Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P01185 (vasopressin)
 23,126 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A second extracellular protease from myxobacter strain AL-1 has been purified to homogeneity and named protease II; the enzyme crystallizes as fine needles. The extracellular, cell wall lytic protease reported previously from the same organism is now designated protease I. Protease II exhibits a pH optimum of 8.5 to 9.0 and is stable from pH 3.0 to 9.0. The enzyme is heat stable at 50 C for 18 hr. Results of sedimentation equilibrium studies yielded a molecular weight of 17,000, and amino acid analysis revealed 157 residues with a minimal molecular weight of 16,660. Cleavage of peptide bonds in the oxidized B-chain of insulin, cytochrome c (horse heart). lysozyme, and vasopressin is restricted to the amino side of lysine. Dilysine and trilysine were not hydrolyzed. Products from digestions of polylysine were lysine and dilysine.
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PMID:Myxobacter AL-1 protease II: specific peptide bond cleavage on the amino side of lysine. 434 25

The unique specificity of Achromobacter protease I for lysine residue was investigated using synthetic and natural substrates, i.e., lysine derivatives, arginine derivatives, lysine vasopressin, substance P, ACTH and insulin. The enzyme cleaved only the -Lys-X- bonds in the above substrates. The binding affinity of alkylamines as determined by Ki was much stronger than that of the corresponding alkylguanidines.
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PMID:Studies on a new proteolytic enzyme from Achromobacter lyticus M497-1. II. specificity and inhibition studies of Achromobacter protease I. 616 93