EC Number   |
General Information |
Reference |
|---|
    1.2.1.5 | evolution |
aldehyde dehydrogenase 1A1 (ALDH3A1) is a member of the aldehyde dehydrogenase superfamily that oxidizes aldehydes to their corresponding acids, reactions that are coupled to the reduction of NAD(P)+ to NAD(P)H |
763529 |
| 1.2.1.5 | evolution |
physiological function of the regulatory mechanism for NAD+-dependent ALDHs via cysteine oxidation and vicinal disulfide formation using yeast Ald4 (EC 1.2.1.5) and Ald6. While both enzymes convert aldehyde to acetate and are important for yeast ethanol metabolism, they differ in cofactor utilization and the regulatory mechanism. Ald4 prefers NAD+ while Ald6 is NADP+-dependent. The regulation of activity via disulfide formation between the catalytic cysteine and adjacent regulatory cysteine is only present in the NAD+-dependent Ald4, but not in the NADP+-dependent Ald6. This regulatory mechanism for Ald4 ensures the fast inactivation of Ald4 upon oxidation and the reactivation upon reduction |
-, 762546 |
| 1.2.1.5 | metabolism |
ALDH1A1 and ALDH3A1 have the same GSH/DHLA-dependent NAD+-reduction activity |
763529 |
| 1.2.1.5 | metabolism |
regulation of activity via disulfide formation between the catalytic cysteine and adjacent regulatory cysteine is only present in the NAD+-dependent Ald4, but not in the NADP+-dependent Ald6. This regulatory mechanism for Ald4 ensures the fast inactivation of Ald4 upon oxidation and the reactivation upon reduction. Isozymes Ald4, Ald5 and Ald6 play important roles in yeast survival when using ethanol as the carbon source. Both Ald4 and Ald5 preferentially use NAD+ as cofactors in cells while Ald6 only utilizes NADP+. With ethanol as the carbon source, the pentose phosphate pathway, a major pathway to generate NADPH, is shut down as the substrate is not available. Instead of cysteine, Ald6 has a serine next to the active site cysteine. As the regulatory cysteine inactivates Ald4 during oxidative stress, Ald6 remains active while Ald4 is inactivated, thus diverting all acetaldehyde to Ald6 for the production of NADPH. This way, yeast can survive oxidative stress better |
-, 762546 |
| 1.2.1.5 | more |
enzyme structure comparisons, overview |
763136 |
| 1.2.1.5 | physiological function |
Ald4 converts aldehyde to acetate and are important for yeast ethanol metabolism |
-, 762546 |
| 1.2.1.5 | physiological function |
aldehyde dehydrogenase 3A1 increases NADH levels and promotes tumor growth via glutathione/dihydrolipoic acid-dependent NAD+ reduction. ALDH3A1 can also use glutathione (GSH) and dihydrolipoic acid (DHLA) as electron donors to reduce NAD+ to NADH. The GSH/DHLA-dependent NAD+-reduction activity of ALDH1A1 is not affected by the aldehyde dehydrogenase inhibitor or by mutation of the residues in its aldehyde-binding pocket. It is thus a distinct biochemical reaction from the classic aldehyde-dehydrogenase activity catalyzed by ALDH3A1. The GSH/DHLA-dependent NAD+-reduction activity of ALDH3A1 can decrease cellular NAD+/NADH ratio and promote tumor growth |
763529 |
| 1.2.1.5 | physiological function |
ALDH9, ALDH13, and ALDH17 genes involve the function of drought stress, acid tolerance, and pathogens infection |
725085 |
| 1.2.1.5 | physiological function |
enzyme ALDH is responsible for catalytic detoxification from aldehyde-induced cytotoxicity. ALDH has been reported to be involved in pseudo-ligandin properties both for nonaldehydic endobiotics and xenobiotics |
762793 |
| 1.2.1.5 | physiological function |
enzyme BcALDH is an atypical aldehyde dehydrogenase having bidirectional oxidizing and reducing activities |
763136 |
