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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. |
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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; 3WY7; 6ERK; |
| Organisms |
-Eubacteria -Archea -Plants -Fungi |
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Family |
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| 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
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| References |
Bezsudnova EY, Stekhanova TN, Popinako AV, Rakitina TV, Nikolaeva AY, Boyko KM, Popov VO (2018) Diaminopelargonic acid transaminase from Psychrobacter cryohalolentis is active towards (S)-(-)-1-phenylethylamine, aldehydes and α-diketones Appl Microbiol Biotechnol 102 71-80. Fan S, Li DF, Wang DC, Fleming J, Zhang H, Zhou Y, Zhou L, Zhou J, Chen T, Chen G, Zhang XE, Bi L
(2015) Structure and function of Mycobacterium smegmatis 7-keto-8-aminopelargonic acid (KAPA) synthase Int J Biochem Cell Biol 58 71-80. Cobessi D, Dumas R, Pautre V, Meinguet C, Ferrer JL, Alban C
(2012) Biochemical and structural characterization of the Arabidopsis bifunctional enzyme dethiobiotin synthetase-diaminopelargonic acid aminotransferase: evidence for substrate channeling in biotin synthesis Plant Cell 24 1608-25. 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. 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. |
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| last changed |
2019/10/22 12:22 |
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