Literature summary for 2.4.2.60 extracted from

Jurgenson, C.; Chatterjee, A.; Begley, T.; Ealick, S.
Structural insights into the function of the thiamin biosynthetic enzyme Thi4 from Saccharomyces cerevisiae (2006), Biochemistry, 45, 11061-11070 .

Search for more literature for 2.4.2.60

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Saccharomyces cerevisiae

Crystallization (Commentary)

Crystallization (Comment)	Organism
to 1.8 A resolution. Thi4 exists as an octamer with two monomers in the asymmetric unit. A tightly bound adenosine diphospho-5-(beta-ethyl)-4-methylthiazole-2-carboxylic acid is present at the active site. The Thi4 structure reveals a protein structure with a GR2 domain that binds NAD instead of FAD	Saccharomyces cerevisiae

Organism

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae	P32318	-	-
Saccharomyces cerevisiae ATCC 204508	P32318	-	-

Synonyms

Synonyms	Comment	Organism
Thi4	-	Saccharomyces cerevisiae

Cofactor

Cofactor	Comment	Organism	Structure
NAD+	-	Saccharomyces cerevisiae

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)