Literature DB >> 20932835

A novel secreted metzincin metalloproteinase from Bacillus intermedius.

Albina R Sabirova1, Natalya L Rudakova, Nelly P Balaban, Olga N Ilyinskaya, Ilya V Demidyuk, Sergey V Kostrov, Galina N Rudenskaya, Margarita R Sharipova.   

Abstract

The mprBi gene from Bacillus intermedius 3-19 encoding a novel secreted metalloproteinase was identified. The mpriBi gene was expressed in an extracellular proteinase-deficient Bacillus subtilis BG 2036 strain and the corresponding protein was characterized biochemically. The 19 kDa MprBi protein was purified to homogeneity and sequenced by mass spectroscopy and Edman degradation methods. Amino acid sequence analysis of MprBi identified an active site motif HEYGHNFGLPHD and a conserved structural component Met-turn, both of which are unique features of the metzincin clan. Furthermore, MprBi harbors a number of distinct sequence elements characteristic of proteinase domains in eukaryotic adamalysins. We conclude that MprBi and similar proteins from other Bacillus species form a novel group of metzincin metalloproteinases in prokaryotes.
Copyright © 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

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Year:  2010        PMID: 20932835     DOI: 10.1016/j.febslet.2010.09.049

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  7 in total

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Journal:  Polymers (Basel)       Date:  2018-09-19       Impact factor: 4.329

5.  Novel Immobilized Biocatalysts Based on Cysteine Proteases Bound to 2-(4-Acetamido-2-sulfanilamide) Chitosan and Research on Their Structural Features.

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6.  Biochemical Properties and Anti-Biofilm Activity of Chitosan-Immobilized Papain.

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Journal:  Mar Drugs       Date:  2021-03-31       Impact factor: 5.118

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  7 in total

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