Studies on adenosine triphosphate transphosphorylases. Amino acid sequence of rabbit muscle ATP-AMP transphosphorylase

Abstract

The total amino acid sequence of rabbit muscle adenylate kinase has been determined, and the single polypeptide chain of 194 amino acid residues starts with N-acetylmethionine and ends with leucyllysine at its carboxyl terminus, in agreement with the earlier data on its amino acid composition [Mahowald, T. A., Noltmann, E. A., & Kuby, S. A. (1962) J. Biol. Chem. 237, 1138-1145] and its carboxyl-terminus sequence [Olson, O. E., & Kuby, S. A. (1964) J. Biol. Chem. 239, 460-467]. Elucidation of the primary structure was based on tryptic and chymotryptic cleavages of the performic acid oxidized protein, cyanogen bromide cleavages of the 14C-labeled S-carboxymethylated protein at its five methionine sites (followed by maleylation of peptide fragments), and tryptic cleavages at its 12 arginine sites of the maleylated 14C-labeled S-carboxymethylated protein. Calf muscle myokinase, whose sequence has also been established, differs primarily from the rabbit muscle myokinase's sequence in the following: His-30 is replaced by Gln-30; Lys-56 is replaced by Met-56; Ala-84 and Asp 85 are replaced by Val-84 and Asn-85. A comparison of the four muscle-type adenylate kinases, whose covalent structures have now been determined, viz., rabbit, calf, porcine, and human [for the latter two sequences see Heil, A., Müller, G., Noda, L., Pinder, T., Schirmer, H., Schirmer, I., & Von Zabern, I. (1974) Eur. J. Biochem. 43, 131-144, and Von Zabern, I., Wittmann-Liebold, B., Untucht-Grau, R., Schirmer, R. H., & Pai, E. F. (1976) Eur. J. Biochem. 68, 281-290], demonstrates an extraordinary degree of homology.(ABSTRACT TRUNCATED AT 250 WORDS)

Analysis of the Bovine Herpesvirus Type 1 Thymidine Kinase (TK) Gene from Wild-type Virus and TK-deficient Mutants

“…There were five regions of strong homology which were arbitrarily numbered I to V for the purpose of this study. Region I has been reported to have homology with the proposed nucleotide-binding sites of other herpesvirus TKs (Otsuka & Kit, 1984;Gentry, 1985), other TKs and other enzymes as diverse as adenylate kinase (Kuby et al, 1984) and myosin (Walker et al, 1982). Moreover, recently it has been shown by means of sitedirected mutagenesis that the five highly conserved amino acids GXXGXGKT (where X represents various amino acids), which occur at residues 56 to 63 of the HSV-1 TK polypeptide, are essential for enzyme function and appear to be involved in the substrate-binding domains of the enzyme (Liu & Summers, 1988).…”

“…Moreover, recently it has been shown by means of sitedirected mutagenesis that the five highly conserved amino acids GXXGXGKT (where X represents various amino acids), which occur at residues 56 to 63 of the HSV-1 TK polypeptide, are essential for enzyme function and appear to be involved in the substrate-binding domains of the enzyme (Liu & Summers, 1988). The regions II and IV have a high degree of conservation among different herpesvirus TKs but similar sequences were not seen in poxvirus or mammalian TKs or adenylate kinases (Boyle et al, 1987 ;Bradshaw & Deininger, 1984;Kwoh & Engler, 1984;Lewis, 1986;Lin et al, 1985;Kuby et al, 1984). The functional roles of these two regions and of regions 'a' and 'b' of the polypeptide are still unknown.…”

Site‐directed mutagenesis and steady‐state kinetic analysis of mutant enzymes of human adenylate kinase

“…Detailed functional analysis of the C-terminal domain of human adenylate kinase has not been reported. Val182, V186, and Leu193 residues are conserved in mammalian species (21). We selected these three residues to elucidate the function of the C-terminal domain on the left side of the AK model (Fig.…”

Ancient divergence of long and short isoforms of adenylate kinase molecular evolution of the nucleoside monophosphate kinase family

“…A sharp (#) points to the divergence of the eukaryotic three kingdoms in the AK2 subgroup. The sequences used in the tree construction are AKls from human [33], pig [34], rabbit [35], bovine [35], chicken [36] and carp [37], NK (AK homolog, substrate unknown) from Schistosoma [38], UMP-CMP kinases from pig [39] and slime mold [16], uridylate kinase from S. cerevisiae [40], AK2s from bovine [41] and rat [42], AKs from C. elegans [43], S. pombe [27], S. cerevisiae [13], rice [44], Trichomonas [31], AK3s from human [45], bovine [46], rat [42] and S. cerevisiae [47], prokaryotic AKs from Bordetella [48], Haemophilus [49], Salmonella [50], E. coil [51], Lactococcus [24], B. stearothermophilus [52], B. subtilis [23], Paracoccus [53], Mycoplasma [54] and Micrococcus [15], protozoan AK from Giardia [14], chloroplast AK from maize [12] and GKs from pig [55], S. cerevisiae [56] and E. coil [57]. sertion or deletion of 20-30 amino acid residues in homologous proteins reflects the more distant evolutionary relationship than do amino acid replacements.…”