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• W1967183724 endingPage "95" @default.
• W1967183724 startingPage "87" @default.
• W1967183724 abstract "The gene (npr) encoding an extracellular neutral metalloprotease (Npr) from Streptomyces cacaoi YM15 was cloned in Streptomyces lividans using pIJ702 as a vector. The nucleotide (nt) sequence of npr was determined. The deduced open reading frame encoded 550 amino acids (aa)(60 kDa) with a putative signal sequence of 34 aa at the N terminus. High-resolution S1 mapping identified the transcriptional start point at about 132–134 nt upstream from the start codon. The nt sequences at both -10 and -35 regions resemble the consensus sequence of typical Escherichia coli promoters and a fragment containing the promoter was functional in an E. coli promoter probe plasmid. In vitro transcription and translation of the cloned npr sequence revealed a 60-kDa protein product, correlated with the sequence data but not with the size (35 kDa) of the extracellular Npr. The N-terminal as sequence in conjunction with the aa composition analyses on the purified mature Npr led to the conclusion that it was processed from the 60-kDa pre-proenzyme form encoded by npr. The Npr protease contained putative zinc ligand-binding regions and two repeated motifs. Asp-Ser-Gly, similar to the active site residues of the aspartic acid and retroviral proteases." @default.
• W1967183724 created "2016-06-24" @default.
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• W1967183724 date "1990-03-01" @default.
• W1967183724 modified "2023-09-23" @default.
• W1967183724 title "Extracellular metalloprotease gene of Streptomyces cacaoi: structure, nucleotide sequence and characterization of the cloned gene product" @default.
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• W1967183724 doi "https://doi.org/10.1016/0378-1119(90)90063-w" @default.
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• W1967183724 hasPublicationYear "1990" @default.
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