Isolation and sequence analysis of the gene for arginine kinase from the chelicerate arthropod, Limulus polyphemus: insights into catalytically important residues
| Autor: | S J Strong, W.R. Ellington |
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| Rok vydání: | 1995 |
| Předmět: |
Untranslated region
DNA Complementary Sequence analysis Molecular Sequence Data Biophysics Biology Biochemistry Catalysis Structural Biology Complementary DNA Horseshoe Crabs Animals Amino Acid Sequence Cloning Molecular Molecular Biology Gene Peptide sequence Binding Sites Base Sequence Arginine Kinase Arginine kinase biology.organism_classification Molecular biology Open reading frame Limulus biology.protein |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1246:197-200 |
| ISSN: | 0167-4838 |
| Popis: | The gene for arginine kinase (AK; EC 2.7.3.3) from the horseshoe crab, Limulus polyphemus, was cloned and the complete cDNA sequence was determined. An open reading frame with 1071 nucleotides was detected that encodes a 357 amino-acid protein with a calculated M(r) of 40,238. The coding transcript is flanked by 13 and 512 nucleotides of 5' and 3' untranslated regions, respectively. The deduced amino-acid sequence of Limulus AK displays extensive similarity to other arginine kinases, vertebrate and invertebrate creatine kinases (CK) and a glycocyamine kinase (GK). Consensus AK and consensus CK sequences, as well as a GK sequence, were compared to CK peptide regions containing residues presumed to be important in catalysis and/or located in close proximity to the active site. Our comparisons revealed some inconsistencies with hypothesized roles of particular residues in catalytic function. |
| Databáze: | OpenAIRE |
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