Interactions of Streptomyces serine-protease inhibitors with Streptomyces griseus metalloendopeptidase II.

  title={Interactions of Streptomyces serine-protease inhibitors with Streptomyces griseus metalloendopeptidase II.},
  author={K. Kajiwara and A. Fujita and H. Tsuyuki and T. Kumazaki and S. Ishii},
  journal={Journal of biochemistry},
  volume={110 3},
Streptomyces griseus metalloendopeptidase II (SGMPII) was shown to form tight complexes with several Streptomyces protein inhibitors which had been believed to be specific to serine proteases, such as Streptomyces subtilisin inhibitor (SSI), plasminostreptin (PS), and alkaline protease inhibitor-2c' (API-2c'), as well as with Streptomyces metalloprotease inhibitor (SMPI). The dissociation constants of complexes between SGMPII and these inhibitors were successfully determined by using a novel… Expand
Primary structure of Streptomyces griseus metalloendopeptidase II.
Based on the sequence comparison of SGMPII and other bacterial metalloproteases, the structural basis for the differences in substrate specificity and stability between SGMP II and other thermolysin-like proteases is discussed. Expand
Resynthesis of reactive site peptide bond and temporary inhibition of Streptomyces metalloproteinase inhibitor.
The native inhibitor was resynthesized from the modified inhibitor by incubation with a catalytic amount of thermolysin under the same conditions as used for hydrolysis, suggesting that SMPI follows the standard mechanism of inhibition of serine proteinase inhibitors. Expand
Extracellular metalloendopeptidase of Streptomyces rimosus
Determination of amino acid sequence of the enzyme’s NH2-part allowed the recognition of its structure homology with isolated and predicted metallopeptidases from several Streptomyces species, contributing to the definition of M7 family of metalloendopeptids in streptomycetes. Expand
Transglutaminase from Streptomyces mobaraensis is activated by an endogenous metalloprotease.
It was clearly shown that the peptide bond between Phe(-4) and Ser(-5) was hydrolyzed, indicating that at least one additional peptidase is necessary to complete TGase processing, even if TAMEP cleavage was sufficient to obtain total activity. Expand
Biochemical characterization of a novel metalloendopeptidase from Streptomyces aureofaciens TH-3 with post-proline hydrolysis activity
Abstract Streptomyces aureofaciens TH-3 secretes a protease termed ‘kibilysin’, for which we showed unique substrate specificity and preference for Tyr, Pro, and Leu at the P 1 position usingExpand
Molecular characterization of a gene encoding extracellular serine protease isolated from a subtilisin inhibitor-deficient mutant of Streptomyces albogriseolus S-3253
An extracellular serine protease produced by a mutant derived from Streptomyces albogriseolus S-3253 that no longer produces a protease inhibitor was isolated and a purified protein was designated SAM-P20, which produced E. coli cells that were shown to be sensitive to SSI inhibition. Expand
The N‐terminal peptide of the transglutaminase‐activating metalloprotease inhibitor from Streptomyces mobaraensis accommodates both inhibition and glutamine cross‐linking sites
SSTI was modified by distinct point mutations as well as elongation or truncation of the N‐terminal peptide by six and three residues respectively, and enzymatic biotinylation revealed that an adjacent glutamine pair, upstream from Leu40‐Tyr41 in the SSTI precursor protein, is the preferred binding site of MTG. Expand
Legumain: asparaginyl endopeptidase.
  • S. Ishii
  • Chemistry, Medicine
  • Methods in enzymology
  • 1994
The inhibition profile of jack bean legumain suggests that the enzyme is a cysteine-type endopeptidase, and the presence of the DNP group with absorption near 370 nm allows easy monitoring of separation between an enzymatic reaction product, DNP-Pro-Glu-Ala-Asn, and either of the substrates by high-performance liquid chromatography (HPLC). Expand
Bacterial extracellular zinc-containing metalloproteases
Extracellular zinc-containing metalloproteases are widely distributed in the bacterial world. The most extensively studied are those which are associated with pathogenic bacteria or bacteria whichExpand
Bacterial extracellular zinc-containing metalloproteases.
Further studies of this broad family of metalloproteases will provide important additional insights into the pathogenesis and structure-function relationships of enzymes and will lead to the development of products, including "designer proteins," which might be industrially and/or therapeutically useful. Expand