Literature summary for 4.2.3.1 extracted from

Shoji, M.; Hanaoka, K.; Ujiie, Y.; Tanaka, W.; Kondo, D.; Umeda, H.; Kamoshida, Y.; Kayanuma, M.; Kamiya, K.; Shiraishi, K.; Machida, Y.; Murakawa, T.; Hayashi, H.
A QM/MM study of the L-threonine formation reaction of threonine synthase: implications into the mechanism of the reaction specificity (2014), J. Am. Chem. Soc., 136, 4525-4533.

Crystallization (Commentary)

Crystallization (Comment)	Organism
comparative QM/MM calculations. The base that abstracts a proton from the attacking water is the epsilon-amino group of Lys61 rather than the phosphate ion. The phosphate ion is important for stabilizing the transition state of the normal transaldimination to form L-threonine by making a hydrogen bond with the hydroxy group of the L-threonine moiety. Proposal of a mechanism, in which a proton temporarily resides at the phenolate O3' of pyridoxal-5'-phosphate, for the transaldimination process	Thermus thermophilus

Crystallization (Comment)

Organism

comparative QM/MM calculations. The base that abstracts a proton from the attacking water is the epsilon-amino group of Lys61 rather than the phosphate ion. The phosphate ion is important for stabilizing the transition state of the normal transaldimination to form L-threonine by making a hydrogen bond with the hydroxy group of the L-threonine moiety. Proposal of a mechanism, in which a proton temporarily resides at the phenolate O3' of pyridoxal-5'-phosphate, for the transaldimination process

Thermus thermophilus

Organism

Organism	UniProt	Comment	Textmining
Thermus thermophilus	-	-	-

Synonyms

Synonyms	Comment	Organism
ThrS	-	Thermus thermophilus

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Release 2023.1 (January 2023)