Literature summary for 4.2.1.28 extracted from

Levin, B.J.; Balskus, E.P.
Characterization of 1,2-propanediol dehydratases reveals distinct mechanisms for B12-dependent and glycyl radical enzymes (2018), Biochemistry, 57, 3222-3226 .

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Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Klebsiella oxytoca
expression in Escherichia coli	Roseburia inulinivorans

Organism

Organism	UniProt	Comment	Textmining
Klebsiella oxytoca	Q59470 and Q59471 and Q59472	Q59470 i.e. alpha-subunit pddA, Q59471 i.e. beta-subunit PddB, Q59472 i.e. gamma-subunit PddC	-
Klebsiella oxytoca ATCC 8724	Q59470 and Q59471 and Q59472	Q59470 i.e. alpha-subunit pddA, Q59471 i.e. beta-subunit PddB, Q59472 i.e. gamma-subunit PddC	-
Roseburia inulinivorans	-	-	-
Roseburia inulinivorans A2-194	-	-	-

Cofactor

Cofactor	Comment	Organism	Structure
[4Fe-4S]-center	presence of 2.80 equivalents of iron and 2.71 ± 0.02 equivalents of sulfur per monomer	Klebsiella oxytoca
[4Fe-4S]-center	presence of 2.80 equivalents of iron and 2.71 ± 0.02 equivalents of sulfur per monomer	Roseburia inulinivorans

General Information

General Information	Comment	Organism
physiological function	mechanistic comparison between glycyl radical-dependent enzyme from Roseburia inulinivorans and vitamin B12-dependent enzyme from Klebsiella oxytoca. Unlike B12-dependent propanediol dehydratase, the glycyl radical-dependent enzyme appears to catalyze the direct elimination of a hydroxyl group from an initially formed substrate-based radical, avoiding the generation of a 1,1-gem diol intermediate	Klebsiella oxytoca
physiological function	mechanistic comparison between glycyl radical-dependent enzyme from Roseburia inulinivorans and vitamin B12-dependent enzyme from Klebsiella oxytoca. Unlike B12-dependent propanediol dehydratase, the glycyl radical-dependent enzyme appears to catalyze the direct elimination of a hydroxyl group from an initially formed substrate-based radical, avoiding the generation of a 1,1-gem diol intermediate	Roseburia inulinivorans

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Release 2023.1 (January 2023)