Tags

Type your tag names separated by a space and hit enter

Biogenesis of volatile aldehydes from fatty acid hydroperoxides: molecular cloning of a hydroperoxide lyase (CYP74C) with specificity for both the 9- and 13-hydroperoxides of linoleic and linolenic acids.
Arch Biochem Biophys. 2001 Feb 15; 386(2):281-9.AB

Abstract

A novel member of the plant cytochrome P450 CYP74 family of fatty acid hydroperoxide metabolizing enzymes has been cloned from melon fruit (Cucumis melo). The cDNA is comprised of 1,446 nucleotides encoding a protein of 481 amino acids. The homology at the amino acid level to other members of the CYP74 family is 35-50%, the closest relatives being allene oxide synthases. The cDNA was expressed in Escherichia coli, and the corresponding protein was purified by affinity column chromatography. The native enzyme showed a main Soret band at 418 nm, indicative of a low spin ferric cytochrome P450, and a 447-nm peak appeared in the CO-difference spectrum. Using [U-14C]radiolabeled substrate, HPLC, UV, and GC-MS, the products of conversion of 9S-hydroperoxy-linoleic acid were identified as 9-oxo-nonanic acid and 3Z-nonenal. Kinetic analysis of this hydroperoxide lyase showed the highest rate of reaction with 9-hydroperoxy-linolenic acid followed by 9-hydroperoxy-linoleic acid and then the corresponding 13-hydroperoxides. Overall, the newly characterized cytochrome P450 enzyme is a fatty acid hydroperoxide lyase with a preference, but not absolute specificity for the 9-positional hydroperoxides of linoleic and linolenic acids.

Authors+Show Affiliations

Department of Pharmacology, Vanderbilt University Medical School, Nashville, Tennessee 37232, USA.No affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article

Language

eng

PubMed ID

11368353

Citation

Tijet, N, et al. "Biogenesis of Volatile Aldehydes From Fatty Acid Hydroperoxides: Molecular Cloning of a Hydroperoxide Lyase (CYP74C) With Specificity for Both the 9- and 13-hydroperoxides of Linoleic and Linolenic Acids." Archives of Biochemistry and Biophysics, vol. 386, no. 2, 2001, pp. 281-9.
Tijet N, Schneider C, Muller BL, et al. Biogenesis of volatile aldehydes from fatty acid hydroperoxides: molecular cloning of a hydroperoxide lyase (CYP74C) with specificity for both the 9- and 13-hydroperoxides of linoleic and linolenic acids. Arch Biochem Biophys. 2001;386(2):281-9.
Tijet, N., Schneider, C., Muller, B. L., & Brash, A. R. (2001). Biogenesis of volatile aldehydes from fatty acid hydroperoxides: molecular cloning of a hydroperoxide lyase (CYP74C) with specificity for both the 9- and 13-hydroperoxides of linoleic and linolenic acids. Archives of Biochemistry and Biophysics, 386(2), 281-9.
Tijet N, et al. Biogenesis of Volatile Aldehydes From Fatty Acid Hydroperoxides: Molecular Cloning of a Hydroperoxide Lyase (CYP74C) With Specificity for Both the 9- and 13-hydroperoxides of Linoleic and Linolenic Acids. Arch Biochem Biophys. 2001 Feb 15;386(2):281-9. PubMed PMID: 11368353.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Biogenesis of volatile aldehydes from fatty acid hydroperoxides: molecular cloning of a hydroperoxide lyase (CYP74C) with specificity for both the 9- and 13-hydroperoxides of linoleic and linolenic acids. AU - Tijet,N, AU - Schneider,C, AU - Muller,B L, AU - Brash,A R, PY - 2001/5/23/pubmed PY - 2001/6/8/medline PY - 2001/5/23/entrez SP - 281 EP - 9 JF - Archives of biochemistry and biophysics JO - Arch Biochem Biophys VL - 386 IS - 2 N2 - A novel member of the plant cytochrome P450 CYP74 family of fatty acid hydroperoxide metabolizing enzymes has been cloned from melon fruit (Cucumis melo). The cDNA is comprised of 1,446 nucleotides encoding a protein of 481 amino acids. The homology at the amino acid level to other members of the CYP74 family is 35-50%, the closest relatives being allene oxide synthases. The cDNA was expressed in Escherichia coli, and the corresponding protein was purified by affinity column chromatography. The native enzyme showed a main Soret band at 418 nm, indicative of a low spin ferric cytochrome P450, and a 447-nm peak appeared in the CO-difference spectrum. Using [U-14C]radiolabeled substrate, HPLC, UV, and GC-MS, the products of conversion of 9S-hydroperoxy-linoleic acid were identified as 9-oxo-nonanic acid and 3Z-nonenal. Kinetic analysis of this hydroperoxide lyase showed the highest rate of reaction with 9-hydroperoxy-linolenic acid followed by 9-hydroperoxy-linoleic acid and then the corresponding 13-hydroperoxides. Overall, the newly characterized cytochrome P450 enzyme is a fatty acid hydroperoxide lyase with a preference, but not absolute specificity for the 9-positional hydroperoxides of linoleic and linolenic acids. SN - 0003-9861 UR - https://www.unboundmedicine.com/medline/citation/11368353/Biogenesis_of_volatile_aldehydes_from_fatty_acid_hydroperoxides:_molecular_cloning_of_a_hydroperoxide_lyase__CYP74C__with_specificity_for_both_the_9__and_13_hydroperoxides_of_linoleic_and_linolenic_acids_ DB - PRIME DP - Unbound Medicine ER -