Search Results
Overview
| Uniprot ID | P30837 |
|---|---|
| Protein Name | Aldehyde dehydrogenase family 1 member B1, mitochondrial |
| Gene Name | ALDH1B1 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 155 | YFAGWADKWHGKTIP |
| 272 | EVGHLIQKAAGDSNL |
| 280 | AAGDSNLKRVTLELG |
| 347 | VEKAKQRKVGNPFEL |
| 379 | GYIQLGQKEGAKLLC |
| 383 | LGQKEGAKLLCGGER |
| 426 | GPVQPLFKFKKIEEV |
| 429 | QPLFKFKKIEEVVER |
| 500 | ELGEDGLKAYTEVKT |
| 506 | LKAYTEVKTVTIKVP |
| 52 | WQDAVSKKTFPTVNP |
Function
Broad specificity, mitochondrial aldehyde dehydrogenase that could play a role in the detoxification of alcohol-derived acetaldehyde and other aldehydes (PubMed:20616185, PubMed:25413692, PubMed:35788181). Shows an absolute preference for NAD(+) as no activity is detected with NADP(+) (PubMed:20616185, PubMed:25413692). Has a high affinity and catalytic efficiency toward aliphatic medium-chain saturated aldehydes relative to short-chain and aromatic aldehydes in vitro (PubMed:20616185). Also capable of metabolizing products of lipid peroxidation, namely 4-hydroxynon-2-enal(4-HNE) and malonaldehyde (MDA) but with lower catalytic efficiency (PubMed:20616185). In vitro, it can also display a nitroglycerin reductase activity (PubMed:25413692). Has also an esterase activity in vitro, but this may be not physiologically relevant in vivo (PubMed:20616185)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0005759 | mitochondrial matrix |
| Cellular Component | GO:0005739 | mitochondrion |
| Molecular Function | GO:0004029 | aldehyde dehydrogenase (NAD+) activity |
| Molecular Function | GO:0051287 | NAD binding |
| Biological Process | GO:0006081 | aldehyde metabolic process |
| Biological Process | GO:0005975 | carbohydrate metabolic process |
| Biological Process | GO:0006068 | ethanol catabolic process |
Reference
[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.
[2] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.