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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
11
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pubmed:dateCreated |
1992-4-3
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pubmed:databankReference |
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pubmed:abstractText |
The sequence of the gene coding for GTP cyclohydrolase I of Escherichia coli and of the adjacent regions was determined. The open reading frame contains 669 nucleotides. The deduced amino-acid sequence represents a protein consisting of 223 amino-acid residues with a molecular mass of 24,873 Da. Partial amino-acid sequences of the N-terminal region and of 5 peptides obtained by trypsin and BrCN cleavage were determined by Edman degradation and were in full agreement with the sequence deduced from the nucleotide sequence. The starting methionine is removed by posttranslational modification. The protein shows extensive homology to the recently reported GTP cyclohydrolase from rats.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0177-3593
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
372
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
991-7
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:1665332-Amino Acid Sequence,
pubmed-meshheading:1665332-Base Sequence,
pubmed-meshheading:1665332-Cyanogen Bromide,
pubmed-meshheading:1665332-DNA, Bacterial,
pubmed-meshheading:1665332-DNA Restriction Enzymes,
pubmed-meshheading:1665332-Escherichia coli,
pubmed-meshheading:1665332-GTP Cyclohydrolase,
pubmed-meshheading:1665332-Hydrolysis,
pubmed-meshheading:1665332-Molecular Sequence Data,
pubmed-meshheading:1665332-Molecular Weight,
pubmed-meshheading:1665332-Plasmids,
pubmed-meshheading:1665332-Sequence Homology, Nucleic Acid,
pubmed-meshheading:1665332-Tetrahydrofolates,
pubmed-meshheading:1665332-Transformation, Bacterial,
pubmed-meshheading:1665332-Trypsin
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pubmed:year |
1991
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pubmed:articleTitle |
Biosynthesis of tetrahydrofolate. Sequence of GTP cyclohydrolase I from Escherichia coli.
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pubmed:affiliation |
Lehrstuhl für Organische Chemie und Biochemie, Technische Universität München.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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