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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
5
|
| pubmed:dateCreated |
1990-3-23
|
| pubmed:databankReference | |
| pubmed:abstractText |
A full-length cDNA encoding porcine heart aconitase was derived from lambda gt10 recombinant clones and by amplification of the 5' end of the mRNA. The 2700-base pair (bp) cDNA contains a 29-bp 5' untranslated region, a 2343-bp coding segment, and a 327-bp 3' untranslated region. The porcine heart enzyme is synthesized as a precursor containing a mitochondrial targeting sequence of 27 amino acid residues which is cleaved to yield a mature enzyme of 754 amino acids, Mr = 82,754, having a blocked amino terminus. The NH2-terminal pyroglutamyl residue of the mature enzyme was identified by fast atom bombardment mass spectrometry and sequence analyses of an NH2-terminal peptide. Mature porcine heart aconitase contains 12 cysteine residues. Cysteines 358, 421, and 424 are ligands to the Fe-S cluster in the inactive [3Fe-4S] (Robbins, A. H., and Stout, C. D. (1989) Proteins 5, 289-312) and active [4Fe-4S] (Robbins, A. H., and Stout, C. D. (1989) Proc. Natl. Acad. Sci. U. S. A. 86, 3639-3643) forms. An alignment of the derived porcine heart sequence with 8 cysteine-containing tryptic peptides from bovine heart aconitase (Plant, D. W., and Howard, J. B. (1988) J. Biol. Chem. 263, 8184-8189; Plank, D. W., Kennedy, M. C., Beinert, H., and Howard, J. B. (1989) J. Biol. Chem. 264, 20385-20393) shows that 198 of 202 amino acids are conserved and suggests that the two enzymes are virtually identical.
|
| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Aconitate Hydratase,
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Mitochondrial,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Recombinant,
http://linkedlifedata.com/resource/pubmed/chemical/Oligonucleotide Probes,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Feb
|
| pubmed:issn |
0021-9258
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
15
|
| pubmed:volume |
265
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
2814-21
|
| pubmed:dateRevised |
2007-11-14
|
| pubmed:meshHeading |
pubmed-meshheading:2303429-Aconitate Hydratase,
pubmed-meshheading:2303429-Amino Acid Sequence,
pubmed-meshheading:2303429-Animals,
pubmed-meshheading:2303429-Base Sequence,
pubmed-meshheading:2303429-Binding Sites,
pubmed-meshheading:2303429-Blotting, Northern,
pubmed-meshheading:2303429-Cloning, Molecular,
pubmed-meshheading:2303429-Cysteine,
pubmed-meshheading:2303429-DNA, Mitochondrial,
pubmed-meshheading:2303429-DNA, Recombinant,
pubmed-meshheading:2303429-Gene Amplification,
pubmed-meshheading:2303429-Gene Library,
pubmed-meshheading:2303429-Mitochondria, Heart,
pubmed-meshheading:2303429-Molecular Sequence Data,
pubmed-meshheading:2303429-Oligonucleotide Probes,
pubmed-meshheading:2303429-Peptide Mapping,
pubmed-meshheading:2303429-RNA, Messenger,
pubmed-meshheading:2303429-Restriction Mapping,
pubmed-meshheading:2303429-Swine
|
| pubmed:year |
1990
|
| pubmed:articleTitle |
Cloning and structural characterization of porcine heart aconitase.
|
| pubmed:affiliation |
Department of Biochemistry, Purdue University, West Lafayette, Indiana 47907.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
|