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B6db families: 2.6.1.36.a

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
Domain alignment
Domain hmm
Fold type I

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) 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.

 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.

 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.

Articles on 2.6.1.36.a
last changed 2016/10/04 14:58

B6db families