Nucleotide sequence of the neutral protease gene from Bacillus subtilis var. amylosacchariticus

Yoshimoto, Tadashi; Oyama, Hiroshi; Takeshita, Tomoaki; Higashi, Hideaki; Xu, Sheng-lin; Tsuru, Daisuke

doi:10.1016/0922-338x(90)90080-g

Cited by 7 publications

(4 citation statements)

References 28 publications

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“…Yoshimoto et al characterized the gene encoding subtilisin amylosacchariticus from B. subtilis subsp. amylosacchariticus (327,328). The sequence was highly homologous to that of subtilisin E from B. subtilis 168 (269).…”

Section: Bacteriamentioning

confidence: 96%

Molecular and Biotechnological Aspects of Microbial Proteases

Rao

Tanksale

Ghatge

et al. 1998

Microbiol Mol Biol Rev

1,766

721

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SUMMARY Proteases represent the class of enzymes which occupy a pivotal position with respect to their physiological roles as well as their commercial applications. They perform both degradative and synthetic functions. Since they are physiologically necessary for living organisms, proteases occur ubiquitously in a wide diversity of sources such as plants, animals, and microorganisms. Microbes are an attractive source of proteases owing to the limited space required for their cultivation and their ready susceptibility to genetic manipulation. Proteases are divided into exo- and endopeptidases based on their action at or away from the termini, respectively. They are also classified as serine proteases, aspartic proteases, cysteine proteases, and metalloproteases depending on the nature of the functional group at the active site. Proteases play a critical role in many physiological and pathophysiological processes. Based on their classification, four different types of catalytic mechanisms are operative. Proteases find extensive applications in the food and dairy industries. Alkaline proteases hold a great potential for application in the detergent and leather industries due to the increasing trend to develop environmentally friendly technologies. There is a renaissance of interest in using proteolytic enzymes as targets for developing therapeutic agents. Protease genes from several bacteria, fungi, and viruses have been cloned and sequenced with the prime aims of (i) overproduction of the enzyme by gene amplification, (ii) delineation of the role of the enzyme in pathogenecity, and (iii) alteration in enzyme properties to suit its commercial application. Protein engineering techniques have been exploited to obtain proteases which show unique specificity and/or enhanced stability at high temperature or pH or in the presence of detergents and to understand the structure-function relationships of the enzyme. Protein sequences of acidic, alkaline, and neutral proteases from diverse origins have been analyzed with the aim of studying their evolutionary relationships. Despite the extensive research on several aspects of proteases, there is a paucity of knowledge about the roles that govern the diverse specificity of these enzymes. Deciphering these secrets would enable us to exploit proteases for their applications in biotechnology.

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Section: Bacteriamentioning

confidence: 96%

Molecular and Biotechnological Aspects of Microbial Proteases

Rao

Tanksale

Ghatge

et al. 1998

Microbiol Mol Biol Rev

1,766

721

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“…1 -4) Recently, its amino acid sequence 5 ) and .the nucleotide sequence of the enzyme gene 6 ) were analyzed in our laboratory. Comparison of the amino acid sequence with those of other Bacillus neutral proteases showed that the B. amylosacchariticus enzyme is 89% homologous to that from B. amyloliquefaciens and 48% homologous to thermolysin, a thermostable Zn-containing endopeptidase from B. thermoproteolyticus.…”

Section: Bacillus Subtilis Var Amylosacchariticus (Bmentioning

confidence: 99%

Dye-sensitized Photooxidation of Neutral Protease fromBacillus subtilisvar.amylosacchariticus: Assignment of Histidine Residue Oxidized

Morikawa

Kanatani

Yoshimoto

et al. 1991

Agricultural and Biological Chemistry

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“…1 ,2) Recently, the primary structure of the neutral protease was established in our laboratory by both protein sequencing 3 ) and nucleotide sequencing of the gene. 4 ) The enzyme was found to have a high homology to thermolysin, a thermostable neutral metalloprotease from B. thermoproteolyticus. 5 ) changes of the enzyme.…”

mentioning

confidence: 99%

“…This tyrosyl residue was also conserved in the B. amylosacchariticus neutral protease, corresponding to Tyr-158, 3,4) which 'was nitrated with TNM, with activity * To whom correspondence should be addressed.…”

mentioning

confidence: 99%