Document Detail


Vascular peroxidase 1 catalyzes the formation of hypohalous acids: characterization of its substrate specificity and enzymatic properties.
MedLine Citation:
PMID:  22982576     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The heme-containing peroxidase family comprises eight members in humans. The physiological and pathophysiological roles of heme-containing peroxidases are not well understood. Phagocyte-derived myeloperoxidase (MPO) utilizes chloride and bromide, in the presence of hydrogen peroxide (H(2)O(2)), to generate hypochlorous acid and hypobromous acid, potent oxidizing species that are known to kill invading pathogens. Vascular peroxidase 1 (VPO1) is a new member of the heme-containing peroxidase family; VPO1 is highly expressed in the cardiovascular system, lung, liver, pancreas, and spleen. However, functional roles of VPO1 have not been defined. In this report, we demonstrate the capacity for VPO1 to catalyze the formation of hypohalous acids, and characterize its enzymatic properties. VPO1, like MPO but unlike lactoperoxidase, is able to generate hypochlorous acid, hypobromous acid, and hypothiocyanous acid in the presence of H(2)O(2). Under physiological pH and concentrations of halides (100μM KBr, 100μM KSCN, and 100mM NaCl), VPO1 utilizes approximately 45% of H(2)O(2) for the generation of hypobromous acid, 35% for hypothiocyanous acid, and 18% for hypochlorous acid. The specific activity of VPO1 is ∼10- to 70-fold lower than that of MPO, depending on the specific substrate. These studies demonstrate that the enzymatic properties and substrate specificity of VPO1 are similar to MPO; however, significantly lower catalytic rate constants of VPO1 relative to MPO suggest the possibility of other physiologic roles for this novel heme-containing peroxidase.
Authors:
Hong Li; Zehong Cao; Guogang Zhang; Victor J Thannickal; Guangjie Cheng
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't     Date:  2012-09-12
Journal Detail:
Title:  Free radical biology & medicine     Volume:  53     ISSN:  1873-4596     ISO Abbreviation:  Free Radic. Biol. Med.     Publication Date:  2012 Nov 
Date Detail:
Created Date:  2012-11-09     Completed Date:  2013-06-10     Revised Date:  2013-12-04    
Medline Journal Info:
Nlm Unique ID:  8709159     Medline TA:  Free Radic Biol Med     Country:  United States    
Other Details:
Languages:  eng     Pagination:  1954-9     Citation Subset:  IM    
Copyright Information:
Copyright © 2012 Elsevier Inc. All rights reserved.
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MeSH Terms
Descriptor/Qualifier:
Biocatalysis
Bromates / chemistry,  metabolism*
Heme / analysis
Humans
Hydrogen Peroxide / chemistry,  metabolism
Hypochlorous Acid / chemistry,  metabolism*
Kinetics
Oxidation-Reduction
Peroxidase / metabolism
Peroxidases / metabolism*
Substrate Specificity
Taurine / metabolism
Thiocyanates / chemistry,  metabolism*
Grant Support
ID/Acronym/Agency:
R01 HL067967/HL/NHLBI NIH HHS; R01 HL086836/HL/NHLBI NIH HHS; R01 HL094230/HL/NHLBI NIH HHS; R01HL067967/HL/NHLBI NIH HHS; R01HL086836/HL/NHLBI NIH HHS
Chemical
Reg. No./Substance:
0/Bromates; 0/Thiocyanates; 0/hypothiocyanous acid; 1EQV5MLY3D/Taurine; 42VZT0U6YR/Heme; 712K4CDC10/Hypochlorous Acid; BBX060AN9V/Hydrogen Peroxide; EC 1.11.1.-/Peroxidases; EC 1.11.1.-/VPO1 protein, human; EC 1.11.1.7/Peroxidase; GHT9BV419J/hypobromous acid
Comments/Corrections

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