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 |
Synechococcus sp. |
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