About: The complete amino acid sequence of the mature form of rat sepiapterin reductase

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About: The complete amino acid sequence of the mature form of rat sepiapterin reductase Goto Sponge NotDistinct Permalink

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scientific article published on 01 December 1990

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована в грудні 1990 (uk) article scientifique publié en 1990 (fr) im Dezember 1990 veröffentlichter wissenschaftlicher Artikel (de) artículu científicu espublizáu n'avientu de 1990 (ast) scientific article published on 01 December 1990 (en)
publication date	wds:Q68635632-B9565321-0F86-4555-8ADA-61C813914380
publication date	1990-12-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q68635632-C9CF0389-A238-40A0-8D7E-B12D4788DBBB
language of work or name	English
cites work	wds:Q68635632-081107E6-0C42-4F04-BAC6-C49F8F27949A wds:Q68635632-2682E553-7D8A-47F4-990D-64F3F4247E95 wds:Q68635632-2AEB5E60-A22C-4280-97D0-BA3287DBE788 wds:Q68635632-3799BFEC-F938-44FC-B7C2-D5FABD59A386 wds:Q68635632-3B556B72-AC57-47BA-A770-7C2FDF073455 wds:Q68635632-53E96FE9-D9B7-430B-B55F-5E545093D51C wds:Q68635632-7CCB4471-3145-4C0E-9B3D-BA5754D45423 wds:Q68635632-7FA00A22-7163-4108-B385-E62012ABC493 wds:Q68635632-8CA37F3F-4560-44C0-996D-0F1461118AAC wds:Q68635632-920C3D3D-4261-447D-9777-CD9516A33800 wds:Q68635632-9B4CA24F-D292-4116-A0EE-EF00E818778C wds:Q68635632-AEB2EF13-C04A-496E-A7FB-D25D19FD2184 wds:Q68635632-B756752E-503F-4394-8BE7-10EDA17F09DF wds:Q68635632-CAB79EBC-79CF-4756-98CE-2078903E1B4F wds:Q68635632-F06B6C11-3602-4D5C-90D9-5B34A3E707AE
cites work	CFS hydroxylase cofactor levels in some neurological diseases Studies on a new proteolytic enzyme from A chromobacter lyticus M497-1. I. Purification and some enzymatic properties Biosynthesis of tetrahydrobiopterin: conversion of dihydroneopterin triphosphate to tetrahydropterin intermediates Tetrahydrobiopterin biosynthesis. Studies with specifically labeled (2H)NAD(P)H and 2H2O and of the enzymes involved Liquid chromatographic determination of amino acids after gas-phase hydrolysis and derivatization with (dimethylamino)azobenzenesulfonyl chloride Sepiapterin reductase from horse liver: purification and properties of the enzyme Amino acid sequence of the regulatory subunit of bovine type I adenosine cyclic 3',5'-phosphate dependent protein kinase On the role of sepiapterin reductase in the biosynthesis of tetrahydrobiopterin Isomerization of 6-lactoyl tetrahydropterin by sepiapterin reductase Purification and characterization of sepiapterin reductase from rat erythrocytes Sepiapterin reductase exhibits a NADPH-dependent dicarbonyl reductase activity Carbonyl reductase activity of sepiapterin reductase from rat erythrocytes Biopterin in human brain and urine from controls and parkinsonian patients: Application of a new radioimmunoassay Sepiapterin reductase Dyspropterin, an intermediate formed from dihydroneopterin triphosphate in the biosynthetic pathway of tetrahydrobiopterin
author name string	wds:Q68635632-11E4BCEF-62C7-4490-A1B8-6F8B09862C59 wds:Q68635632-5A90339D-D2B4-4C1A-9FD6-47D4B9E6D5BC wds:Q68635632-BC3ACEE8-7A61-4446-BF35-A1D12DE67321 wds:Q68635632-ED4AE46F-8628-4053-BA05-169EC49E2347 wds:Q68635632-F0D8FA4C-FBFF-4F84-B16B-1CD74F815EBD wds:Q68635632-F40670FB-B7D0-4EEE-98F6-90D38F308A6C
author name string	M Suzuki T Nagatsu S Katoh K Titani R Oyama T Sueoka
rdfs:label	The complete amino acid sequence of the mature form of rat sepiapterin reductase (en) The complete amino acid sequence of the mature form of rat sepiapterin reductase (nl)
skos:prefLabel	The complete amino acid sequence of the mature form of rat sepiapterin reductase (en) The complete amino acid sequence of the mature form of rat sepiapterin reductase (nl)
name	The complete amino acid sequence of the mature form of rat sepiapterin reductase (en) The complete amino acid sequence of the mature form of rat sepiapterin reductase (nl)
author	wds:Q68635632-33C5B8EA-9483-4AED-95D2-CED3D2ADA3A5
author	Hiroshi Ichinose
title	wds:Q68635632-A0C040F5-8E7A-4667-8AB1-6D8E0A381068
title	The complete amino acid sequence of the mature form of rat sepiapterin reductase (en)
page(s)	wds:Q68635632-211F45E8-C38B-4DE4-AE31-13F113066FB0
page(s)	627-631
instance of	wds:Q68635632-BFDA065E-368B-456C-A0A1-AAF182F322C5
instance of	scholarly article
PubMed ID	wds:Q68635632-07AAA504-338E-4C87-A59A-39FBB655EC41
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/2260974
PubMed ID	2260974
published in	wds:Q68635632-441E813D-CDA0-4E1F-8124-857EDCE3468C
published in	Biochemical and Biophysical Research Communications
issue	wds:Q68635632-1043B1B3-BA43-4D7E-B698-C4F046237B30
volume	wds:Q68635632-58BE50CB-1EAC-4AEA-BE69-B7362134E3F8
issue	2
volume	173
DOI	wds:Q68635632-19FEAA0D-EBCD-4341-B79D-BC031446D813
DOI	http://dx.doi.org/10.1016/S0006-291X(05)80081-6
DOI	10.1016/S0006-291X(05)80081-6
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q68635632
is cites work of	Cloning and sequencing of cDNA encoding human sepiapterin reductase--an enzyme involved in tetrahydrobiopterin biosynthesis Multiple mRNA forms of human GTP cyclohydrolase I Tetrahydrobiopterin biosynthesis, regeneration and functions Phosphorylation by Ca2+/calmodulin-dependent protein kinase II and protein kinase C of sepiapterin reductase, the terminal enzyme in the biosynthetic pathway of tetrahydrobiopterin Functionally important residues tyrosine-171 and serine-158 in sepiapterin reductase Mutational analysis of sites in sepiapterin reductase phosphorylated by Ca2+/calmodulin-dependent protein kinase II Mutations in the sepiapterin reductase gene cause a novel tetrahydrobiopterin-dependent monoamine-neurotransmitter deficiency without hyperphenylalaninemia Localization of sepiapterin reductase in the human brain Sepiapterin reductase regulation of endothelial tetrahydrobiopterin and nitric oxide bioavailability. The catecholamine system in health and disease -Relation to tyrosine 3-monooxygenase and other catecholamine-synthesizing enzymes Effect of antisense oligodeoxynucleotide for sepiapterin reductase on the viability of PC12 cells in the presence of exogenous carbonyl compounds Role of the conserved Ser-Tyr-Lys triad of the SDR family in sepiapterin reductase
is cites work of	wds:Q28609858-67E22BE7-52BD-4AA4-B01C-F81C039DB52E wds:Q28251068-31C667FA-CACD-4942-933E-1CCBE3DD35E0 wds:Q35115456-E93235E2-9F80-4CD6-84D2-D0C1C87FEF3F wds:Q28578204-7C5A8F3E-2B44-46AC-9268-F602CE949927 wds:Q44203413-6B6D659B-121B-4721-8B88-ABEC0C219849 wds:Q24531994-B1F18897-63CF-43E0-9D5F-99575541DBC1 wds:Q24318818-26FEE7EE-1765-4303-ACED-CD5C6EA86DA7 wds:Q24535755-0989A187-6FCF-407E-8E7B-E46B0A2C191B

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