Literature summary for 4.2.1.30 extracted from

Demick, J.M.; Lanzilotta, W.N.
Radical SAM activation of the B12-independent glycerol dehydratase results in formation of 5-deoxy-5-(methylthio)adenosine and not 5-deoxyadenosine (2011), Biochemistry, 50, 440-442.

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Activating Compound

Activating Compound	Comment	Organism	Structure
glycerol dehydratase activating enzyme	glycerol dehydratase is activated by another enzyme termed the glycerol dehydratase activating enzyme, GD-AE, leading to formation of a glycyl radical. Formation of the glycyl radical requires a reduced iron-sulfur cluster, contained by GD-AE, and S-adenosyl-L-methionine. The GD-AE harbors adenosine and catalytic cluster (CX3CX2C) binding motifs, an additional [4Fe-4S] cluster binding motifs in the primary structure of the GD-AE and multiple Fe-S clusters that may or may not be spin-coupled	Clostridium butyricum
additional information	glycerol dehydratase requires strictly anoxic conditions	Clostridium butyricum
S-adenosyl-L-methionine	glycerol dehydratase requires S-adenosyl-L-methionine and strictly anoxic conditions	Clostridium butyricum

Organism

Organism	UniProt	Comment	Textmining
Clostridium butyricum	-	-	-

General Information

General Information	Comment	Organism
physiological function	radical S-adenosyl-L-methionine activation of the B12-independent glycerol dehydratase results in formation of 5-deoxy-5-(methylthio)adenosine and not 5-deoxyadenosine	Clostridium butyricum

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Release 2023.1 (January 2023)