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 488 nm line of the CW argon ion laser provides a convenient visible source for the direct excitation of the emissive 5D4 state of the Tb(III) ion. Room temperature emission spectra of Tb(III) in a variety of environments have been examined under relatively high resolution. The samples studied include structurally well-characterized crystalline solids, model chelate complexes in solution and Tb(III) bound to the enzyme thermolysin and the protein parvalbumin. The fine structure in the emissions is caused by ligand field splittings of both ground and excited state J manifolds. These spectra provide signatures sensitive to the immediate coordination environment of the Tb(III) ion. Solid state/solution state structural comparisons are made. The emission fine structure reveal differences between the EF side calcium-binding sites of parvalbumin and the calcium site 1 of thermolysin.
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PMID:Lanthanide ion probes of structure in biology. Environmentally sensitive fine structure in laser-induced terbium(III) luminescence. 45 62

The amino acid sequence of the parvalbumin II of the pike is reported. The protein has a molecular weight of 11 435. It consists of a single polypeptide chain of 107 amino acid residues with an acetyl group blocking the N-terminus and an alanine residue at the C-terminus. The molecule has been enzymically cleaved by trypsin, thermolysin and by the protease of the Staphylococcus aureus strain V8. Chemical cleavages make use of the CNBr reaction and of the sulfocyanoethylation method. The comparison of this amino acid sequence with that of the parvalbumin III of the pike indicates that these two homologous proteins belong respectively to two different subgroups derived from an early gene duplication of an ancestral gene at least prior to the differentiation of the Osteichthyes.
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PMID:The primary structure of the parvalbumin II of pike (Esox lucius). 100 32

The synthetic tetrapeptide acetyl-aspartyl-valyl-aspartyl-alanine (Ac-DVDA) is a model of the calcium binding site of proteins such as carp parvalbumin, thermolysin and calmodulin. 1H n.m.r. spectra of the tetrapeptide are presented and assigned for D2O and DMSO solutions to determine the conformational mobility. The resonance of the two aspartyl side chains could be completely analysed and the vicinal coupling (C alpha H-C beta H and NH-C alpha H) indicated that the free peptide has considerable conformational mobility. The Ca(II) complex generates a different 1H n.m.r. spectrum for the aspartyl resonances at neutral pH. The solution conformation of Pr(III) complex of Ac-DVDA has been investigated using induced chemical shifts. The observed trends in the magnitude of the shift ratios and the rotamer population suggest that the metal ion binds predominantly to both carboxylates of two aspartyl residues in a bidentate fashion. We discuss the consistency of the differentiated spectra for aspartyl residues in the complex with the stepwise binding of Ca2+ to the carrier.
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PMID:Calcium and praseodymium complexes in solution. 1H n.m.r. conformational study of the model tetrapeptide acetyl-aspartyl-valyl-aspartyl-alanine. 405 28

The primary structure of the most basic (pI = 4.88) of the two major parvalbumins from frog skeletal muscle (Rana esculenta) has been determined by partial automatic sequencing of the protein which exhibits a free N terminus, and a study of overlapping peptides obtained by cyanogen bromide cleavage and digestion with trypsin, thermolysin and Armillaria mellea protease. This protein shows the typical structure of an alpha-parvalbumin. Comparison of the primary structure of ion-binding loops of alpha and beta-parvalbumins does not provide a clear-cut explanation of their differences in ion-binding properties.
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PMID:Amino-acid sequence of an alpha-parvalbumin, pI = 4.88, from frog skeletal muscle. 704 41