Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.4.24.27 (thermolysin)
 1,894 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The amino acid sequence of the C-terminal domain of the elongation factor G (EF-G) has been studied. The polypeptide chain of the domain consists of 228 amino acid residues, and contains no tryptophan or cysteine residues. To determine its structure, the peptides obtained as a result of the fragment digestion by staphylococcal glutamic protease, cyanogen bromide cleavage, and tryptic hydrolysis of the fragment modified by maleic anhydride have been analyzed, as well as peptides obtained after hydrolyses of cyanogen bromide fragments with chymotrypsin, thermolysin and trypsin.
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PMID:[Primary structure of the elongation factor G from Escherichia coli. V. Amino acid sequence of the C-terminal domain]. 638 96

The amino acid sequence of cysteine- and cystine-containing peptides resulting from cleavage of the G-factor by cyanogen bromide has been determined. For structure analysis cyanogen bromide peptides were further degradated using trypsin, chymotrypsin, thermolysin, staphylococcal glutamic protease, or limited acid hydrolysis. The products of the G-factor cleavage at Asp-Pro bonds were also studied. The obtained data together with those published earlier permitted to establish the complete primary structure of the elongation factor G. The polypeptide chain consists of 701 amino acid residues and has molecular mass of 77321,46.
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PMID:[Primary structure of the elongation factor G from Escherichia coli. IX. Structure of peptides generated by cyanogen bromide cleavage of the G-factor isolated on thiol-activated sepharose and of the products of the G-factor cleavage at Asp-Pro bonds. Complete primary structure]. 638

Class II actins, such as Drosophila and mammalian skeletal muscle actins, have genes that code for a Met-X-Asp NH2 terminus where X is usually cysteine. These actins have an Ac-Asp NH2 terminus so two amino acids must be removed. To determine the nature of this processing, we labeled Drosophila Schneider L-2 cells with [35S]methionine or cysteine, isolated the actin, and analyzed the NH2-terminal actin tryptic peptides and their thermolysin digestion products. After a 4-h labeling period, we detected completed actin polypeptide chains with either an unblocked Asp or an Ac-Asp NH2 terminus. No intermediate with an NH2-terminal Cys or Met could be demonstrated. If, however, Drosophila mRNA was translated in a mRNA-dependent rabbit reticulocyte lysate system, an additional 43-kDa actin intermediate was observed. On the basis of thermolysin digestion studies and experiments using mild acid hydrolysis of a labeled actin NH2-terminal tryptic peptide fragment, we identified this intermediate as having an Ac-Cys-Asp NH2 terminus. In a time-dependent fashion, Ac-Cys was removed generating actin with an exposed NH2-terminal Asp which was subsequently acetylated to produce the mature form of actin. The removal of Met and the acetylation of Cys may occur early in translation while the nascent polypeptide chain is still attached to the ribosome. Subsequent processing occurs following completion of the synthesis of the actin polypeptide. The removal of Ac-Cys from Drosophila actin is thus similar to removal of Ac-Met from the NH2 terminus of class I actins although in the case of the class II actins, it is the second amino acid that is removed as an acetylated species.
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PMID:NH2-terminal processing of Drosophila melanogaster actin. Sequential removal of two amino acids. 641 30

Anti-BPTI-antibody inactivated the antitrypsin activity of basic pancreatic trypsin inhibitor. Esterification of BPTI with methanol did not affect its antitrypsin activity and precipitate formation with antibody. Acetylation, maleylation and hexa-S-carboxylation of BPTI completely inactivated the inhibitor reactivity and markedly diminished its precipitating ability. Performic acid oxidized BPTI and thermolysin digested BPTI lost its antitrypsin as well as antigenic activities. The both preparations as well as oxidized N-acetyl-L-cysteinyl-L-lysyl-L-alanylglycylglycyl-L-cysteine amide did not affect the complex formation between the inhibitor and antibody.
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PMID:Effect of some chemical modifications of basic pancreatic trypsin inhibitor (BPTI) on its reaction with specific antibody. 647 63

The complete primary structures of the two main forms, PRP-IV and PRP-V, of a proline-rich polypeptide bound in vivo to rat prostatic binding protein has been determined. Their sequences were established using manual Edman degradation of the native polypeptide and of purified fragments derived from trypsin and thermolysin digestions. Both polypeptides contain 38 amino acid residues (Mr = 4397 and 4339); cysteine, methionine, and serine are missing. In spite of the high proline content (21%), no polyproline stretches were detected. PRP-IV and PRP-V show an extensive structural homology and differ only by three substitutions. These amino acid replacements are located in the NH2-terminal part of the molecule at positions 6 (His leads to Pro), 10 (Pro leads to His), and 11 (Asp leads to Gly). Moreover, each component displays a microheterogeneity at several positions in the sequence which indicates that multiple structural variants exist for PRP-IV and PRP-V. These data not only suggest the existence in rat ventral prostate of a multigene family coding for the proline-rich polypeptides but also the occurrence of a pronounced genetic polymorphism for these components. In addition, a remarkable sequence homology is observed between the PRP components and the region of the B chain in the precursor of mouse renin.
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PMID:Proline-rich polypeptides bound to rat prostatic binding protein. The primary structure of the two main components, proline-rich polypeptides IV and V. 668 33

An isoactin analysis was performed on L-[35S]cysteine labeled BC3H1 cells to determine if these smooth muscle-like cells synthesize vascular smooth muscle actin. Three different NH2-terminal peptides were identified on thin layer electrophoretograms of DNase I-purified and trypsin-digested BC3H1 cell actin. Results obtained from secondary digestion with thermolysin or Staphylococcus aureus V8 protease showed that the most acidic NH2-terminal peptide was derived from vascular smooth muscle alpha-isoactin. Treatment of cell monolayers with serum-free medium caused a 3-fold increase in the level of alpha-isoactin expression and a concomitant decrease in the level of non-muscle beta- and gamma-isoactin. Cell-cell contact was required for induction of alpha-isoactin, and the effects of serum depletion on isoactin expression and cell growth were reversible. The intensity of about 11 out of 500 polypeptide spots on two-dimensional gels of BC3H1 cell polypeptides also was influenced by the culture conditions. The finding that smooth muscle isoactin expression was coupled to cell growth conditions indicate the potential usefulness of BC3H1 cells in studies of isoactin expression and utilization during vascular smooth muscle development.
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PMID:Induction of vascular smooth muscle alpha-isoactin expression in BC3H1 cells. 669 10

The complete amino acid sequence of a lectin from sainfoin ( Onobrychis viciifolia Scop . var. Eski ) has been determined by sequential Edman analyses of the intact protein and peptides derived from digests with trypsin and thermolysin. Peptides were purified by pH fractionation, by gel filtration, and by cation-exchange and reverse-phase high-performance liquid chromatography. Seven segments of continuous sequence, accounting for the entire protein, were aligned through sequence comparison with several homologous leguminous lectins to give the final structure. Sainfoin lectin monomer, a glycoprotein which contains a single polypeptide chain of 236 amino acid residues with a molecular weight of 26 509, has amino- and carboxyl-terminal residues of alanine and threonine, respectively. A single residue of cysteine, located at position 33, is the only sulfur-containing amino acid present. Asparagine-118 is the single oligosaccharide attachment site. At least two apparent allelomorphic forms of the protein, having valine or isoleucine at position 49 in equal amounts, were detected. The amino acid sequence of sainfoin lectin exhibits circular permutation relative to that of the homologous protein concanavalin A.
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PMID:Lectin from sainfoin (Onobrychis viciifolia scop.). Complete amino acid sequence. 672 25

A fully translated actin biosynthetic intermediate containing N-acetylcysteine at the NH2 terminus has been identified in homogenates of differentiated mouse BC3H1 cerebrovascular smooth muscle cells labeled with L-[35S]cysteine. Thermolysin digestion of the highly acidic NH2-terminal tryptic peptide of this intermediate and electrophoretic analysis of the resulting fragments indicated that the intermediate was a precursor of smooth muscle alpha- isoactin , the major isoactin species in vascular smooth muscle. Carboxypeptidase A digestion of the thermolysin cleavage product corresponding to the first eight amino acid residues of the NH2-terminal tryptic peptide demonstrated an acetylcysteine-glutamate residue at the NH2 terminus. These results imply that the gene for smooth muscle alpha- isoactin , like genes coding for skeletal and cardiac alpha- isoactins , contains a cysteine codon immediately following the initiator methionine codon. Both the methionine and cysteine residues must be removed from the NH2 terminus of the intermediate to yield the mature form of smooth muscle alpha- isoactin . The removal of the cysteine residue in vivo is not direct but apparently involves acetylation of the cysteine and subsequent post-translational cleavage of the resulting acetylcysteine. Such an acetylation-dependent pathway has been demonstrated for removal of cysteine from the NH2 terminus of Drosophila actin synthesized in a cell-free translation system ( Rubenstein , P. A., and Martin, D. J. (1983) J. Biol. Chem. 258, 11354-11360). In vivo pulse-chase experiments indicate that the smooth muscle alpha- isoactin intermediate in BC3H1 cells turns over much more slowly than nonmuscle actin intermediates previously identified in mouse L-cells.
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PMID:A vascular smooth muscle alpha-isoactin biosynthetic intermediate in BC3H1 cells. Identification of acetylcysteine at the NH2 terminus. 672 86

The 22076-Mr Zn2+-containing D-alanyl-D-alanine-cleaving carboxypeptidase of Streptomyces abuls G effectively catalyses the transfer of the N alpha, N epsilon-diacetyl-L-lysyl-D-alanyl electrophilic group of the standard tripeptide substrate N alpha, N epsilon-diacetyl-L-lysyl-D-alanyl-D-alanine to water. It also performs a weak beta-lactamase activity, hydrolysing penicillin into penicilloate at a very low rate. This protein consists of 212 amino acid residues in a single polypeptide chain. The N terminus is partially blocked as a result of the cyclization of the dipeptide Asn-Gly into anhydroaspartylglycine imide. The protein has been fragmented by cyanogen bromide into five fragments whose sequences have been determined via appropriate subcleavages with various proteases. The ordering of the cyanogen bromide peptide fragments has been carried out (a) by submitting the S-carboxymethylated protein to complete tryptic digestion and labelling the methionine-containing peptides thus obtained with iodo[14C]-acetamide, and (b) by submitting to limited tryptic digestion the S-[2-(4'-pyridyl)ethyl]-cysteine protein whose amino groups have been blocked by reaction with exo-cis-3,6-endoxo-delta 4-tetrahydrophthalic anhydride prior to digestion. The protein contains six cysteine residues in the form of three disulfide bridges. No homology is found by comparing this peptidase with other Zn2+-containing enzymes (carboxypeptidase A, thermolysin, carbonic anhydrase B and alcohol dehydrogenase) and several completely or partially sequenced, serine-containing D-alanyl-D-alanine-cleaving peptidases and Zn2+/serine-containing beta-lactamases.
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PMID:The complete amino acid sequence of the Zn2+-containing D-alanyl-D-alanine-cleaving carboxypeptidase of streptomyces albus G. 682 89

The amino acid sequence of the glycosylated component C3 of rat prostatic binding protein has been determined. The peptides obtained by digestion of the S-carboxamidomethylated or S-aminoethylated glycoprotein with trypsin and Staphylococcus aureus protease were sequenced by manual Edman degradation. The alignment of the fragments was further established with overlapping peptides obtained by enzymic hydrolysis of the modified protein with chymotrypsin and thermolysin, and by chemical cleavage with cyanogen bromide. The glycopeptide C3 contains 77 amino acids corresponding to a molecular weight of 8653. the oligosaccharide chain is attached to the peptide by an N-glycosidic bond to asparagine-17. C3 is an acidic polypeptide due to the presence of ten acidic residues; its three cysteine residues are located at both extremities and in the middle of the molecule.
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PMID:Structural studies on rat prostatic binding protein. The primary structure of its glycosylated component C3. 701 18


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