UNIGE document Scientific Article
previous document  unige:24407  next document
add to browser collection
Title

The last piece in the vitamin B1 biosynthesis puzzle: Structural and functional insight into yeast 4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate (HMP-P) synthase

Authors
Published in Journal of Biological Chemistry. 2012, vol. 287, no. 50, p. 42333
Abstract Vitamin B1 is essential for all organisms being well recognized as a necessary cofactor for key metabolic pathways such as glycolysis and was more recently implicated in DNA damage responses. Little is known about the enzyme responsible for the formation of the pyrimidine moiety (HMP-P synthase). We report a structure-function study of the HMP-P synthase from yeast, THI5p. Our crystallographic structure shows that the THI5p is a mix between periplasmic binding proteins and pyridoxal 5'-phosphate (PLP) dependent enzymes. Mutational and yeast complementation studies identify the key residues for HMP-P biosynthesis and offers unprecedented insights into the use of PLP as a substrate rather than as a cofactor, the requirement of iron and more generally into the HMP-P synthase reaction mechanism.
Identifiers
PMID: 23048037
Full text
Article (Published version) (2.6 MB) - document accessible for UNIGE members only Limited access to UNIGE
Structures
Projects FNS: 31003A_124909
FNS: 316030_128787
Citation
(ISO format)
COQUILLE, Sandrine Claire et al. The last piece in the vitamin B1 biosynthesis puzzle: Structural and functional insight into yeast 4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate (HMP-P) synthase. In: Journal of Biological Chemistry, 2012, vol. 287, n° 50, p. 42333. https://archive-ouverte.unige.ch/unige:24407

217 hits

2 downloads

Update

Deposited on : 2012-12-11

Export document
Format :
Citation style :