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B6db activities: 2.6.1.62

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 -Eubacteria -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 2010/03/11 16:25

B6db activities