Literature summary for 3.4.21.50 extracted from

Masaki, T.; Tanaka, T.; Tsunasawa, S.; Sakiyama, F.; Soejima, S.
Inhibition of Achromobacter protease I by lysinal derivatives (1992), Biosci. Biotechnol. Biochem., 56, 1604-1607.

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Inhibitors

Inhibitors	Comment	Organism	Structure
benzoyl-DL-lysinal	-	Achromobacter lyticus
benzyloxycarbonyl-Leu-Leu-lysinal	most potent inhibitor in amidolytic assay, non-competitive	Achromobacter lyticus
benzyloxycarbonyl-Leu-Pro-lysinal	-	Achromobacter lyticus
benzyloxycarbonyl-Pro-lysinal	-	Achromobacter lyticus
benzyloxycarbonyl-Val-lysinal	most potent competitive inhibitor in esterolytic assay with tosyl-Lys-methyl ester	Achromobacter lyticus
benzyloxycarbonyl-Val-lysinol	poor competitive inhibitor	Achromobacter lyticus
additional information	acyllysinals, acylaminoacyllysinals and acylpeptidyllysinals function as a transition-state inhibitor	Achromobacter lyticus

Organism

Organism	UniProt	Comment	Textmining
Achromobacter lyticus	-	-	-

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Release 2023.1 (January 2023)