Literature summary for 5.3.1.1 extracted from

Borchert, T.V.; Abagyan, R.; Jaenicke, R.; Wierenga, R.K.
Design, creation, and characterization of a stable, monomeric triosephosphate isomerase (1994), Proc. Natl. Acad. Sci. USA, 91, 1515-1518.

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Protein Variants

Protein Variants	Comment	Organism
additional information	wild-type enzyme consists of two identical subunits that form a very tight dimer involving interactions of 32 residues of each subunit. By replacing 15 residues of the major interface loop by another 8-residue fragment, a variant is constructed that is a stable and monomeric protein with TIM activity, monoTIM. The turnover numer of the monomeric form is 100fold lower	Trypanosoma brucei

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
22000	25360	genetically engineered monomeric enzyme form, gel filtration, sedimentation equilibrium experiments	Trypanosoma brucei

Organism

Organism	UniProt	Comment	Textmining
Trypanosoma brucei	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
D-Glyceraldehyde 3-phosphate	-	Trypanosoma brucei	Glycerone phosphate	-	?

Subunits

Subunits	Comment	Organism
dimer	wild-type enzyme consists of two identical subunits that form a very tight dimer involving interactions of 32 residues of each subunit	Trypanosoma brucei

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Release 2023.1 (January 2023)