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2.6.1.36 a |
| Activity |
2.6.1.36 |
| Description |
L-lysine aminotransferase (family a) |
| Notes |
This family includes L-lysine aminotransferases from gram-positive bacteria. Similar genes also occur in fungi (which indeed are reported to show L-lysine aminotransferase activity) but none of them has been functionally validated. |
| PDB |
2CJH;2CJD;2CIN; |
| PLP Fold Type |
I |
| PLP-dependent Domain |
|
| Number of sequences |
15 |
| Sequences in seed alignment |
|
| Reference sequence |
LAT_MYCTU |
| Domain interval |
38-395 |
| Catalytic site |
300 K |
| | |
|---|
| References |
Hanson, R.L.; Johnston, R.M.; Goldberg, S.L.; Parker, W.L.; Patel, R.N.
(2011) Enzymatic preparation of 5-hydroxy-L-proline, N-Cbz-5-hydroxy-L-proline, and N-Boc-5-hydroxy-L-proline from (α-N-protected)-L-ornithine using a transaminase or an amine oxidase Enzyme Microb Technol. 48 445-53. Mani Tripathi S, Ramachandran R.
(2006) Overexpression, purification and crystallization of lysine epsilon-aminotransferase (Rv3290c) from Mycobacterium tuberculosis H37Rv Acta Crystallogr Sect F Struct Biol Cryst Commun 62 572-5. Mani Tripathi S, Ramachandran R.
(2006) Direct evidence for a glutamate switch necessary for substrate recognition: crystal structures of lysine epsilon-aminotransferase (Rv3290c) from Mycobacterium tuberculosis H37Rv J Mol Biol 362 877-86. Patel R.N., Banerjee A., Nanduri V.B., Goldberg S.L., Johnston R.M., Hanson R.L., McNamee C.G., Brzozowski D.B., Tully T.P., Ko R.Y., LaPorte T.L., Cazzulino D.L., Swaminathan S., Chen C., Parker L.W., Venit J.J. (2000) Biocatalytic preparation of a chiral synthon for a vasopeptidase inhibitor: enzymatic conversion of N-2-[N-phenylmethoxy)carbonyl] L-homocysteinyl]-L-lysine (1-> 1 ')-disulfide to [4S-(4I,7I,10aJ)] 1-octahydro-5-oxo-4-[phenylmethoxy)carbonyl]amino]-7H-pyrido-[2,1-b] [1,3]thiazepine-7-carboxylic acid methyl ester by a novel L-lysine epsilon-aminotransferase
Enzyme Microb Tech 27 376-389 . Coque, J. J.; Liras, P.; Laiz, L.; Martin, J. F. (1991) A gene encoding lysine 6-aminotransferase, which forms the beta-lactam precursor alpha-aminoadipic acid, is located in the cluster of cephamycin biosynthetic genes in Nocardia lactamdurans J Bacteriol 173 6258-64. Tobin, M.B.; Kovacevic, S.; Madduri, K.; Hoskins, J.A.; Skatrud, P.L.; Vining, L.C.; Stuttard, C.; Miller, J.R. (1991) Localization of the lysine epsilon-aminotransferase (lat) and delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase (pcbAB) genes from Streptomyces clavuligerus and production of lysine epsilon-aminotransferase activity in Escherichia coli J Bacteriol 173 6223-9. |
| last changed |
2016/10/04 14:58 |
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