EC Number   |
Reaction |
Reference |
|---|
    2.6.1.62 | S-adenosyl-L-methionine + 8-amino-7-oxononanoate = S-adenosyl-4-(methylsulfanyl)-2-oxobutanoate + 7,8-diaminononanoate |
double displacement or ping pong reaction mechanism |
661370 |
| 2.6.1.62 | S-adenosyl-L-methionine + 8-amino-7-oxononanoate = S-adenosyl-4-(methylsulfanyl)-2-oxobutanoate + 7,8-diaminononanoate |
enzyme shows a Ping Pong Bi Bi kinetic mechanism with strong substrate inhibition |
-, 673564 |
| 2.6.1.62 | S-adenosyl-L-methionine + 8-amino-7-oxononanoate = S-adenosyl-4-(methylsulfanyl)-2-oxobutanoate + 7,8-diaminononanoate |
ping pong kinetics, reaction mechanism, via a enzyme-pyridoxamine phosphate, a quinonoid intermediate |
663002 |
| 2.6.1.62 | S-adenosyl-L-methionine + 8-amino-7-oxononanoate = S-adenosyl-4-(methylsulfanyl)-2-oxobutanoate + 7,8-diaminononanoate |
ping-pong mechanism |
637092 |
| 2.6.1.62 | S-adenosyl-L-methionine + 8-amino-7-oxononanoate = S-adenosyl-4-(methylsulfanyl)-2-oxobutanoate + 7,8-diaminononanoate |
reaction mechanism analysis, via a enzyme-pyridoxamine phosphate, a S-adenosyl-L-methionine quinonoid intermediate, the substrate structure is a major determinant of the thermodynamic and/or kinetic accessibility of the quinonoid and ketimine intermediates |
660565 |
| 2.6.1.62 | S-adenosyl-L-methionine + 8-amino-7-oxononanoate = S-adenosyl-4-(methylsulfanyl)-2-oxobutanoate + 7,8-diaminononanoate |
reaction mechanism, substrate binding structure, detailed reversible aminotransferase half-reaction, overview, residues Tyr17, Asp147, and conserved Tyr144 and Arg253 are important for catalysis |
661088 |
| 2.6.1.62 | S-adenosyl-L-methionine + 8-amino-7-oxononanoate = S-adenosyl-4-(methylsulfanyl)-2-oxobutanoate + 7,8-diaminononanoate |
structural basis for reaction mechanism |
661047 |
