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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
18
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pubmed:dateCreated |
1992-8-6
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pubmed:databankReference |
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M63381,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M63382,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M63383,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M80912,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M86615,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M86616,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M86617,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M86618,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M86619,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M86620
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pubmed:abstractText |
The primary sequence of maize 2,3-bisphosphoglycerate-independent phosphoglycerate mutase was deduced from cDNAs isolated from maize cDNA libraries by screening with specific antibodies to the cofactor-independent enzyme and from a maize genomic clone. The genomic clone provided the 5'-nucleotide sequence encoding the N-terminal amino acids which could not be obtained from the cDNA. Confirmation that the nucleotide sequence was for the cofactor-independent phosphoglycerate mutase was obtained by sequencing the peptides generated from cyanogen bromide cleavage of the purified protein. This is the first report of the amino acid sequence of a 2,3-bisphosphoglycerate cofactor-independent phosphoglycerate mutase, which consists of 559 amino acids and is twice the molecular size of the mammalian cofactor-dependent enzyme subunit. Analysis of the cofactor-independent phosphoglycerate mutase amino acid sequence revealed no identity with the cofactor-dependent mutase types. Northern blot analysis confirmed this difference since the maize cofactor-independent phosphoglycerate mutase cDNA did not hybridize with mRNA of the cofactor-dependent mutase. The lack of amino acid identity between cofactor-dependent and -independent enzymes is consistent with their different catalytic mechanisms and suggests that both enzymes are unrelated evolutionarily and arose from two independent ancestral genes. However, a constellation of residues which are involved in metal ion binding in various alkaline phosphatases is conserved in the maize cofactor-independent phosphoglycerate mutase, which suggests that the enzyme is a member of the alkaline phosphatase family of enzymes.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
25
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pubmed:volume |
267
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
12797-803
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:1535626-Alkaline Phosphatase,
pubmed-meshheading:1535626-Amino Acid Sequence,
pubmed-meshheading:1535626-Base Sequence,
pubmed-meshheading:1535626-Biological Evolution,
pubmed-meshheading:1535626-Bisphosphoglycerate Mutase,
pubmed-meshheading:1535626-Blotting, Northern,
pubmed-meshheading:1535626-Blotting, Southern,
pubmed-meshheading:1535626-Cloning, Molecular,
pubmed-meshheading:1535626-DNA,
pubmed-meshheading:1535626-Diphosphoglyceric Acids,
pubmed-meshheading:1535626-Gene Library,
pubmed-meshheading:1535626-Molecular Sequence Data,
pubmed-meshheading:1535626-Restriction Mapping,
pubmed-meshheading:1535626-Sequence Alignment,
pubmed-meshheading:1535626-Zea mays
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pubmed:year |
1992
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pubmed:articleTitle |
Cloning and sequencing of a cDNA encoding 2,3-bisphosphoglycerate-independent phosphoglycerate mutase from maize. Possible relationship to the alkaline phosphatase family.
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pubmed:affiliation |
Unitat de Bioquímica, Facultat de Medicina, Universitat de Barcelona, Spain.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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