B6db activities : 2_6_1

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	2.6.1.62
Description	Adenosylmethionine--8-amino-7-oxononanoate aminotransferase.
Alternative names	7,8-diamino-pelargonic acid aminotransferase. 7,8-diaminononanoate aminotransferase. DAPA aminotransferase. Diaminopelargonate synthase. Diaminopelargonic acid synthase
Catalyzed reaction	S-adenosyl-L-methionine + 8-amino-7-oxononanoate = S-adenosyl-4- methylthio-2-oxobutanoate + 7,8-diaminononanoate.
Cofactor	Pyridoxal-phosphate.
Comments	-!- S-adenosylhomocysteine can also act as donor.
	The enzyme from Bacillus subtilis does not use S-adenosyl-L-methionine as the amino group donor; apparently it requires L-lysine, which may grant its inclusion in a different enzyme activity.
Prosite	PROSITE; PDOC00519;
PDB	1QJ5; 1QJ3; 1DTY;
Organisms	-Bacteria -Fungi
Family	2.6.1.62 (27)

Links	Enzyme (activities) 2.6.1.62 BRENDA (activities) 2.6.1.62 KEGG (pathways) 2.6.1.62 PLPMDB (PLP mutants) 2.6.1.62

References	Bhor, V.M.; Dev, S.; Vasanthakumar, G.R.; Surolia, A. (2006) Spectral and kinetic characterization of 7,8-diaminopelargonic acid synthase from Mycobacterium tuberculosis IUBMB Life 58 225-33. Mann S, Ploux O. (2006) 7,8-Diaminoperlargonic acid aminotransferase from Mycobacterium tuberculosis, a potential therapeutic target. Characterization and inhibition studies FEBS J 273 4778-89. Van Arsdell, SW.; Perkins, J.B.; Yocum, R.R.; Luan, L.; Howitt, C.L.; Prasad Chatterjee, N.; Pero, J.G. (2005) Removing a bottleneck in the Bacillus subtilis biotin pathway: bioA utilizes lysine rather than S-adenosylmethionine as the amino donor in the KAPA-to-DAPA reaction Biotechnol Bioeng 91 75-83. Eliot, A. C.; Sandmark, J.; Schneider, G.; Kirsch, J. F. (2002) The dual-specific active site of 7,8-diaminopelargonic acid synthase and the effect of the R391A mutation Biochemistry 41 12582-9.. Kack, H.; Sandmark, J.; Gibson, K.; Schneider, G.; Lindqvist, Y. (1999) Crystal structure of diaminopelargonic acid synthase: evolutionary relationships between pyridoxal-5'-phosphate-dependent enzymes J Mol Biol 291 857-76.. Articles on 2.6.1.62

last changed	2007/12/05 20:10

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