Sandbox Reserved 1665: Difference between revisions
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The biochemical activity of AldC from PtoDC3000 is consistent with the traditional role of aldehyde dehydrogenases as metabolic clean-up enzymes that convert reactive aldehydes into less active carboxylates. | The biochemical activity of AldC from PtoDC3000 is consistent with the traditional role of aldehyde dehydrogenases as metabolic clean-up enzymes that convert reactive aldehydes into less active carboxylates. | ||
== Other important features == | == Other important features == | ||
Ald C shared 30-40% of amino acid residues as AldA and Ald B. | |||
In the AldC crystal structure, Phe 456 pie stacks with Tyr 468, which forms an interaction network with Tyr 163 and Trp 450. | |||
The adenine ring of NAD1 is mainly stabilized by multiple van der Waals interactions with Pro216, Ile233, Leu242, and Val243,along with a hydrogen bond with a water molecule in an apolar pocket. As with nicotinamide-ribose binding, polar interactions between the adenine-ribose ring and the side-chains of Lys182 and Glu185 contribute to NAD1 binding. | |||
