Biomaterial Database

A new substrate and two inhibitors applicable for thermitase, subtilisin BPN' and alpha-chymotrypsin. Comparison of kinetic parameters with customary substrates and inhibitors. 1985

D Brömme, and S Fittkau

A new chromogenic substrate and two inhibitors with the common peptide sequence X-Ala-Ala-Phe-Y have been synthesized, and were found to be of higher efficiency as hitherto available customary substrates and inhibitors for thermitase, subtilisin BPN' and alpha-chymotrypsin. The proteolytic coefficient kcat/Km for the hydrolysis of the substrate Suc-Ala-Ala-Phe-pNA is about 80 times higher in the case of thermitase and subtilisin BPN' and about 20 times higher for alpha-chymotrypsin compared with Suc-Ala3-pNA and Suc-Phe-pNA, respectively. The irreversible inhibitory effect of Z-Ala2-Phe-CH2Cl compared with Z-Phe-CH2Cl is 280 times greater for thermitase and subtilisin BPN' and 50 times for alpha-chymotrypsin. The corresponding methyl ketone Z-Ala2-Phe-CH3 is a high affinity competitive inhibitor for thermitase but not for the two other enzymes.

UI	MeSH Term	Description	Entries
D007700	Kinetics	The rate dynamics in chemical or physical systems.
D009842	Oligopeptides	Peptides composed of between two and twelve amino acids.	Oligopeptide
D010450	Endopeptidases	A subclass of PEPTIDE HYDROLASES that catalyze the internal cleavage of PEPTIDES or PROTEINS.	Endopeptidase,Peptide Peptidohydrolases
D011480	Protease Inhibitors	Compounds which inhibit or antagonize biosynthesis or actions of proteases (ENDOPEPTIDASES).	Antiprotease,Endopeptidase Inhibitor,Endopeptidase Inhibitors,Peptidase Inhibitor,Peptidase Inhibitors,Peptide Hydrolase Inhibitor,Peptide Hydrolase Inhibitors,Peptide Peptidohydrolase Inhibitor,Peptide Peptidohydrolase Inhibitors,Protease Antagonist,Protease Antagonists,Antiproteases,Protease Inhibitor,Antagonist, Protease,Antagonists, Protease,Hydrolase Inhibitor, Peptide,Hydrolase Inhibitors, Peptide,Inhibitor, Endopeptidase,Inhibitor, Peptidase,Inhibitor, Peptide Hydrolase,Inhibitor, Peptide Peptidohydrolase,Inhibitor, Protease,Inhibitors, Endopeptidase,Inhibitors, Peptidase,Inhibitors, Peptide Hydrolase,Inhibitors, Peptide Peptidohydrolase,Inhibitors, Protease,Peptidohydrolase Inhibitor, Peptide,Peptidohydrolase Inhibitors, Peptide
D002863	Chromogenic Compounds	Colorless, endogenous or exogenous pigment precursors that may be transformed by biological mechanisms into colored compounds; used in biochemical assays and in diagnosis as indicators, especially in the form of enzyme substrates. Synonym: chromogens (not to be confused with pigment-synthesizing bacteria also called chromogens).	Chromogenic Compound,Chromogenic Substrate,Chromogenic Substrates,Compound, Chromogenic,Compounds, Chromogenic,Substrate, Chromogenic,Substrates, Chromogenic
D002918	Chymotrypsin	A serine endopeptidase secreted by the pancreas as its zymogen, CHYMOTRYPSINOGEN and carried in the pancreatic juice to the duodenum where it is activated by TRYPSIN. It selectively cleaves aromatic amino acids on the carboxyl side.	Alpha-Chymotrypsin Choay,Alphacutanée,Avazyme
D000590	Amino Acid Chloromethyl Ketones	Inhibitors of SERINE ENDOPEPTIDASES and sulfhydryl group-containing enzymes. They act as alkylating agents and are known to interfere in the translation process.	Peptide Chloromethyl Ketones,Chloromethyl Ketones, Peptide,Ketones, Peptide Chloromethyl
D000595	Amino Acid Sequence	The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.	Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D001665	Binding Sites	The parts of a macromolecule that directly participate in its specific combination with another molecule.	Combining Site,Binding Site,Combining Sites,Site, Binding,Site, Combining,Sites, Binding,Sites, Combining
D001667	Binding, Competitive	The interaction of two or more substrates or ligands with the same binding site. The displacement of one by the other is used in quantitative and selective affinity measurements.	Competitive Binding