We are analyzing https://link.springer.com/article/10.1007/bf02115689.

Title:
The mouse muscle creatine kinase cDNA and deduced amino acid sequences: Comparison to evolutionarily related enzymes | Journal of Molecular Evolution
Description:
The nucleotide sequence of cloned DNA corresponding to full-length mouse muscle creatine kinase mRNA has been determined. This 1415 base pair DNA sequence and the deduced 381 amino acid sequence of the protein have been compared to creatine kinase sequences from other vertebrate species and to invertebrate guanidino kinase sequences. These comparisons show that the vertebrate muscle creatine kinases constitute a remarkably conserved protein family with a unit evolutionary period of 30. The creatine kinases also retain marked sequence similarity with the more distantly related invertebrate guanidino kinases. A portion of the sequence, presumably part of the ATP binding site, shows similarity to other nucleotide binding proteins with diverse functions. Comparisons of the untranslated regions of the creatine kinase cDNA sequences show that the 5′ untranslated regions are more highly conserved than are the 3′ untranslated regions; this may point to some regulatory function in the 5′ region.
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Keywords {🔍}

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Topics {✒️}

month download article/chapter muscle-specific creatine kinase acetylcholine receptor-enriched membranes camp-dependent protein kinase predicted nucleotide-binding properties lobster-muscle arginine kinase hormone-activated transmembrane signalling double-digest restriction fragments invertebrate guanidino kinases dideoxy chain-termination method full-length cdna human heart muscle porcine skeletal muscle chicken skeletal muscle creatine kinases mm amino acid sequence complete nucleotide sequence molecular evolution aims creatine kinase sequences full article pdf differentiating mouse myoblasts mitochondrial creatine kinase creatine kinase induction creatine kinase isozymes mm creatine kinase creatine kinase isoenzymes nucleotide binding proteins related subjects cdna clones coding adenosine 5′-triphosphatecreatine phosphotransferase privacy choices/manage cookies homarus vulgaris muscle lumbricus terrestris muscle atp binding site evolutionarily related enzymes protein sequencing estronen-induced protein chimeric protein homologous separate protein families cold spring harbor creatine kinases tissue-specific isozymes chain-terminating inhibitors coding region sequences nucleotide sequence european economic area scope submit manuscript unit evolutionary period check access thiol group reactivity

Schema {🗺️}

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         description:The nucleotide sequence of cloned DNA corresponding to full-length mouse muscle creatine kinase mRNA has been determined. This 1415 base pair DNA sequence and the deduced 381 amino acid sequence of the protein have been compared to creatine kinase sequences from other vertebrate species and to invertebrate guanidino kinase sequences. These comparisons show that the vertebrate muscle creatine kinases constitute a remarkably conserved protein family with a unit evolutionary period of 30. The creatine kinases also retain marked sequence similarity with the more distantly related invertebrate guanidino kinases. A portion of the sequence, presumably part of the ATP binding site, shows similarity to other nucleotide binding proteins with diverse functions. Comparisons of the untranslated regions of the creatine kinase cDNA sequences show that the 5′ untranslated regions are more highly conserved than are the 3′ untranslated regions; this may point to some regulatory function in the 5′ region.
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      headline:The mouse muscle creatine kinase cDNA and deduced amino acid sequences: Comparison to evolutionarily related enzymes
      description:The nucleotide sequence of cloned DNA corresponding to full-length mouse muscle creatine kinase mRNA has been determined. This 1415 base pair DNA sequence and the deduced 381 amino acid sequence of the protein have been compared to creatine kinase sequences from other vertebrate species and to invertebrate guanidino kinase sequences. These comparisons show that the vertebrate muscle creatine kinases constitute a remarkably conserved protein family with a unit evolutionary period of 30. The creatine kinases also retain marked sequence similarity with the more distantly related invertebrate guanidino kinases. A portion of the sequence, presumably part of the ATP binding site, shows similarity to other nucleotide binding proteins with diverse functions. Comparisons of the untranslated regions of the creatine kinase cDNA sequences show that the 5′ untranslated regions are more highly conserved than are the 3′ untranslated regions; this may point to some regulatory function in the 5′ region.
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