Dual positional substrate specificity of rice allene oxide synthase-1: insight into mechanism of inhibition by type II ligand imidazole

Dual positional substrate specificity of rice allene oxide synthase-1: insight into mechanism of inhibition by type II ligand imidazole

Phylogenetic and amino acid sequence analysis indicated thatrice allene oxide synthase-1 (OsAOS1) is CYP74, and is clearlydistinct from CYP74B, C and D subfamilies. Regio- andstereo-chemical analysis revealed the dual substrate specificityof OsAOS1 for (cis,trans)-configurational isomers of 13(S)- a...

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Main Authors: Sereyvath Yoeun, Randeep Rakwal, Oksoo Han
Format: Article
Language:English
Published: Korean Society for Biochemistry and Molecular Biology 2013-03-01
Series:BMB Reports
Subjects:
Allene oxide synthase
Cytochrome P450
Enzyme
Lipid
Octadecanoid
Online Access:http://bmbreports.org/jbmb/pdf.php?data=MTMwOTI3MTBAcGRmX3JhaW50cmFjZV9sZWV5c0AlNUI0Ni0zJTVEMTMwMzI3MjEyNF8lMjgxNTEtMTU2JTI5Qk1CXzEyLTExNy5wZGY=
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spelling doaj-adf200ccbbe44a3284bc3f3bfd068f8d2020-11-25T01:43:14ZengKorean Society for Biochemistry and Molecular BiologyBMB Reports1976-66961976-670X2013-03-01463151156http://dx.doi.org/10.5483/BMBRep.2013.46.3.117Dual positional substrate specificity of rice allene oxide synthase-1: insight into mechanism of inhibition by type II ligand imidazoleSereyvath YoeunRandeep RakwalOksoo HanPhylogenetic and amino acid sequence analysis indicated thatrice allene oxide synthase-1 (OsAOS1) is CYP74, and is clearlydistinct from CYP74B, C and D subfamilies. Regio- andstereo-chemical analysis revealed the dual substrate specificityof OsAOS1 for (cis,trans)-configurational isomers of 13(S)- and9(S)-hydroperoxyoctadecadienoic acid. GC-MS analysis showedthat OsAOS1 converts 13(S)- and 9(S)-hydroperoxyoctadecadi(tri)enoic acid into their corresponding allene oxide.UV-Visible spectral analysis of native OsAOS1 revealed a Soretmaximum at 393 nm, which shifted to 424 nm with severalclean isobestic points upon binding of OsAOS1 to imidazole.The spectral shift induced by imidazole correlated withinhibition of OsAOS1 activity, implying that imidazole maycoordinate to ferric heme iron, triggering a heme-iron transitionfrom high spin state to low spin state. The implications andsignificance of a putative type II ligand-induced spin statetransition in OsAOS1 are discussed. [BMB Reports 2013; 46(3):151-156]http://bmbreports.org/jbmb/pdf.php?data=MTMwOTI3MTBAcGRmX3JhaW50cmFjZV9sZWV5c0AlNUI0Ni0zJTVEMTMwMzI3MjEyNF8lMjgxNTEtMTU2JTI5Qk1CXzEyLTExNy5wZGY=Allene oxide synthaseCytochrome P450EnzymeLipidOctadecanoid
collection DOAJ
language English
format Article
sources DOAJ
author Sereyvath Yoeun
Randeep Rakwal
Oksoo Han
spellingShingle Sereyvath Yoeun
Randeep Rakwal
Oksoo Han
Dual positional substrate specificity of rice allene oxide synthase-1: insight into mechanism of inhibition by type II ligand imidazole
BMB Reports
Allene oxide synthase
Cytochrome P450
Enzyme
Lipid
Octadecanoid
author_facet Sereyvath Yoeun
Randeep Rakwal
Oksoo Han
author_sort Sereyvath Yoeun
title Dual positional substrate specificity of rice allene oxide synthase-1: insight into mechanism of inhibition by type II ligand imidazole
title_short Dual positional substrate specificity of rice allene oxide synthase-1: insight into mechanism of inhibition by type II ligand imidazole
title_full Dual positional substrate specificity of rice allene oxide synthase-1: insight into mechanism of inhibition by type II ligand imidazole
title_fullStr Dual positional substrate specificity of rice allene oxide synthase-1: insight into mechanism of inhibition by type II ligand imidazole
title_full_unstemmed Dual positional substrate specificity of rice allene oxide synthase-1: insight into mechanism of inhibition by type II ligand imidazole
title_sort dual positional substrate specificity of rice allene oxide synthase-1: insight into mechanism of inhibition by type ii ligand imidazole
publisher Korean Society for Biochemistry and Molecular Biology
series BMB Reports
issn 1976-6696
1976-670X
publishDate 2013-03-01
description Phylogenetic and amino acid sequence analysis indicated thatrice allene oxide synthase-1 (OsAOS1) is CYP74, and is clearlydistinct from CYP74B, C and D subfamilies. Regio- andstereo-chemical analysis revealed the dual substrate specificityof OsAOS1 for (cis,trans)-configurational isomers of 13(S)- and9(S)-hydroperoxyoctadecadienoic acid. GC-MS analysis showedthat OsAOS1 converts 13(S)- and 9(S)-hydroperoxyoctadecadi(tri)enoic acid into their corresponding allene oxide.UV-Visible spectral analysis of native OsAOS1 revealed a Soretmaximum at 393 nm, which shifted to 424 nm with severalclean isobestic points upon binding of OsAOS1 to imidazole.The spectral shift induced by imidazole correlated withinhibition of OsAOS1 activity, implying that imidazole maycoordinate to ferric heme iron, triggering a heme-iron transitionfrom high spin state to low spin state. The implications andsignificance of a putative type II ligand-induced spin statetransition in OsAOS1 are discussed. [BMB Reports 2013; 46(3):151-156]
topic Allene oxide synthase
Cytochrome P450
Enzyme
Lipid
Octadecanoid
url http://bmbreports.org/jbmb/pdf.php?data=MTMwOTI3MTBAcGRmX3JhaW50cmFjZV9sZWV5c0AlNUI0Ni0zJTVEMTMwMzI3MjEyNF8lMjgxNTEtMTU2JTI5Qk1CXzEyLTExNy5wZGY=
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AT randeeprakwal dualpositionalsubstratespecificityofricealleneoxidesynthase1insightintomechanismofinhibitionbytypeiiligandimidazole
AT oksoohan dualpositionalsubstratespecificityofricealleneoxidesynthase1insightintomechanismofinhibitionbytypeiiligandimidazole
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