Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1995-4-13
pubmed:abstractText
GTP cyclohydrolase I catalyses the first committing step in the biosynthesis of the pterin moiety of folic acid: conversion of GTP to dihydroneopterin triphosphate. GTP cyclohydrolase I of Bacillus subtilis was purified to homogeneity and shown to have a homo-octameric structure. The enzyme had an apparent Km for GTP of 4 microM and, in the absence of cations, a Vmax. of 80 nmol/min per mg of protein. K+ ions moderately increased its Vmax., whereas UTP and Ca2+ and Mg2+ ions drastically increased its Km for GTP. Dihydrofolate and other products of the folate and tetrahydrobiopterin pathways did not inhibit GTP cyclohydrolase I. In addition to their effect on the enzyme activity, Ca2+ and Mg2+ ions catalysed the chemical dephosphorylation of dihydroneopterin triphosphate to non-cyclic dihydroneopterin monophosphate, the substrate for the phosphomonoesterase reaction in folate biosynthesis. This dephosphorylation was specific and did not require the action of a phosphatase. We suggest a physiological role for Ca2+ ions and UTP in regulation of folate biosynthesis at the levels of GTP cyclohydrolase I and dephosphorylation of dihydroneopterin triphosphate.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/7887891-103543, http://linkedlifedata.com/resource/pubmed/commentcorrection/7887891-1356983, http://linkedlifedata.com/resource/pubmed/commentcorrection/7887891-1459137, http://linkedlifedata.com/resource/pubmed/commentcorrection/7887891-1563478, http://linkedlifedata.com/resource/pubmed/commentcorrection/7887891-1665332, http://linkedlifedata.com/resource/pubmed/commentcorrection/7887891-1702732, http://linkedlifedata.com/resource/pubmed/commentcorrection/7887891-1905717, http://linkedlifedata.com/resource/pubmed/commentcorrection/7887891-2115863, http://linkedlifedata.com/resource/pubmed/commentcorrection/7887891-2116574, http://linkedlifedata.com/resource/pubmed/commentcorrection/7887891-2120210, http://linkedlifedata.com/resource/pubmed/commentcorrection/7887891-2123343, http://linkedlifedata.com/resource/pubmed/commentcorrection/7887891-2154472, http://linkedlifedata.com/resource/pubmed/commentcorrection/7887891-2463916, http://linkedlifedata.com/resource/pubmed/commentcorrection/7887891-2557335, http://linkedlifedata.com/resource/pubmed/commentcorrection/7887891-2584186, http://linkedlifedata.com/resource/pubmed/commentcorrection/7887891-2584226, http://linkedlifedata.com/resource/pubmed/commentcorrection/7887891-2762302, http://linkedlifedata.com/resource/pubmed/commentcorrection/7887891-2862841, http://linkedlifedata.com/resource/pubmed/commentcorrection/7887891-3004429, http://linkedlifedata.com/resource/pubmed/commentcorrection/7887891-3080426, http://linkedlifedata.com/resource/pubmed/commentcorrection/7887891-3254432, http://linkedlifedata.com/resource/pubmed/commentcorrection/7887891-3349105, http://linkedlifedata.com/resource/pubmed/commentcorrection/7887891-3547188, http://linkedlifedata.com/resource/pubmed/commentcorrection/7887891-3891906, http://linkedlifedata.com/resource/pubmed/commentcorrection/7887891-396813, http://linkedlifedata.com/resource/pubmed/commentcorrection/7887891-4296838, http://linkedlifedata.com/resource/pubmed/commentcorrection/7887891-4334904, http://linkedlifedata.com/resource/pubmed/commentcorrection/7887891-4362677, http://linkedlifedata.com/resource/pubmed/commentcorrection/7887891-4415400, http://linkedlifedata.com/resource/pubmed/commentcorrection/7887891-4904679, http://linkedlifedata.com/resource/pubmed/commentcorrection/7887891-6276567, http://linkedlifedata.com/resource/pubmed/commentcorrection/7887891-6286632, http://linkedlifedata.com/resource/pubmed/commentcorrection/7887891-6696731, http://linkedlifedata.com/resource/pubmed/commentcorrection/7887891-6800221, http://linkedlifedata.com/resource/pubmed/commentcorrection/7887891-7017928, http://linkedlifedata.com/resource/pubmed/commentcorrection/7887891-776973, http://linkedlifedata.com/resource/pubmed/commentcorrection/7887891-821948, http://linkedlifedata.com/resource/pubmed/commentcorrection/7887891-8502995
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Calcium, http://linkedlifedata.com/resource/pubmed/chemical/Folic Acid, http://linkedlifedata.com/resource/pubmed/chemical/GTP Cyclohydrolase, http://linkedlifedata.com/resource/pubmed/chemical/Guanosine Triphosphate, http://linkedlifedata.com/resource/pubmed/chemical/Magnesium, http://linkedlifedata.com/resource/pubmed/chemical/Neopterin, http://linkedlifedata.com/resource/pubmed/chemical/Potassium, http://linkedlifedata.com/resource/pubmed/chemical/Pteridines, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Uridine Triphosphate, http://linkedlifedata.com/resource/pubmed/chemical/dihydrofolate, http://linkedlifedata.com/resource/pubmed/chemical/dihydroneopterin triphosphate
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0264-6021
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
306 ( Pt 2)
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
371-7
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed-meshheading:7887891-Bacillus subtilis, pubmed-meshheading:7887891-Base Sequence, pubmed-meshheading:7887891-Binding, Competitive, pubmed-meshheading:7887891-Calcium, pubmed-meshheading:7887891-Folic Acid, pubmed-meshheading:7887891-GTP Cyclohydrolase, pubmed-meshheading:7887891-Gene Expression, pubmed-meshheading:7887891-Guanosine Triphosphate, pubmed-meshheading:7887891-Kinetics, pubmed-meshheading:7887891-Magnesium, pubmed-meshheading:7887891-Molecular Sequence Data, pubmed-meshheading:7887891-Neopterin, pubmed-meshheading:7887891-Operon, pubmed-meshheading:7887891-Phosphorylation, pubmed-meshheading:7887891-Plasmids, pubmed-meshheading:7887891-Potassium, pubmed-meshheading:7887891-Promoter Regions, Genetic, pubmed-meshheading:7887891-Pteridines, pubmed-meshheading:7887891-Recombinant Proteins, pubmed-meshheading:7887891-Uridine Triphosphate
pubmed:year
1995
pubmed:articleTitle
Enzymic characterization of Bacillus subtilis GTP cyclohydrolase I. Evidence for a chemical dephosphorylation of dihydroneopterin triphosphate.
pubmed:affiliation
Biotechnology Section, F. Hoffmann-La Roche Ltd., Basel, Switzerland.
pubmed:publicationType
Journal Article