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Title:
Reduced Pterins as Scavengers for Reactive Oxygen Species | SpringerLink
Description:
Pterins are widely distributed in nature in three forms: tetrahydro, dihydro, and oxidized. The most studied pterin is L-erythro-5,6,7,8-tetrahydrobiopterin (BH4), the electron donor for mixed function oxidases, such as Phe hydroxylase during the conversion of Phe to...
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ScholarlyArticle:
headline:Reduced Pterins as Scavengers for Reactive Oxygen Species
pageEnd:354
pageStart:351
image:https://media.springernature.com/w153/springer-static/cover/book/978-1-4615-2960-6.jpg
genre:
Biomedical and Life Sciences
Biomedical and Life Sciences (R0)
isPartOf:
name:Chemistry and Biology of Pteridines and Folates
isbn:
978-1-4615-2960-6
978-1-4613-6287-6
type:Book
publisher:
name:Springer US
logo:
url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
type:ImageObject
type:Organization
author:
name:Rong-sen Shen
affiliation:
name:The University of Texas Medical Branch
address:
name:Department of Human Biological Chemistry and Genetics, The University of Texas Medical Branch, Galveston, USA
type:PostalAddress
type:Organization
type:Person
name:Yixian Zhang
affiliation:
name:The University of Texas Medical Branch
address:
name:Department of Human Biological Chemistry and Genetics, The University of Texas Medical Branch, Galveston, USA
type:PostalAddress
type:Organization
type:Person
keywords:Nitric Oxide, Antioxidant System, Mixed Function Oxidase, Boric Acid Solution, Dihydropteridine Reductase
description:Pterins are widely distributed in nature in three forms: tetrahydro, dihydro, and oxidized. The most studied pterin is L-erythro-5,6,7,8-tetrahydrobiopterin (BH4), the electron donor for mixed function oxidases, such as Phe hydroxylase during the conversion of Phe to Tyr, and Tyr and Trp hydroxylases during biogenic amine synthesis.1 BH4 also serves as the cofactor for nitric oxide synthase which produces nitric oxide from the vascular endothelium, platelets, neutrophils, and neurons.2 Upon oxidation to the quinonoid dihydrobiopterin (qBH2), BH4 is regenerated by dihydropteridine reductase (NAD[P]H:6,7-dihydropteridine oxidoreductase, EC 1.6.99.7;DHPR) using NADH as cofactor.3 BH4 and DHPR are ubiquitous.4 Their parallel distribution in some organs and blood cells which apparently do not synthesize catecholamine neurotransmitters and/or nitric oxide, implies that BH4 and DHPR may involve in other physiological functions.
datePublished:1993
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isbn:
978-1-4615-2960-6
978-1-4613-6287-6
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name:Springer US
logo:
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name:The University of Texas Medical Branch
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name:Rong-sen Shen
affiliation:
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type:PostalAddress
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name:Yixian Zhang
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name:The University of Texas Medical Branch
address:
name:Department of Human Biological Chemistry and Genetics, The University of Texas Medical Branch, Galveston, USA
type:PostalAddress
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PostalAddress:
name:Department of Human Biological Chemistry and Genetics, The University of Texas Medical Branch, Galveston, USA
name:Department of Human Biological Chemistry and Genetics, The University of Texas Medical Branch, Galveston, USA
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