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|
2.6.1.1 e |
Activity |
2.6.1.1 |
Description |
Aspartate aminotransferase (family e) |
Notes |
This family includes enzymes from Archaea and from Eubacteria. The family is most strictly related to families 2.6.1.45 and 2.6.1.51 (serine-glyoxylate and alanine glyoxylate aminotransferases). |
PLP Fold Type |
I |
PLP-dependent Domain |
|
Number of sequences |
13 |
Sequences in seed alignment |
|
Reference sequence |
BAA05953 |
Domain interval |
4-352 |
Catalytic site |
190 K |
| |
References |
Lee DK, Hwang JY, Cho HY, Kong KH (2009) A Thermostable Aspartate Aminotransferase from Aeropyrum pernix K1 Bull. Korean Chem. Soc. 30 3143–3146. Koma D, Sawai T, Hara R, Harayama S, Kino K. (2008) Two groups of thermophilic amino acid aminotransferases exhibiting broad substrate specificities for the synthesis of phenylglycine derivatives Appl Microbiol Biotechnol 79 775-84. Tanaka, T.; Yamamoto, S.; Moriya, T.; Taniguchi, M.; Hayashi, H.; Kagamiyama, H.; Oi, S. (1994) 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 J Biochem (Tokyo) 115 309-17. Articles on 2.6.1.1.e |
last changed |
2018/10/16 12:16 |
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