1993
DOI: 10.1016/0167-4838(93)90176-r
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Purification, characterization and molecular cloning of an acidic amino acid-specific proteinase from Streptomyces fradiae ATCC 14544

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Cited by 35 publications
(24 citation statements)
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“…We have reported on an acidic-amino-acid-specific proteinase from S. frudiae [14]. We were successful in expressing its proteinase and are now working on its crystallization with the aim of correlating the three-dimensional structure of proteinases with their recognition of acidic amino acids.…”
Section: Crystallization and Preliminary Crystallographic Studymentioning
confidence: 99%
See 1 more Smart Citation
“…We have reported on an acidic-amino-acid-specific proteinase from S. frudiae [14]. We were successful in expressing its proteinase and are now working on its crystallization with the aim of correlating the three-dimensional structure of proteinases with their recognition of acidic amino acids.…”
Section: Crystallization and Preliminary Crystallographic Studymentioning
confidence: 99%
“…1). As the result, an acidic-amino-acid-specific proteinase [14] was eluted with 0.05 M NaCl in 10 mM sodium acetate pH 5.25; SFase-2 was obtained next with about 0.075 M NaCl in the same buffer. As a final step, the fraction containing trypsin-like proteinase activity was found with the eluate of 1.0 M NaCl.…”
Section: Purification Of Sfase-2mentioning
confidence: 99%
“…However, a glutamic acid residue is not present in the Mpr propeptide cleavage site, suggesting that it is not autoprocessed. Many glutamic-acidspecific proteases such as V8 protease (5) and SPase (43) have been found in Staphylococcus aureus and some nonpathogenic bacteria (10,13,42); however, the processing mechanisms of glutamyl endopeptidases have not been clearly defined.…”
mentioning
confidence: 99%
“…Asn174 in the S1 site of SFase-2 is deleted in SFase-1, resulting in a difference in location of the disulfide bridge between Cys148 and Cys175. The shape of the S l site in SFase-1 is 'narrower' than in SFase-2, and this may be the cause of the reported lack of preference of SFase-1 for large hydrophobic residues at the P1 position [18]. If the SFase-1 shown in red (Fig.…”
Section: Prediction Of the Tertiary Structure Of Sfase-1mentioning
confidence: 99%
“…Streptomyces griseus, in part, produces many proteinases [12, 131, two of which have been well studied, namely proteinase A 1141 and proteinase B [15]. These enzymes have been isolated from the commercially available extracellular filtrate Pronase (Kaken Seiyaku, Tokyo), and their sequences, biochemical properties and crystal structures have been reported [16, 171. We recently investigated an acidic-amino-acid-specific proteinase [18] and a serine proteinase with broad substrate specificity from S. fradiae. The serine proteinase from S.…”
mentioning
confidence: 99%