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2.6.1.66 a |
Activity |
2.6.1.66 |
Description |
Valine--pyruvate aminotransferase (family a) |
Notes |
This group of enzymes play a minor role in the bacterial biosynthesis of valine.
The family has been built starting from the only functionally characterized gene (E. coli).
Note that the enzymes in this family are fold-type I, whereas the enzymes in the 2.6.1.42 family (branched-chain amino acid aminotransferase) are are fold-type IV. This may represent yet another instance of convergent evolution in PLP-dependent enzymes.
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PLP Fold Type |
I |
PLP-dependent Domain |
|
Number of sequences |
13 |
Sequences in seed alignment |
|
Domain interval |
30-405 |
Catalytic site |
249 |
| |
References |
Peña-Soler E, Fernandez FJ, López-Estepa M, Garces F, Richardson AJ, Quintana JF, Rudd KE, Coll M, Vega MC
(2014) Structural analysis and mutant growth properties reveal distinctive enzymatic and cellular roles for the three major L-alanine transaminases of Escherichia coli PLoS One 9 e102139. Wang, M. D.; Liu, L.; Wang, B. M.; Berg, C. M. (1987) Cloning and characterization of the Escherichia coli K-12 alanine- valine transaminase (avtA) gene J Bacteriol 169 4228-34. Articles on 2.6.1.66.a |
last changed |
2019/06/19 15:33 |
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