Literature DB >> 2511841

Human liver 6-pyruvoyl tetrahydropterin reductase is biochemically and immunologically indistinguishable from aldose reductase.

P Steinerstauch1, B Wermuth, W Leimbacher, H C Curtius.   

Abstract

6-Pyruvoyl tetrahydropterin reductase has been implicated in the biosynthesis of tetrahydrobiopterin. Using immunochemical and biochemical techniques the purified human liver enzyme was shown to be identical to aldose reductase. This suggests that 6-pyruvoyl tetrahydropterin reductase may play an additional role in the reduction of aldehydes derived from the biogenic amine neuro-transmitters and corticosteroid hormones as well as in the pathogenesis of diabetic complications, as has been postulated for aldose reductase.

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Year:  1989        PMID: 2511841     DOI: 10.1016/0006-291x(89)91786-5

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  3 in total

1.  Mutations in the sepiapterin reductase gene cause a novel tetrahydrobiopterin-dependent monoamine-neurotransmitter deficiency without hyperphenylalaninemia.

Authors:  L Bonafé; B Thöny; J M Penzien; B Czarnecki; N Blau
Journal:  Am J Hum Genet       Date:  2001-07-06       Impact factor: 11.025

2.  Production of sepiapterin in Escherichia coli by coexpression of cyanobacterial GTP cyclohydrolase I and human 6-pyruvoyltetrahydropterin synthase.

Authors:  Hyun Joo Woo; Jee Yun Kang; Yong Kee Choi; Young Shik Park
Journal:  Appl Environ Microbiol       Date:  2002-06       Impact factor: 4.792

3.  Isolation and expression of rat liver sepiapterin reductase cDNA.

Authors:  B A Citron; S Milstien; J C Gutierrez; R A Levine; B L Yanak; S Kaufman
Journal:  Proc Natl Acad Sci U S A       Date:  1990-08       Impact factor: 11.205

  3 in total

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