Substitution of active-site His-223 in Pseudomonas aeruginosa elastase and expression of the mutated lasB alleles in Escherichia coli show evidence for autoproteolytic processing of proelastase.
about
Synthesis of multiple exoproducts in Pseudomonas aeruginosa is under the control of RhlR-RhlI, another set of regulators in strain PAO1 with homology to the autoinducer-responsive LuxR-LuxI familyPosttranslational control of the algT (algU)-encoded sigma22 for expression of the alginate regulon in Pseudomonas aeruginosa and localization of its antagonist proteins MucA and MucB (AlgN)Deletion of algK in mucoid Pseudomonas aeruginosa blocks alginate polymer formation and results in uronic acid secretionIdentification of a chitin-binding protein secreted by Pseudomonas aeruginosaSecretion of elastinolytic enzymes and their propeptides by Pseudomonas aeruginosa.Efficient production and processing of elastase and LasA by Pseudomonas aeruginosa require zinc and calcium ionsA major secreted elastase is essential for pathogenicity of Aeromonas hydrophilaBacterial extracellular zinc-containing metalloproteasesA substitution at His-120 in the LasA protease of Pseudomonas aeruginosa blocks enzymatic activity without affecting propeptide processing or extracellular secretionFurther molecular characterization of the cloned Legionella pneumophila zinc metalloprotease.Pseudomonas aeruginosa lasB1 mutants produce an elastase, substituted at active-site His-223, that is defective in activity, processing, and secretion.Functional analysis of the Burkholderia cenocepacia ZmpA metalloprotease.Specific inhibition of mature fungal serine proteinases and metalloproteinases by their propeptides.Functional domains of a zinc metalloprotease from Vibrio vulnificusProtection of sheep against caseous lymphadenitis by use of a single oral dose of live recombinant Corynebacterium pseudotuberculosis.The metalloprotease of Listeria monocytogenes is activated by intramolecular autocatalysis.Molecular cloning of the gene encoding Vibrio metalloproteinase vimelysin and isolation of a mutant with high stability in organic solvents.Identification of cleavage sites involved in proteolytic processing of Pseudomonas aeruginosa preproelastase.Maturation of Pseudomonas aeruginosa elastase. Formation of the disulfide bonds.Intramolecular processing of prothermolysin.
P2860
Q24685109-435592F6-BE42-4CBB-8468-E7FC4DC6B3F8Q28492759-2EE3779E-7203-4283-BFB0-C0F8A98926AEQ28492785-C823CE43-9CA8-459F-A7A7-C5B1FFE5E3EBQ28492925-F39258D2-5A3E-424F-ADD3-DE34DB9216CDQ28492991-28618300-EBD4-4BF2-B409-B96AEA486F7EQ28493133-8EE10317-4612-459B-975A-8B7393F118F3Q30872031-F833AC8F-D382-4ABB-AA85-6AC5945218E1Q34061222-9A890916-FD6B-4165-B45A-622AD26BDDE2Q35617007-46F121EF-F5B2-40F8-932A-0C6BE35E7DB3Q35774304-37DC19F9-7602-43B8-9032-113B192D4329Q36102336-8FA32831-5572-4CA8-BF2D-1110948E00A5Q38324668-ABA42649-A133-4F5F-AB04-37C2A4D45426Q39840978-B00FAC0D-0F88-402A-B8EC-511880459E0FQ39848201-7EF4AC12-9D80-4A01-B3AD-E993DE364C39Q40376405-E1F46606-5BA5-458D-9481-9F68BBC1F608Q41911742-D0CAD9C0-EE0F-4A15-B875-7F3EC54A5EF4Q42678523-1D610A66-D15B-453F-A470-1DDDACA98F9EQ43411238-2A5A048B-4B03-4B82-AEA1-3D0E4312ED60Q43606301-361E6D31-AE8B-4A9D-95FA-BA5528CFAEB4Q47852439-B5284FFD-C256-4179-BE1D-57B6EFE865EA
P2860
Substitution of active-site His-223 in Pseudomonas aeruginosa elastase and expression of the mutated lasB alleles in Escherichia coli show evidence for autoproteolytic processing of proelastase.
description
1991 nî lūn-bûn
@nan
1991年の論文
@ja
1991年論文
@yue
1991年論文
@zh-hant
1991年論文
@zh-hk
1991年論文
@zh-mo
1991年論文
@zh-tw
1991年论文
@wuu
1991年论文
@zh
1991年论文
@zh-cn
name
Substitution of active-site Hi ...... tic processing of proelastase.
@ast
Substitution of active-site Hi ...... tic processing of proelastase.
@en
type
label
Substitution of active-site Hi ...... tic processing of proelastase.
@ast
Substitution of active-site Hi ...... tic processing of proelastase.
@en
prefLabel
Substitution of active-site Hi ...... tic processing of proelastase.
@ast
Substitution of active-site Hi ...... tic processing of proelastase.
@en
P2860
P1476
Substitution of active-site Hi ...... ytic processing of proelastase
@en
P2093
P2860
P304
P356
10.1128/JB.173.24.7781-7789.1991
P407
P577
1991-12-01T00:00:00Z