B6db activities : 2_6_1

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	2.6.1.36
Description	L-lysine aminotransferase
Alternative names	L-Lysine 6-aminotransferase; Lysine-epsilon aminotransferase; L-Lysine 6-transaminase.
Catalyzed reaction	L-lysine + 2-oxoglutarate = 2-aminoadipate 6-semialdehyde + L-glutamate.
Cofactor	Pyridoxal-phosphate.
Comments	-!- The product (allysine) is converted into the intramolecularly dehydrated form, 1-piperideine 6-carboxylate.
	The enzyme is involved in L-lysine catabolism. In actinomycetes, this enzyme is specific to the first step of the beta-lactam antibiotic biosynthetic pathway. An enzyme from Sphingomonas paucimobilis has been cloned (see Patel et al., 2000) but the sequence is not available from current primary databases.
PDB	2CJH; 2CJD; 2CIN;
Organisms	-Eubacteria -Fungi
Family	2.6.1.36_a (0) 2.6.1.36_b (0)

Links	Enzyme (activities) 2.6.1.36 BRENDA (activities) 2.6.1.36 KEGG (pathways) 2.6.1.36 PLPMDB (PLP mutants) 2.6.1.36

References	Duan X, Li Y, Du Q, Huang Q, Guo S, Xu M, Lin Y, Liu Z, Xie J (2016) Mycobacterium Lysine ε-aminotransferase is a novel alarmone metabolism related persister gene via dysregulating the intracellular amino acid level Sci Rep 6 19695. 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. Fujii, T.; Narita, T.; Agematu, H.; Agata, N.; Isshiki, K. (2000) Characterization of L-lysine 6-aminotransferase and its structural gene from Flavobacterium lutescens IFO3084 J Biochem (Tokyo) 128 391-7. 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

last changed	2019/01/07 14:42

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