EC Number |
Reaction |
Reference |
---|
5.4.3.8 | L-glutamate 1-semialdehyde = 5-aminolevulinate |
catalytic mechanism via external aldimine and Gem-diamine intermediates, overview |
727125 |
5.4.3.8 | L-glutamate 1-semialdehyde = 5-aminolevulinate |
enzyme shows an active-site gating loop, which undergoes a dramatic conformational change during catalysis, that is simultaneously open in one subunit and closed in the other. Loop movement requires a beta-sheet-to-alpha-helix transition to assume the closed conformation, thus facilitating transport of substrate toward, and concomitantly forming, an integral part of the active site. The accompanying intersubunit cross-talk controls negative cooperativity between the allosteric pair |
682509 |
5.4.3.8 | L-glutamate 1-semialdehyde = 5-aminolevulinate |
intermolecular transamination occurs during conversion of (S)-4-amino-5-oxopentanoate to 5-amino-4-oxopentanoate |
3424 |
5.4.3.8 | L-glutamate 1-semialdehyde = 5-aminolevulinate |
mechanism |
3442 |
5.4.3.8 | L-glutamate 1-semialdehyde = 5-aminolevulinate |
ping-pong bi-bi mechanism in which 4,5-diaminovalerate is the second substrate and 4,5-dioxovalerate is an alternative first substrate |
3441 |
5.4.3.8 | L-glutamate 1-semialdehyde = 5-aminolevulinate |
the catalytic mechanism includes enzyme-bound diaminovalerate as a central intermediate |
3439 |
5.4.3.8 | L-glutamate 1-semialdehyde = 5-aminolevulinate |
wild-type enzyme and gabaculine-resistant mutant enzyme use a ping-pong bi-bi mechanism in which 4,5-diaminovalerate is a likely intermediate |
3430 |