P37685 · ALDB_ECOLI
- ProteinAldehyde dehydrogenase B
- GenealdB
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids512 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the NADP+-dependent oxidation of diverse aldehydes to their corresponding carboxylic acids, with a preference for acetaldehyde and chloroacetaldehyde (PubMed:15659684).
May play a role in detoxifying aldehydes present during stationary phase (Probable). Cannot use NAD+ instead of NADP+ as the electron acceptor. To a lesser extent is also able to oxidize propionaldehyde (propanal), benzaldehyde, mafosfamide, and 4-hydroperoxycyclophosphamide. Does not use either glyceraldehyde or glycolaldehyde as substrates (PubMed:15659684).
May play a role in detoxifying aldehydes present during stationary phase (Probable). Cannot use NAD+ instead of NADP+ as the electron acceptor. To a lesser extent is also able to oxidize propionaldehyde (propanal), benzaldehyde, mafosfamide, and 4-hydroperoxycyclophosphamide. Does not use either glyceraldehyde or glycolaldehyde as substrates (PubMed:15659684).
Catalytic activity
- an aldehyde + H2O + NADP+ = a carboxylate + 2 H+ + NADPH
- chloroacetaldehyde + H2O + NADP+ = chloroacetate + 2 H+ + NADPH
- H2O + NADP+ + propanal = 2 H+ + NADPH + propanoate
Activity regulation
Magnesium increases enzyme activity with various substrates.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
2.5 μM | acetaldehyde | |||||
3.6 μM | chloroacetaldehyde | |||||
5.8 μM | propionaldehyde | |||||
56.8 μM | benzaldehyde | |||||
900 μM | 4-hydroperoxycyclophosphamide | |||||
65 μM | NADP |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
2 μmol/min/mg | with acetaldehyde as substrate | ||||
3.3 μmol/min/mg | with chloroacetaldehyde as substrate | ||||
1 μmol/min/mg | with propionaldehyde as substrate | ||||
0.6 μmol/min/mg | with benzaldehyde as substrate | ||||
0.2 μmol/min/mg | with 4-hydroperoxycyclophosphamide |
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 268 | |||||
Sequence: E | ||||||
Active site | 307 | |||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | aldehyde dehydrogenase (NAD+) activity | |
Molecular Function | aldehyde dehydrogenase (NADP+) activity | |
Molecular Function | oxidoreductase activity | |
Biological Process | DNA damage response | |
Biological Process | response to ethanol |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAldehyde dehydrogenase B
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionP37685
- Secondary accessions
Proteomes
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 197 | Less than 10% of wild-type acetaldehyde dehydrogenase activity. | ||||
Sequence: R → E |
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000056565 | 1-512 | Aldehyde dehydrogenase B | |||
Sequence: MTNNPPSAQIKPGEYGFPLKLKARYDNFIGGEWVAPADGEYYQNLTPVTGQLLCEVASSGKRDIDLALDAAHKVKDKWAHTSVQDRAAILFKIADRMEQNLELLATAETWDNGKPIRETSAADVPLAIDHFRYFASCIRAQEGGISEVDSETVAYHFHEPLGVVGQIIPWNFPLLMASWKMAPALAAGNCVVLKPARLTPLSVLLLMEIVGDLLPPGVVNVVNGAGGVIGEYLATSKRIAKVAFTGSTEVGQQIMQYATQNIIPVTLELGGKSPNIFFADVMDEEDAFFDKALEGFALFAFNQGEVCTCPSRALVQESIYERFMERAIRRVESIRSGNPLDSVTQMGAQVSHGQLETILNYIDIGKKEGADVLTGGRRKLLEGELKDGYYLEPTILFGQNNMRVFQEEIFGPVLAVTTFKTMEEALELANDTQYGLGAGVWSRNGNLAYKMGRGIQAGRVWTNCYHAYPAHAAFGGYKQSGIGRETHKMMLEHYQQTKCLLVSYSDKPLGLF |
Proteomic databases
Expression
Induction
Is repressed by Fis. Positively regulated by RpoS and Crp. Induced by ethanol. Expression is maximally induced during the transition from exponential phase to stationary phase.
Structure
Sequence
- Sequence statusComplete
- Length512
- Mass (Da)56,306
- Last updated1995-11-01 v2
- ChecksumE673C34340DF68CD
Sequence caution
Mass Spectrometry
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
L40742 EMBL· GenBank· DDBJ | AAC36939.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U00039 EMBL· GenBank· DDBJ | AAB18565.1 EMBL· GenBank· DDBJ | Genomic DNA | Different initiation | |
U00096 EMBL· GenBank· DDBJ | AAC76612.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP009048 EMBL· GenBank· DDBJ | BAE77705.1 EMBL· GenBank· DDBJ | Genomic DNA |