Literature summary for 4.2.1.28 extracted from

Doitomi, K.; Kamachi, T.; Toraya, T.; Yoshizawa, K.
Computational mutation study of the roles of catalytic residues in coenzyme B12-dependent diol dehydratase (2016), Bull. Chem. Soc. JPN, 89, 955-964 .

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Protein Variants

Protein Variants	Comment	Organism
D335A	computational mutation study. The OH group migration is accelerated in the Asp335Ala mutant, due to the absence of the electric repulsion between Asp335 and the migrating OH group	Klebsiella oxytoca
E170A E170Q	computational mutation study. The spectator OH group is not fully activated in the Glu170Gln and Glu170Ala mutants during the OH group migration, and thus the activation energies in the Glu170Gln and Glu170Ala mutants are higher than that in the wild-type enzyme	Klebsiella oxytoca
E170Q	computational mutation study. The spectator OH group is not fully activated in the Glu170Gln and Glu170Ala mutants during the OH group migration, and thus the activation energies in the Glu170Gln and Glu170Ala mutants are higher than that in the wild-type enzyme	Klebsiella oxytoca
H143A	computational mutation study. The resonance stabilization of the transition state in the OH group migration is observed in the wild-type enzyme while not in the His143Ala mutant. Since the cleavage of the C2-oxygen bond of 1,2-diol radical proceeds in a more homolytic manner in the His143Ala mutant, Glu170 cannot effectively deprotonate the spectator OH group in the transition state, leading to increased activation energy of the OH group migration in the His143Ala mutant	Klebsiella oxytoca

Organism

Organism	UniProt	Comment	Textmining
Klebsiella oxytoca	Q59470	-	-

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Release 2023.1 (January 2023)