(Q27666029)

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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

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16 January 2020

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 (English)

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16 January 2020

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16 January 2020

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16 January 2020

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16 January 2020

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Weixiao Yuan Wahlgren

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16 January 2020

Pálma Porrogi

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16 January 2020

Borbála Szenthe

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16 January 2020

András Patthy

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16 January 2020

László Gráf

7

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16 January 2020

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21 November 2010

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16 January 2020

Journal of Biological Chemistry

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16 January 2020

286

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16 January 2020

5

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16 January 2020

3587-3596

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16 January 2020

Light-induced structural changes in a photosynthetic reaction center caught by Laue diffraction

1 reference

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Structure of a serine protease poised to resynthesize a peptide bond

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Probing the dynamic interface between trimethylamine dehydrogenase (TMADH) and electron transferring flavoprotein (ETF) in the TMADH-2ETF complex: role of the Arg-alpha237 (ETF) and Tyr-442 (TMADH) residue pair

1 reference

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20 March 2017

The determination of protonation states in proteins

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20 March 2017

Trypsin revisited: crystallography AT (SUB) atomic resolution and quantum chemistry revealing details of catalysis

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20 March 2017

X-ray structure of a serine protease acyl-enzyme complex at 0.95-A resolution

1 reference

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Factorising ligand affinity: a combined thermodynamic and crystallographic study of trypsin and thrombin inhibition

1 reference

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Atomic resolution structure of native porcine pancreatic elastase at 1.1 A

1 reference

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20 March 2017

The Protein Data Bank

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20 March 2017

The 0.78 A structure of a serine protease: Bacillus lentus subtilisin

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20 March 2017

The three-dimensional structure of Asn102 mutant of trypsin: role of Asp102 in serine protease catalysis

1 reference

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20 March 2017

SHELXL: high-resolution refinement

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Likelihood-enhanced fast translation functions

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20 March 2017

Coot: model-building tools for molecular graphics

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20 March 2017

Automated refinement of protein models

1 reference

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20 March 2017

The CCP4 suite: programs for protein crystallography

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20 March 2017

A low-barrier hydrogen bond in the catalytic triad of serine proteases? Theory versus experiment

1 reference

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20 March 2017

A low-barrier hydrogen bond in the catalytic triad of serine proteases

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3030363

20 March 2017

Role of a Buried Acid Group in the Mechanism of Action of Chymotrypsin

1 reference

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20 March 2017

How do serine proteases really work?

1 reference

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20 March 2017

Serine Proteases: Structure and Mechanism of Catalysis

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PDB2PQR: expanding and upgrading automated preparation of biomolecular structures for molecular simulations

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7 April 2017

Very fast empirical prediction and rationalization of protein pKa values

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7 April 2017

When the surface tells what lies beneath: combinatorial phage-display mutagenesis reveals complex networks of surface-core interactions in the pacifastin protease inhibitor family.

1 reference

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29 September 2017

Insights into the serine protease mechanism from atomic resolution structures of trypsin reaction intermediates

1 reference

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29 September 2017

Enzyme:substrate hydrogen bond shortening during the acylation phase of serine protease catalysis.

1 reference

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29 September 2017

Extended intermolecular interactions in a serine protease-canonical inhibitor complex account for strong and highly specific inhibition.

1 reference

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Understanding noncovalent interactions: ligand binding energy and catalytic efficiency from ligand-induced reductions in motion within receptors and enzymes

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Sub-Angstrom resolution enzyme X-ray structures: is seeing believing?

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Studies of intestinal digestion and absorption in the human

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1 reference

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Expanding the model: anisotropic displacement parameters in protein structure refinement.

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Substrate phage: selection of protease substrates by monovalent phage display

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based on heuristic

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Mechanism of hydrolysis by serine proteases: direct determination of the pKa's of aspartyl-102 and aspartyl-194 in bovine trypsin using difference infrared spectroscopy

1 reference

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inferred from PubMed ID database lookup

Hydrogen bonding markedly reduces the pK of buried carboxyl groups in proteins

1 reference

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inferred from PubMed ID database lookup

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1 reference

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based on heuristic

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High resolution nuclear magnetic resonance study of the histidine—Aspartate hydrogen bond in chymotrypsin and chymotrypsinogen

1 reference

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Identifiers

10.1074/JBC.M110.161604

1 reference

Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:21097875%20AND%20SRC:MED&resulttype=core&format=json

16 January 2020

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Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:21097875%20AND%20SRC:MED&resulttype=core&format=json

16 January 2020

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Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:21097875%20AND%20SRC:MED&resulttype=core&format=json

16 January 2020

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