Literature summary for 3.4.23.B8 extracted from

Ma, S.; Vogt, K.; Petrillo, N.; Ruhoff, A.
Characterizing the protonation states of the catalytic residues in apo and substrate-bound human T-cell leukemia virus type 1 protease (2015), Comput. Biol. Chem., 56, 61-70.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
molecular dynamics simulation. In the apo-enzyme, the two catalytic residues are chemically equivalent and are expected to be both unprotonated. Upon substrate binding, the catalytic residues of HTLV-1 protease evolve to a singly protonated state, in which the carboxylic oxygen atom OD1 of Asp32 is protonated and forms a hydrogen bond with the OD1 atom of Asp32' , which is unprotonated	Human T-cell leukemia virus type I

Organism

Organism	UniProt	Comment	Textmining
Human T-cell leukemia virus type I	Q82134	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
Ace-Pro-Val-Ile-Leu-Pro-Ile-NMe + H2O	-	Human T-cell leukemia virus type I	Ace-Pro-Val-Ile-Leu + Pro-Ile-NMe	-	?

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Release 2023.1 (January 2023)