|
|
2.6.1.2 a |
Activity |
2.6.1.2 |
Description |
Alanine aminotransferase (family a) |
Notes |
This family includes archaeal enzymes, similar to the prototypical alanine aminotransferase from Pyrococcus furiosus, and enzymes from bacteria, like the rather broad-specificity AlaT from C. glutamicum and the preliminarly characterized AlaA from E. coli. |
PDB |
1XI9;4CVQ; |
PLP Fold Type |
I |
PLP-dependent Domain |
|
Number of sequences |
30 |
Sequences in seed alignment |
|
Reference sequence |
AAF65616 |
Domain interval |
30-388 |
Catalytic site |
237 K |
| |
References |
Jansen RS, Mandyoli L, Hughes R, Wakabayashi S, Pinkham JT, Selbach B, Guinn KM, Rubin EJ, Sacchettini JC, Rhee KY (2020) Aspartate aminotransferase Rv3722c governs aspartate-dependent nitrogen metabolism in Mycobacterium tuberculosis Nat Commun 11 1960. 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. Kim SH, Schneider BL, Reitzer L.
(2010) Genetics and regulation of the major enzymes of alanine synthesis in Escherichia coli J Bacteriol 192 5304-11. Marienhagen J, Kennerknecht N, Sahm H, Eggeling L. (2005) Functional analysis of all aminotransferase proteins inferred from the genome sequence of Corynebacterium glutamicum J Bacteriol 187 7639-46. Ward, D.E.; Kengen, S.W.; van Der Oost, J.; de Vos, W.M. (2000) Purification and characterization of the alanine aminotransferase from the hyperthermophilic Archaeon pyrococcus furiosus and its role in alanine production
J Bacteriol 182 2559-2566. Articles on 2.6.1.2.a |
last changed |
2017/11/15 10:31 |
|