Inactivation of Subtilisin Carlsberg by N-((tert-Butoxycarbonyl)alanylprolylphenylalanyl)-O-benzoyl Hydroxylamine: Formation of a Covalent Enzyme-Inhibitor Linkage in the Form of a Carbamate Derivative (original) (raw)

A Method for Designing Peptide Substrates for Proteases. Tripeptidyl-p-nitroanilide Substrates for Subtilisin Carlsberg

Marianne Pusztai-Carey

European Journal of Biochemistry, 1979

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Polypeptide halomethyl ketones bind to serine proteases as analogs of the tetrahedral intermediate. X-ray crystallographic comparison of lysine- and phenylalanine-polypeptide chloromethyl ketone-inhibited subtilisin

Jens Birktoft

The Journal of biological chemistry, 1976

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Regulation of an intracellular subtilisin protease activity by a short propeptide sequence through an original combined dual mechanism

Dafydd Jones

Proceedings of the …, 2011

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Importance of Tetrahedral Intermediate Formation in the Catalytic Mechanism of the Serine Proteases Chymotrypsin and Subtilisin

J. Malthouse

Biochemistry, 2012

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Subtilisin-catalyzed hydrolysis of peptide methyl esters

Manfred Philipp

FEBS Letters, 1974

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A highly active and oxidation-resistant subtilisin-like enzyme produced by a combination of site-directed mutagenesis and chemical modification

lene bech

European Journal of Biochemistry, 1990

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A study of the unfolding of the inhibited subtilisin in guanidine hydrochloride

Richard Epand

International journal of peptide and protein research, 1975

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Alteration of the specificity of subtilisin BPN' by site-directed mutagenesis in its S1 and S1' binding sites

Thomas Graycar

Journal of the American Chemical Society, 1991

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Insights on activity and stability of subtilisin E towards guanidinium chloride and sodium dodecylsulfate

Danilo Roccatano

Journal of Biotechnology, 2014

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Redesigning the reactive site loop of the wheat subtilisin/chymotrypsin inhibitor (WSCI) by site-directed mutagenesis. A protein–protein interaction study by affinity chromatography and molecular modeling

Augusto Parente

Biochimie, 2009

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Modification of arginine residues in subtilisins Novo and Carlsberg

Krassimira Idakieva

International Journal of Peptide and Protein Research, 1983

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The crystal structure of an autoprocessed Ser221Cys-subtilisin E-propeptide complex at 2.0 å resolution 1 1 Edited by I. A. Wilson

ujwal shinde

Journal of Molecular Biology, 1998

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Comparison of x-ray crystal structures of an acyl-enzyme intermediate of subtilisin Carlsberg formed in anhydrous acetonitrile and in water

Lawrence Stern

Proceedings of the National Academy of Sciences, 1998

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Complex between the subtilisin from a mesophilic bacterium and the Leech inhibitor eglin-C

Z. Dauter

Acta Crystallographica Section B Structural Science, 1991

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Pro‐peptide as an intermolecular chaperone: renaturation of denatured subtilisin E with a synthetic pro‐peptide

Saburo Aimoto

Molecular Microbiology, 1991

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Transformation of active-site lysine in naturally occurring trypsin inhibitors. A basis for a general mechanism for inhibition of proteolytic enzymes

Royce Haynes

Biochemistry, 1968

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Structural Basis of Inhibition Revealed by a 1:2 Complex of the Two-headed Tomato Inhibitor-II and Subtilisin Carlsberg

Isabelle Barrette-Ng

Journal of Biological Chemistry, 2003

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The crystal structure of an autoprocessed Ser221Cys-subtilisin E-propeptide complex at 2.0 å resolution1

ujwal shinde

Journal of Molecular Biology, 1998

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Molecular dynamic study of subtilisin Carlsberg in aqueous and nonaqueous solvents

Gabriel Barletta

Molecular Simulation, 2009

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Structural Basis for Dual-Inhibition Mechanism of a Non-Classical Kazal-Type Serine Protease Inhibitor from Horseshoe Crab in Complex with Subtilisin

Adrian Velazquez-Campoy

PLoS ONE, 2011

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The crystal structure of an autoprocessed Ser221Cys-subtilisin E-propeptide complex at 2.0 å resolution

U. Shinde

Journal of Molecular Biology, 1998

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Engineering Substrate Preference in Subtilisin: Structural and Kinetic Analysis of a Specificity Mutant †

Biao Ruan

Biochemistry, 2008

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Crystal structure of an intracellular subtilisin reveals novel structural features unique to this subtilisin family

Dafydd Jones

Structure, 2010

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Re-examination of the charge relay system in subtilisin comparison with other serine proteases

Jens Birktoft

Journal of Biological …, 1977

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Molecular orbital analysis of the catalytic process of serine proteinases: Effect of environment on protonation of the histidine-aspartate diad of subtilisin

Paul Mezey

Journal of Molecular Structure-theochem, 1982

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Computational Study of the Michaelis Complex Formation and the Effect on the Reaction Mechanism of Cruzain Cysteine Protease

Kemel Arafet

ACS Omega

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Inhibition of subtilisin by substituted arylboronic acids

Manfred Philipp

FEBS Letters, 1981

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Novel Protease Inhibitors via Computational Redesign of Subtilisin BPN′ Propeptide

Stefan Lutz

Biochemistry, 2012

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Activity of Subtilisin Carlsberg in macromolecular crowding

Ajay Shaw

Journal of Photochemistry and Photobiology B: Biology, 2007

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Subtilisin from Bacillus subtilis strain 72. The influence of substrate structure, temperature and pH on catalytic properties

Mikhail Gololobov

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1992

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Folding Pathway Mediated by an Intramolecular Chaperone: Characterization of the Structural Changes in Pro-subtilisin E Coincident with Autoprocess ing

ujwal shinde

Journal of Molecular Biology, 1995

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Probing structure-function relationships of serine hydrolases and proteases with carbamate and thiocarbamate inhibitors

Gialih Lin

The protein journal, 2006

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A novel serine protease inhibition motif involving a multi-centered short hydrogen bonding network at the active site

James Janc

Journal of Molecular Biology, 2001

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The Catalytic Aspartate Is Protonated in the Michaelis Complex Formed between Trypsin and an in Vitro Evolved Substrate-like Inhibitor A REFINED MECHANISM OF SERINE PROTEASE ACTION * □ S

Gergely Katona

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Enzymes in organic synthesis: use of subtilisin and a highly stable mutant derived from multiple site-specific mutations

Bill Hennen

Journal of the American Chemical Society, 1990

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