By Antje Chang, Dietmar Schomburg, Ida Schomburg
The Springer guide of Enzymes presents concise information on a few 5,000 enzymes sufficiently good characterised – and this is the second one, up to date version. Their program in analytical, artificial and biotechnology procedures in addition to in meals undefined, and for medicinal remedies is additional. information sheets are prepared of their EC-Number series. the recent variation displays significant growth in enzymology: the full fabric has greater than doubled, and the entire 2d version contains 39 volumes plus Synonym Index. beginning in 2009, all newly categorized enzymes are taken care of in complement Volumes.
Read Online or Download Class 1 Oxidoreductases XII: EC 1.14.15 - 1.97 (Springer Handbook of Enzymes) PDF
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Extra resources for Class 1 Oxidoreductases XII: EC 1.14.15 - 1.97 (Springer Handbook of Enzymes)
Res. : Relation between evolutionary distance and enzymic properties among the members of the CYP52A subfamily of Candida maltosa. Biochem. Biophys. Res. : Glu-325 and Asp-328 are determinants of the cyp4A1 hydroxylation regiospecificity and resistance to inactivation by 1-aminobenzotriazole. : Subcellular location of enzymes involved in oxidation of n-alkane by Cladosporium resinae. Appl. Microbiol. : Homology modeling and substrate binding study of human CYP4A11 enzyme. : Structural determination of the substrate specificities and regioselectivities of the rat and human fatty acid w-hydroxylases.
1> )  n-octanol + oxidized rubredoxin + H2 O palmitic acid + NAD(P)H + H+ + O2 <5-8> (Reversibility: ? <5-8> [11, 12-15, 17, 18, 23]) [11, 12-15, 17, 18, 23] 16-hydroxyhexadecanoic acid + NAD(P)+ + H2 O phosphatidylethanolamine + NADH + H+ + O2 <1> (Reversibility: ? <1> )  ? phosphatidylserine + NADH + H+ + O2 <1> (Reversibility: ? <1> )  ? prostaglandin A1 + NADPH + O2 <5, 6> (Reversibility: ? <5, 6> [11, 12, 17]) [11, 12, 17] ? 3 Alkane 1-monooxygenase S P S P S prostaglandin A2 + NADPH + O2 <5> (Reversibility: ?
Biol. : Enzymatic w-oxidation. IV. Purification and properties of the w-hydroxylase of Pseudomonas oleovorans. J. Biol. : Identification of the whydroxylase of Pseudomonas oleovorans as a nonheme iron protein requiring phospholipid for catalytic activity. Biochem. Biophys. Res. : Characterization of the w-hydroxylase of Pseudomonas oleovorans as a nonheme iron protein. Arch. Biochem. : Fatty acid w-hydroxylase (alkane hydroxylase) from Pseudomonas oleovorans. : A new n-alkane oxidation system from Pseudomonas aeruginosa S7B1.
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