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Primary Information | |
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| BoMiProt ID | Bomi213 |
| Protein Name | Aldehyde dehydrogenase, mitochondrial |
| Organism | Bos taurus |
| Uniprot ID | P20000 |
| Milk Fraction | MFGM |
| Ref Sequence ID | NP_001068835.1 |
| Aminoacid Length | 520 |
| Molecular Weight | 56653 |
| FASTA Sequence | Download |
| Gene Name | ALDH2 |
| Gene ID | 508629 |
| Protein Existence Status | Reviewed: Experimental evidence at protein level |
Secondary Information | |
| Protein Function | represent large family members of NAD(P)+-dependent dehydrogenases responsible for the irreversible metabolism of many endogenous and exogenous aldehydes to the corresponding acids; catalyzes the oxidation of acetaldehyde to acetate during ethanol metabolism; |
| Biochemical Properties | cytosolic and mitochondrial forms, designated as ALDH1 and ALDH2, are both tetrameric with individual subunits comprising 499–500 amino acids and they share 68% sequence identity with each other; vA transition to full-site reactivity, however, occurs at elevated pH or in the presence of Mg2+; low Km enzyme responsible for the metabolism of acetaldehyde and lipid peroxides such as malondialdehyde and 4-hydroxynonenal, both of which are highly reactive and toxic; inhibition of ALDH2 would lead to elevated levels of acetaldehyde and other reactive lipid peroxides; require NAD+ as a cofactor |
| Significance in milk | in lactating rodent mammary epicelial cells, upregulation of aldehyde dehydrogenase which is associated with the breakdown of acetate and beta-hydroxy butyrate to provide additional sources of acetyl CoA, a substrate for the TCA cycle and subsequent ATP synthesis |
| PTMs | cytosolic ALDH1A1, mitochondrial ALDH2, and other isozymes such as ALDH5A1 and ALDH6A1 were oxidatively-modified in rats exposed to alcohol; protein kinases such as protein kinase Cε (PKCε) can phosphorylate and activate mitochondrial ALDH2 - Thr185, Thr412 and possibly Ser279 of ALDH2 could be phosphorylated by PKCε, resulting in ALDH2 activation; ALDH2 could be inhibited through protein nitration based on the recent data where GTN promotes nitration signaling; ALDH2 activity was mildly inhibited by NO or hydrogen peroxide in the experimental conditions, but was markedly inhibited by incubation with peroxynitrite |
| Site(s) of PTM(s) N-glycosylation, O-glycosylation, Phosphorylation | |
| SCOP | Class : Alpha and beta proteins (a/b) Fold : ALDH-like Superfamily : ALDH-like Family : ALDH-like Domain Name : 1AG8 A:8-500 |
| CATH | Matched CATH superfamily 3.40.605.10 3.40.309.10 |
| Predicted Disorder Regions | NA |
| DisProt Annotation | |
| TM Helix Prediction | No TM helices |
| Significance of PTMs | regulates activation and deactivation of the enzyme |
| PDB ID | 1A4Z, 1AG8, |
| Bibliography | 1. Jansen, S., Collins, A., Golden, L., Sokolova, O., & Goode, B. L. (2014). Structure and mechanism of mouse cyclase-associated protein (CAP1) in regulating actin dynamics. Journal of Biological Chemistry, 289(44), 30732–30742. https://doi.org/10.1074/jbc.M114.601765. 2. Yuan, X., Zhen, Z., Zhang, M., Yu, Y., Gao, X., & Ao, J.-X. (2019). Cyclase-associated protein 1 is a key negative regulator of milk synthesis and proliferation of bovine mammary epithelial cells. Cell Biochemistry and Function, 37(3), 185–192. https://doi.org/10.1002/cbf.3387. |