Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

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Gene Review:

serC - phosphoserine aminotransferase

Escherichia coli O157:H7 str. EDL933

Helgad??ttir, S. et al., Tanaka, T. et al., Hester, G. et al.

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Disease relevance of serC

The M. maripaludis homolog complemented a serC mutation in the Escherichia coli phosphoserine aminotransferase [1].

High impact information on serC

Phosphoserine aminotransferase (PSAT; EC 2.6.1.52), a member of subgroup IV of the aminotransferases, catalyses the conversion of 3-phosphohydroxypyruvate to l-phosphoserine [2].
On the other hand, the Methanobacterium AspAT showed remarkable amino acid sequence homology, 31.5%, with rat serine:pyruvate aminotransferase and, 13.5%, with E. coli phosphoserine aminotransferase [3].

Associations of serC with chemical compounds

To establish the mode of phosphoserine production in Methanococcales, cell extracts of M. maripaludis were shown to have phosphoglycerate dehydrogenase and phosphoserine aminotransferase activities [1].

References

Biosynthesis of phosphoserine in the methanococcales. Helgad??ttir, S., Rosas-Sandoval, G., S??ll, D., Graham, D.E. J. Bacteriol. (2007) [Pubmed]
Crystal structure of phosphoserine aminotransferase from Escherichia coli at 2.3 A resolution: comparison of the unligated enzyme and a complex with alpha-methyl-l-glutamate. Hester, G., Stark, W., Moser, M., Kallen, J., Marković-Housley, Z., Jansonius, J.N. J. Mol. Biol. (1999) [Pubmed]
Aspartate aminotransferase from a thermophilic formate-utilizing methanogen, Methanobacterium thermoformicicum strain SF-4: relation to serine and phosphoserine aminotransferases, but not to the aspartate aminotransferase family. Tanaka, T., Yamamoto, S., Moriya, T., Taniguchi, M., Hayashi, H., Kagamiyama, H., Oi, S. J. Biochem. (1994) [Pubmed]

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