Literature DB >> 11224565

Crystal structure of rat biliverdin reductase.

A Kikuchi1, S Y Park, H Miyatake, D Sun, M Sato, T Yoshida, Y Shiro.   

Abstract

Biliverdin reductase (BVR) is a soluble cytoplasmic enzyme that catalyzes the conversion of biliverdin to bilirubin using NADH or NADPH as electron donor. Bilirubin is a significant biological antioxidant, but it is also neurotoxic and the cause of kernicterus. In this study, we have determined the crystal structure of rat BVR at 1.4 A resolution. The structure contains two domains: an N-terminal domain characteristic of a dinucleotide binding fold (Rossmann fold) and a C-terminal domain that is predominantly an antiparallel six-stranded beta-sheet. Based on this structure, we propose modes of binding for NAD(P)H and biliverdin, and a possible mechanism for the enzyme.

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Year:  2001        PMID： 11224565     DOI： 10.1038/84955

Source DB:  PubMed          Journal:  Nat Struct Biol        ISSN： 1072-8368


  30 in total

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Journal:  Proc Natl Acad Sci U S A       Date:  2008-05-07       Impact factor: 11.205

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Journal:  Cell Chem Biol       Date:  2019-07-25       Impact factor: 8.116

9.  A novel sensor of NADH/NAD+ redox poise in Streptomyces coelicolor A3(2).

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