Literature summary for 3.4.24.27 extracted from

Blumberger, J.; Lamoureux, G.; Klein, M.L.
Peptide hydrolysis in thermolysin: ab initio QM/MM investigation of the Glu143-assisted water addition mechanism (2007), J. Chem. Theory Comput., 3, 1837-1850.

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Metals/Ions

Metals/Ions	Comment	Organism	Structure
Zn2+	a zinc metalloprotease	Bacillus thermoproteolyticus

Organism

Organism	UniProt	Comment	Textmining
Bacillus thermoproteolyticus	-	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
preferential cleavage: -/-Leu > -/-Phe	classical molecular dynamics simulation., and ab initio quantum mechanics/molecular mechanics, QM/MM, investigation of the Glu143-assisted water addition mechanism in thermolysin peptide hydrolysis. The mechanism consists of three distinct steps: (i) a Zn-bound water molecule is deprotonated by Glu143 and attacks the carbonyl bond of the substrate; (ii) Glu143 transfers the proton to the amide nitrogen atom; (iii) the nitrogen atom is protonated and the peptide bond is irreversibly broken. Transition state stabilization for nucleophilic attack is achieved by formation of a weak coordination bond between the substrate carbonyl oxygen atom and the Zn ion and of three strong hydrogen bonds between the substrate and protonated His231 and two solvent molecules, overview	Bacillus thermoproteolyticus	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
Ac-Gly-Leu-Ala-methylamide + H2O	model substrate, enzyme-substrate complex, docking structures, overview	Bacillus thermoproteolyticus	?	-	ir

Synonyms

Synonyms	Comment	Organism
TLN	-	Bacillus thermoproteolyticus

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Release 2023.1 (January 2023)