Literature summary for 4.1.99.19 extracted from

Kriek, M.; Martins, F.; Leonardi, R.; Fairhurst, S.A.; Lowe, D.J.; Roach, P.L.
Thiazole synthase from Escherichia coli: an investigation of the substrates and purified proteins required for activity in vitro (2007), J. Biol. Chem., 282, 17413-17423.

Search for more literature for 4.1.99.19

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Iron	iron content is 5.2 mol eq of iron per mol of ThiH, contains an 4F-4S cluster essential for activity	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P30140	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Escherichia coli

Reaction

Reaction	Comment	Organism	Reaction ID
L-tyrosine + S-adenosyl-L-methionine + NADPH = 2-iminoacetate + 4-methylphenol + 5'-deoxyadenosine + L-methionine + NADP+ + H+	ThiH is a member of the radical-S-adenosyl-L-methionine family. Proposed mechanism of ThiH-dependent cleavage of L-tyrosine: S-adenosyl-L-methionine is reductively cleaved to yield a highly reactive 5'-deoxyadenosyl radical. This radical is proposed to abstract the phenolic hydrogen atom from tyrosine, and the resultant substrate radical cleaves to yield dehydroglycine, which is required by ThiG for the thiazole cyclization reaction	Escherichia coli	a

Synonyms

Synonyms	Comment	Organism
thiH	-	Escherichia coli

Cofactor

Cofactor	Comment	Organism	Structure
[4Fe-4S]-center	essential for activity	Escherichia coli

General Information

General Information	Comment	Organism
physiological function	the enzyme is essential for thiazole biosynthesis in Escherichia coli	Escherichia coli

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Release 2023.1 (January 2023)