On the stability of tetrahedral intermediates within the active sites of serine and cysteine proteases.

No abstract is available for this paper.

• Publication year

  1983

• Venue

  European Journal of Biochemistry

• Publication date

  1983-09-01

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1111/J.1432-1033.1983.TB07659.XPMID 6350001
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• Lack of evidence for a tetrahedral intermediate in the hydrolysis of nitroanilide substrates by serine proteinases. Subzero-temperature stopped-flow experiments.

  1981cited by this paper
• Soybean trypsin inhibitor (Kunitz) and its complex with trypsin. Carbon-13 nuclear magnetic resonance studies of the reactive site arginine.

  1980cited by this paper
• The detection, accumulation and stabilization of a tetrahedral intermediate in trypsin catalysis.

  1980cited by this paper
• Applications of 15N NMR spectroscopy to the study of unsymmetrically N-substituted amides and model peptide compounds

  1980cited by this paper
• Carbon-13 nuclear magnetic resonance studies of the selectively isotope-labeled reactive site peptide bond of the basic pancreatic trypsin inhibitor in the complexes with trypsin, trypsinogen, and anhydrotrypsin.

  1980cited by this paper
• Stereospecific synthesis of α-aminoacyl aldehydes and their interaction with α-chymotrypsin

  1980cited by this paper
• Mechanism of association of a specific aldehyde "transition-state analogue" to the active site of alpha-chymotrypsin.

  1979cited by this paper
• Evidence for hemiacetal formation between N-acyl-L-phenylalaninals and alpha-chymotrypsin by cross-saturation nuclear magnetic resonance spectroscopy.

  1979cited by this paper
• Reaction of peptide aldehydes with serine proteases. Implications for the entropy changes associated with enzymatic catalysis.

  1979cited by this paper
• Detection and accumulation of tetrahedral intermediates in elastase catalysis.

  1979cited by this paper
• Detection of a tetrahedral intermediate in the trypsin-catalysed hydrolysis of specific ring-activated anilides.

  1978cited by this paper
• Serine proteases: structure and mechanism of catalysis.

  1977cited by this paper
• Estimation of the free energies of addition of nucleophiles to conjugated carbonyl compounds and to acyl derivatives

  1977cited by this paper
• Inhibition of papain by N-acyl-aminoacetaldehydes and N-acyl-aminopropanones. Evidence for hemithioacetal formation by a cross-saturation technique in nuclear-magnetic resonance spectroscopy.

  1977cited by this paper
• Antiproteolytic aldehydes and ketones: substituent and secondary deuterium isotope effects on equilibrium addition of water and other nucleophiles.

  1977cited by this paper
• Interaction of papain with derivatives of phenylalanylglycinal.

  1977cited by this paper
• Evidence for hemiacetal formation between α-chymotrypsin and hydrocinnamaldehyde by cross-saturation nuclear magnetic resonance spectroscopy

  1977cited by this paper
• Thiohemiacetal formation by inhibitory aldehydes at the active site of papain.

  1977cited by this paper
• Mechanism of chymotrypsin: acid/base catalysis and transition-state solvation by the active site.

  1977cited by this paper
• Mechanism of action of serine proteases: tetrahedral intermediate and concerted proton transfer.

  1976cited by this paper
• The structure of the complex formed by bovine trypsin and bovine pancreatic trypsin inhibitor

  1975cited by this paper
• The binding of specific and non-specific aldehyde substrate analogs to alpha-chymotrypsin.

  1975cited by this paper
• The binding of a non-specific "transition state analogue" to alpha-chymotrypsin.

  1975cited by this paper
• The binding of a non‐specific ‘transition state analogue’ to α‐chymotrypsin

  1975cited by this paper
• Mechanism of serine protease action. Ionization behavior of tetrahedral adduct between α‐lytic protease and tripeptide aldehyde studied by carbon‐13 magnetic resonance

  1975cited by this paper
• The binding of specific and non‐specific aldehyde substrate analogs to α‐chymotrypsin

  1975cited by this paper
• Structure of the complex formed by bovine trypsin and bovine pancreatic trypsin inhibitor. II. Crystallographic refinement at 1.9 A resolution.

  1974cited by this paper
• Electronic and stearic effects of substitution at nitrogen on hindered rotation in formanilides

  1974cited by this paper
• Crystal structure of the complex of porcine trypsin with soybean trypsin inhibitor (Kunitz) at 2.6-A resolution.

  1974cited by this paper
• Specificity of -chymotrypsin. Separation of polar, steric, and specific effects in the -chymotrypsin-catalyzed hydrolysis of acyl-substituted p-nitrophenyl esters.

  1973cited by this paper
• Mechanism of chymotrypsin. Structure, reactivity, and nonproductive binding relationships.

  1973cited by this paper
• Structure of the complex formed by bovine trypsin and bovine pancreatic trypsin inhibitor. Crystal structure determination and stereochemistry of the contact region.

  1973cited by this paper
• Substituent effects. III. Dissociation constants of .beta.-arylpropionic acids, .beta.-arylisovaleric acids, N-arylglycines, aryloxyacetic acids, N-aryl-.beta.-alanines, and some related systems

  1973cited by this paper
• Leaving group specificity in the chymotrypsin-catalyzed hydrolysis of peptides. A stereochemical interpretation.

  1973cited by this paper
• Use of peptide aldehydes to generate transition-state analogs of elastase.

  1973cited by this paper
• Peptide aldehydes inhibiting chymotrypsin.

  1972cited by this paper
• Aldehydes as inhibitors of papain.

  1972cited by this paper
• Free energies of hydrolysis of amides and peptides in aqueous solution at 25 degrees.

  1971cited by this paper
• Nuclear Magnetic Resonance Spectra of Anilides. II. NMR Parameters and Rotational Barriers for Some p-Substituted Formanilides.

  1968cited by this paper
• Investigations of the chymotrypsin-catalyzed hydrolysis of specific substrates. I. The pH dependence of the catalytic hydrolysis of N-acetyl-L-tryptophanamide by three forms of the enzyme at alkaline pH.

  1967cited by this paper
• THE REACTIVITY OF NUCLEOPHILIC REAGENTS WITH FUROYL-CHYMOTRYPSIN.

  1965cited by this paper
• THE REACTIVITY OF NUCLEOPHILIC REAGENTS WITH FUROYL-CHYMOTRYPSIN.

  1965cited by this paper
• The Ionization Constants of N-(Substituted-phenyl)-glycines

  1963cited by this paper

• Dynamics in the active site of β-secretase: a network analysis of atomistic simulations.

  2011cites this paper
• X-ray snapshot of HIV-1 protease in action: observation of tetrahedral intermediate and short ionic hydrogen bond SIHB with catalytic aspartate.

  2010cites this paper
• Catalytic mechanism in papain family of cysteine peptidases.

  1994cites this paper
• A study of the stabilization of tetrahedral adducts by trypsin and delta-chymotrypsin.

  1992cites this paper
• Recent developments in inhibiting cysteine and serine proteases.

  1990cites this paper
• Chapter 3 Structure and function of serine proteases

  1987cites this paper
• Chapter 2 Cysteine proteinases

  1987cites this paper
• 13C NMR study of the ionizations within a trypsin-chloromethyl ketone inhibitor complex.

  1985cites this paper
• Studying enzyme mechanism by 13C nuclear magnetic resonance.

  1984cites this paper
• Dynamics in the Active Site of Β-secretase: a Network Analysis of Atomistic Simulations

  year unknowncites this paper