Molecular analysis of the gene encoding alpha-lytic protease: evidence for a preproenzyme.
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Molecular and biotechnological aspects of microbial proteasesStructure of alpha-lytic protease complexed with its pro regionThe complete general secretory pathway in gram-negative bacteriaMolecular cloning and nucleotide sequence of the beta-lytic protease gene from Achromobacter lyticusMolecular characterization and expression in Escherichia coli of three beta-1,3-glucanase genes from Lysobacter enzymogenes strain N4-7.Cloning, sequencing, and expression of a Thermomonospora fusca protease gene in Streptomyces lividansThe non-penicillin-binding module of the tripartite penicillin-binding protein 3 of Escherichia coli is required for folding and/or stability of the penicillin-binding module and the membrane-anchoring module confers cell septation activity on the fA substitution at His-120 in the LasA protease of Pseudomonas aeruginosa blocks enzymatic activity without affecting propeptide processing or extracellular secretionAnalysis of prepro-alpha-lytic protease expression in Escherichia coli reveals that the pro region is required for activityKinetic stability as a mechanism for protease longevity.Protein purification, gene cloning and sequencing of an acidic endoprotease from Myxococcus xanthus DK101.Propeptide of carboxypeptidase Y provides a chaperone-like function as well as inhibition of the enzymatic activity.Biofilm-degrading enzymes from Lysobacter gummosus.Streptomyces griseus protease B: secretion correlates with the length of the propeptide.Specific inhibition of mature fungal serine proteinases and metalloproteinases by their propeptides.Characterization of the S1 binding site of the glutamic acid-specific protease from Streptomyces griseus.Correct folding of alpha-lytic protease is required for its extracellular secretion from Escherichia coli.The autocatalytic processing of the subtilisin Carlsberg pro-region is independent of the primary structure of the cleavage site.Amino acid and DNA sequences of an extracellular basic protease of Dichelobacter nodosus show that it is a member of the subtilisin family of proteases.
P2860
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P2860
Molecular analysis of the gene encoding alpha-lytic protease: evidence for a preproenzyme.
description
1988 nî lūn-bûn
@nan
1988年の論文
@ja
1988年論文
@yue
1988年論文
@zh-hant
1988年論文
@zh-hk
1988年論文
@zh-mo
1988年論文
@zh-tw
1988年论文
@wuu
1988年论文
@zh
1988年论文
@zh-cn
name
Molecular analysis of the gene ...... : evidence for a preproenzyme.
@en
type
label
Molecular analysis of the gene ...... : evidence for a preproenzyme.
@en
prefLabel
Molecular analysis of the gene ...... : evidence for a preproenzyme.
@en
P2093
P1433
P1476
Molecular analysis of the gene ...... : evidence for a preproenzyme.
@en
P2093
P304
P356
10.1016/0378-1119(88)90434-9
P407
P577
1988-09-01T00:00:00Z