Literature summary for 3.4.14.5 extracted from

Bjelke, J.R.; Christensen, J.; Branner, S.; Wagtmann, N.; Olsen, C.; Kanstrup, A.B.; Rasmussen, H.B.
Tyrosine 547 constitutes an essential part of the catalytic mechanism of dipeptidyl peptidase IV (2004), J. Biol. Chem., 279, 34691-34697.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
hanging drop vapor diffusion method, crystallization of apoenzyme, mutant enzyme Y547F and DPP-IV in complex with diisopropyl fluorophosphate. X-ray crystal structurte analysis of the Y547 mutant reveals no overal changes compared with wild-type apoDPP-IV, except the ablation of the hydroxyl group of Tyr547 and a water molecule positioned in close proximity to Tyr547	Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
D708A	mutant enzyme shows less than 1% of wild-type activity	Homo sapiens
H740L	mutant enzyme shows less than 1% of wild-type activity	Homo sapiens
S630A	mutant enzyme shows less than 1% of wild-type activity	Homo sapiens
Y547F	mutant enzyme shows less than 1% of wild-type activity, kcat/Km is 1523fold lower than wild-type value	Homo sapiens

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
1.43	-	Gly-Pro-4-nitroanilide	pH 7.4, wild-type enzyme	Homo sapiens
44.08	-	Gly-Pro-4-nitroanilide	pH 7.4, mutant enzymeY547F	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P27487	recombinant	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
Gly-Pro-4-nitroanilide + H2O	-	Homo sapiens	Gly-Pro + 4-nitroaniline	-	?

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
5560	-	Gly-Pro-4-nitroanilide	pH 7.4, mutant enzymeY547F	Homo sapiens
279000	-	Gly-Pro-4-nitroanilide	pH 7.4, wild-type enzyme	Homo sapiens

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Release 2023.1 (January 2023)