Structure and mechanism of a proline-specific aminopeptidase from Escherichia coli - Wikidata - wikimedia - TriplyDB

Structure and mechanism of a proline-specific aminopeptidase from Escherichia coli

Structure and mechanism of a proline-specific aminopeptidase from Escherichia coli

http://www.wikidata.org/entity/Q27748986

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Structure of human cytosolic X-prolyl aminopeptidase: a double Mn(II)-dependent dimeric enzyme with a novel three-domain subunit Coupling between catalytic site and collective dynamics: a requirement for mechanochemical activity of enzymes The anti-angiogenic agent fumagillin covalently modifies a conserved active-site histidine in the Escherichia coli methionine aminopeptidase Crystal structure of aminopeptidase N from human pathogen Neisseria meningitidis Structural and molecular basis for the novel catalytic mechanism and evolution of DddP, an abundant peptidase-like bacterial Dimethylsulfoniopropionate lyase: a new enzyme from an old fold Evidence for catalytic roles for Plasmodium falciparum aminopeptidase P in the food vacuole and cytosol Cloning, expression, and characterization of tomato (Lycopersicon esculentum) aminopeptidase P.Cobalt proteins.Crystal Structural and Functional Analysis of the Putative Dipeptidase from Pyrococcus horikoshii OT3 Bacterial protease inhibitors.Crystal structure of X-prolyl aminopeptidase from Caenorhabditis elegans: A cytosolic enzyme with a di-nuclear active site Prolidase activity in chronic plaque psoriasis patients.Microbial degradation of organophosphorus compounds.Structural basis for the metal-selective activation of the manganese transport regulator of Bacillus subtilis.TvMP50 is an immunogenic metalloproteinase during male trichomoniasis Mutations in pepQ Confer Low-Level Resistance to Bedaquiline and Clofazimine in Mycobacterium tuberculosis Structurally distinct active sites in the copper(II)-substituted aminopeptidases from Aeromonas proteolytica and Escherichia coli Identification of cleavage sites and substrate proteins for two mitochondrial intermediate peptidases in Arabidopsis thaliana Analyzing the catalytic role of Asp97 in the methionine aminopeptidase from Escherichia coli.Catalytic mechanisms for phosphotriesterases Comparative characterization of fungal anthracenone and naphthacenedione biosynthetic pathways reveals an α-hydroxylation-dependent Claisen-like cyclization catalyzed by a dimanganese thioesterase.Metal preferences of zinc-binding motif on metalloproteases.Osmoprotection of Bacillus subtilis through import and proteolysis of proline-containing peptides.Cloning, expression, and characterization of aminopeptidase P from the hyperthermophilic archaeon Thermococcus sp. strain NA1.Structural basis of substrate selectivity of E. coli prolidase FE(II) is the native cofactor for Escherichia coli methionine aminopeptidase.Characterization of two new aminopeptidases in Escherichia coli.Functional expression and characterization of the cytoplasmic aminopeptidase P of Caenorhabditis elegans.Crystallization and preliminary X-ray diffraction analysis of Xaa-Pro dipeptidase from Xanthomonas campestris.Crystal structure of a novel prolidase from Deinococcus radiodurans identifies new subfamily of bacterial prolidases.Staphylococcus aureus aminopeptidase S is a founding member of a new peptidase clan.Aminopeptidase p mediated detoxification of organophosphonate analogues of sarin: mechanistic and stereochemical study at the phosphorus atom of the substrate.Structure-Function Relationship of Aminopeptidase P from Pseudomonas aeruginosa.Reduction of product-related species during the fermentation and purification of a recombinant IL-1 receptor antagonist at the laboratory and pilot scale.Investigation of the proton relay system operative in human cystosolic aminopeptidase P.Substrate specificity and reaction mechanism of human prolidase.Structure of the human aminopeptidase XPNPEP3 and comparison of its in vitro activity with Icp55 orthologs: Insights into diverse cellular processes.Using directed evolution to improve the solubility of the C-terminal domain of Escherichia coli aminopeptidase P. Implications for metal binding and protein stability.Improvement of Aminopeptidase Activity of Dizinc(II) Complexes by Increasing Substrate Accessibility Bacterial proteases: current therapeutic use and future prospects for the development of new antibiotics

P2860

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P2860

Structure and mechanism of a proline-specific aminopeptidase from Escherichia coli

http://www.wikidata.org/entity/Q27748986

description

1998 nî lūn-bûn

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1998 թուականի Մարտին հրատարակուած գիտական յօդուած

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1998 թվականի մարտին հրատարակված գիտական հոդված

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1998年の論文

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1998年学术文章

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1998年学术文章

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1998年学术文章

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1998年学术文章

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1998年学术文章

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1998年學術文章

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name

Structure and mechanism of a proline-specific aminopeptidase from Escherichia coli

@ast

Structure and mechanism of a proline-specific aminopeptidase from Escherichia coli

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Structure and mechanism of a proline-specific aminopeptidase from Escherichia coli

@nl

type

label

Structure and mechanism of a proline-specific aminopeptidase from Escherichia coli

@ast

Structure and mechanism of a proline-specific aminopeptidase from Escherichia coli

@en

Structure and mechanism of a proline-specific aminopeptidase from Escherichia coli

@nl

prefLabel

Structure and mechanism of a proline-specific aminopeptidase from Escherichia coli

@ast

Structure and mechanism of a proline-specific aminopeptidase from Escherichia coli

@en

Structure and mechanism of a proline-specific aminopeptidase from Escherichia coli

@nl

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P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

Structure and mechanism of a proline-specific aminopeptidase from Escherichia coli

@en

P2093

H C Freeman

http://www.w3.org/2001/XMLSchema#string

J A Wilce

http://www.w3.org/2001/XMLSchema#string

M C Wilce

http://www.w3.org/2001/XMLSchema#string

P E Lilley

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P2860

Improved methods for building protein models in electron density maps and the location of errors in these models

Structure of the cobalt-dependent methionine aminopeptidase from Escherichia coli: a new type of proteolytic enzyme

Structure of a unique binuclear manganese cluster in arginase

Altering the binuclear manganese cluster of arginase diminishes thermostability and catalytic function

Automated refinement of protein models

The CCP4 suite: programs for protein crystallography

CLUSTAL V: improved software for multiple sequence alignment

Binuclear Metallohydrolases.

Aminopeptidase-P.

Sequence and structure comparison suggest that methionine aminopeptidase, prolidase, aminopeptidase P, and creatinase share a common fold.

P304

3472-3477

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scholarly article

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10.1073/PNAS.95.7.3472

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P433

7

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95

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Nicholas E. Dixon

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1998-03-01T00:00:00Z

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51314447

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9520390

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P921

Escherichia coli

P932

19860

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