Bacillus thermoproteolyticus neutral proteinase
This enzyme belongs to peptidase family-M4 (Thermolysin family). Although this enzyme binds four calcium ions, they are not involved in catalysis. According to the literature [8], the catalytic reaction proceeds as follows: (1) Carbonyl oxygen of Target bond and hydrorytic water molecule are bound to zinc ion, which facilitates the catalysis. Glu143 acts as a general base to deprotonate and activate the water molecule. (2) The water molecule makes a nucleophilic attack on the carbonyl carbon to form a tetrahedral intermediate. (3) The intermediate is stabilized by His231, Tyr157, Asn112 and mainchain carbonyl of Ala113, together with the zinc ion. Here, His231 and Tyr157 stabilize the negative charge on the hydroxyl anion (originally carbonyl oxygen), whereas Asn112 and mainchain carbonyl group of Ala113 stabilize the leaving amine group. The zinc ion stabilizes the negative charge on the hydroxyl anion and the new hydroxyl group (originally water). (4) Glu143 acts as a genral acid to protonate the leaving amine group. (Glu143 may also shuttle the remaining proton from the hydroxyl group to the amine to complete the bond cleavage.)
Evidence of an essential histidine residue in thermolysin
The binding of L-valyl-L-tryptophan to crystalline thermolysin illustrates the mode of interaction of a product of peptide hydrolysis
Thermolysin as a catalyst in enzymatic synthesis of asparagine-containing peptides II
Structural comparison suggests that thermolysin and related neutral proteases undergo hinge-bending motion during catalysis
Inhibition of thermolysin and neutral endopeptidase 24.11 by a novel glutaramide derivative: X-ray structure determination of the thermolysin-inhibitor complex
NMR solution structure of the C-terminal fragment 255-316 of thermolysin: a dimer formed by subunits having the native structure
Redetermination and refinement of the complex of benzylsuccinic acid with thermolysin and its relation to the complex with carboxypeptidase A
Observation of the pre-steady state process in thermolysin catalysis with a fluorescent displacement probe at low pH
The role of histidine 231 in thermolysin-like enzymes. A site-directed mutagenesis study
Solid-state nuclear magnetic resonance analysis of the conformation of an inhibitor bound to thermolysin
Structural analysis of zinc substitutions in the active site of thermolysin
Arazoformyl dipeptide substrates for thermolysin. Confirmation of a reverse protonation catalytic mechanism
NMR solution structure of the 205-316 C-terminal fragment of thermolysin. An example of dimerization coupled to partial unfolding
Synthesis of dipeptides by suspension-to-suspension conversion via thermolysin catalysis: from analytical to preparative scale
Model building of a thermolysin-like protease by mutagenesis.
Enzymatic and structural approaches of the thermolysin mechanism in glycerol-containing media
Testing for diffusion limitations in salt-activated enzyme catalysts operating in organic solvents
Intramolecular processing of prothermolysin
Elucidation of the mode of interaction of thermolysin with a proteinaceous metalloproteinase inhibitor, SMPI, based on a model complex structure and a structural dynamics analysis
Crystal structures of alpha-mercaptoacyldipeptides in the thermolysin active site: structural parameters for a Zn monodentation or bidentation in metalloendopeptidases
Characterization of a novel stable biocatalyst obtained by protein engineering.
Binding of hydroxamic acid inhibitors to crystalline thermolysin suggests a pentacoordinate zinc intermediate in catalysis
Locating interaction sites on proteins: the crystal structure of thermolysin soaked in 2% to 100% isopropanol
Substrate specificity in the highly heterogeneous M4 peptidase family is determined by a small subset of amino acids.
A novel method of aligning molecules by local surface shape similarity
An evolutionary computational approach to the phase problem in macromolecular X-ray crystallography
Novel kinetic analysis of enzymatic dipeptide synthesis: effect of pH and substrates on thermolysin catalysis
Experimental and computational mapping of the binding surface of a crystalline protein
The 2.2 A resolution structure of thermolysin (TLN) crystallized in the presence of potassium thiocyanate.
Thermolysin in the absence of substrate has an open conformation
Efficient transesterification of sucrose catalysed by the metalloprotease thermolysin in dimethylsulfoxide
Molecular imprinting of enzymes with water-insoluble ligands for nonaqueous biocatalysis
Structure of thermolysin refined at 1.6 A resolution
The effects of modifying the surface charge on the catalytic activity of a thermolysin-like protease.
A theoretical study of the mechanism for peptide hydrolysis by thermolysin.
Consensus scoring for ligand/protein interactions
Interactions of a new alpha-aminophosphinic derivative inside the active site of TLN (thermolysin): a model for zinc-metalloendopeptidase inhibition.
A cyclic metallopeptide induces alpha helicity in short peptide fragments of thermolysin.
Origin of the stereospecificity in binding hydroxamates of alpha- and beta-phenylalanine methylamide to thermolysin revealed by the X-ray crystallographic study.
Structural analysis of the inhibition of thermolysin by an active-site-directed irreversible inhibitor
Binding of N-carboxymethyl dipeptide inhibitors to thermolysin determined by X-ray crystallography: a novel class of transition-state analogues for zinc peptidases
Crystallographic structural analysis of phosphoramidates as inhibitors and transition-state analogs of thermolysin
Slow- and fast-binding inhibitors of thermolysin display different modes of binding: crystallographic analysis of extended phosphonamidate transition-state analogues
Structures of two thermolysin-inhibitor complexes that differ by a single hydrogen bond