» Articles » PMID: 6758764

Current Problems in Mechanistic Studies of Serine and Cysteine Proteinases

Overview
Journal Biochem J
Specialty Biochemistry
Date 1982 Oct 1
PMID 6758764
Citations 35
Authors
Affiliations
Soon will be listed here.
Citing Articles

Molecular basis of specificity and deamidation of eIF4A by Burkholderia Lethal Factor 1.

Mobbs G, Aziz A, Dix S, Blackburn G, Sedelnikova S, Minshull T Commun Biol. 2022; 5(1):272.

PMID: 35347220 PMC: 8960835. DOI: 10.1038/s42003-022-03186-2.


Catalytic Site p Values of Aspartic, Cysteine, and Serine Proteases: Constant pH MD Simulations.

Hofer F, Kraml J, Kahler U, Kamenik A, Liedl K J Chem Inf Model. 2020; 60(6):3030-3042.

PMID: 32348143 PMC: 7312390. DOI: 10.1021/acs.jcim.0c00190.


Distinct Roles of Catalytic Cysteine and Histidine in the Protease and Ligase Mechanisms of Human Legumain As Revealed by DFT-Based QM/MM Simulations.

Elsasser B, Zauner F, Messner J, Soh W, Dall E, Brandstetter H ACS Catal. 2017; 7(9):5585-5593.

PMID: 28932620 PMC: 5600538. DOI: 10.1021/acscatal.7b01505.


Role of proteases in the pathophysiology of cardiac disease.

Singh R, Dandekar S, Elimban V, Gupta S, Dhalla N Mol Cell Biochem. 2016; 263(1):241-56.

PMID: 27520682 DOI: 10.1023/B:MCBI.0000041865.63445.40.


An Unusual Member of the Papain Superfamily: Mapping the Catalytic Cleft of the Marasmius oreades agglutinin (MOA) with a Caspase Inhibitor.

Cordara G, van Eerde A, Grahn E, Winter H, Goldstein I, Krengel U PLoS One. 2016; 11(2):e0149407.

PMID: 26901797 PMC: 4764322. DOI: 10.1371/journal.pone.0149407.


References
1.
Birktoft J, Blow D . Structure of crystalline -chymotrypsin. V. The atomic structure of tosyl- -chymotrypsin at 2 A resolution. J Mol Biol. 1972; 68(2):187-240. DOI: 10.1016/0022-2836(72)90210-0. View

2.
Kossiakoff A, Spencer S . Neutron diffraction identifies His 57 as the catalytic base in trypsin. Nature. 1980; 288(5789):414-6. DOI: 10.1038/288414a0. View

3.
Polgar L . Deuterium isotope effects on papain acylation. Evidence for lack of general base catalysis and for enzyme--leaving-group interaction. Eur J Biochem. 1979; 98(2):369-74. DOI: 10.1111/j.1432-1033.1979.tb13196.x. View

4.
Markley J, Travers F, Balny C . Lack of evidence for a tetrahedral intermediate in the hydrolysis of nitroanilide substrates by serine proteinases. Subzero-temperature stopped-flow experiments. Eur J Biochem. 1981; 120(3):477-85. DOI: 10.1111/j.1432-1033.1981.tb05726.x. View

5.
Brocklehurst K, Baines B, Malthouse J . Differences in the interaction of the catalytic groups of the active centres of actinidin and papain. Rapid purification of fully active actinidin by covalent chromatography and characterization of its active centre by use of two-protonic-state.... Biochem J. 1981; 197(3):739-46. PMC: 1163189. DOI: 10.1042/bj1970739. View