,F87L) and C(78-82,F87L,328-330) show the most complete change in substrate selectivity from fatty acids to farnesol, and both retain superior enzyme activity with respect to CYP102A1 approximately 5times and approximately 2times greater, respectively. C(78-82,F87L,328-330) produces 12-hydroxyfarnesol as the major metabolite, as does CYP4C7 Priestia megaterium ?
-
 ?
geraniol + [reduced NADPH-hemoprotein reductase] + O2
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 Priestia megaterium 8-hydroxygeraniol + 10-hydroxygeraniol + [oxidized NADPH-hemoprotein reductase] + H2O
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 ?
lauric acid + [reduced NADPH-hemoprotein reductase] + O2 products of hydroxylation by wild-type CYP102A1 are 11-OH, 10-OH, 9-OH, 8-OH, 7-OH, and 6-OH, corresponding to omega-1 to omega-6 hydroxylation Priestia megaterium ?
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 ?
methyl 10,11-epoxyfarnesoate + [reduced NADPH-hemoprotein reductase] + O2 the major product of C(78-82,F87L,328-330) during 10,11-epoxymethylfarnesoate oxidation is determined to be the 12-hydroxy isomer Priestia megaterium ?
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 ?
methyl farnesoate + O2 + NADPH the major product of C(78-82,F87L,328-330) during methylfarnesoate oxidation is determined to be the 12-hydroxy isomer Priestia megaterium ?
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 ?
palmitic acid + [reduced NADPH-hemoprotein reductase] + O2 products of hydroxylation by wild-type CYP102A1 are 15-OH, 14-OH, 13-OH, 12-OH, 11-OH, and 10-OH, corresponding to omega-1 to omega-6 hydroxylation, with omega-1 to omega-3 being the major products in both cases Priestia megaterium ?
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 ?

Synonyms

Synonyms Comment Organism
CYP102A1
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 Priestia megaterium
cytochrome P450 BM3
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 Priestia megaterium

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
 additional information scanning chimeragenesis succeeds in changing bacterial monooxygenase CYP102A1 into an enzyme capable of carrying out the major reaction of insect terpenoid omega-hydroxylase CYP4C7, with a 100fold increase in turnover number Priestia megaterium

Cofactor

Cofactor Comment Organism Structure
NADPH
-
 Priestia megaterium