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2.6.1.51 |
| Activity |
2.6.1.51 |
| Description |
Serine--pyruvate aminotransferase. |
| Notes |
The sequences included here are close homologs of the enzyme from rat liver organelles, which is identical to isoenzyme 1 of alanine-glyoxylate aminotransferase (2.6.1.44) and also to asparagine-oxo-acid aminotransferase (2.6.1.14) [Noguchi & Fujiwara (1988) JBC 263, 182].
The enzymes from Drosophila and Aedes also show alanine-glyoxylate aminotransferase activity.
We have included in this family a number of bacterial sequences, as they seem very closely related to the metazoan ones. It must be remarked, however, that for none of these bacterial enzymes activity has been tested biochemically. Even for the Nostoc (Anabaena) enzyme, whose structure has been published, functional validation is lacking. |
| PDB |
1H0C; |
| PLP Fold Type |
I |
| PLP-dependent Domain |
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| Number of sequences |
22 |
| Sequences in seed alignment |
|
| Reference sequence |
SPYA_RAT |
| Domain interval |
45-398 |
| Catalytic site |
231 K |
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| References |
Han GW, Schwarzenbacher R, Page R et al. (2005) Crystal structure of an alanine-glyoxylate aminotransferase from Anabaena sp. at 1.70 A resolution reveals a noncovalently linked PLP cofactor. Proteins 58 971-75. Han, Q.; Fang, J.; Li, J. (2002) 3-Hydroxykynurenine transaminase identity with alanine glyoxylate transaminase. A probable detoxification protein in Aedes aegypti J Biol Chem 277 15781-7.. Han, Q.; Li, J. (2002) Comparative characterization of Aedes 3-hydroxykynurenine transaminase/alanine glyoxylate transaminase and Drosophila serine pyruvate aminotransferase FEBS Lett 527 199-204.. Oda, T.; Miyajima, H.; Suzuki, Y.; Ito, T.; Yokota, S.; Hoshino, M.; Ichiyama, A. (1989) Purification and characterization of the active serine: pyruvate aminotransferase of rat liver mitochondria expressed in Escherichia coli J Biochem (Tokyo) 106 460-7.. Articles on 2.6.1.51 |
| last changed |
2007/11/30 14:25 |
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