Q2TW47 · REDAM_ASPOR
- ProteinNADPH-dependent reductive aminase
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids295 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
NADPH-dependent reductive aminase that catalyzes the reductive coupling of a broad set of carbonyl compounds with a variety of primary and secondary amines (Ref.2). Possesses remarkably high activity for the reductive amination of ketones and amines, often with high stereoselectivity and in some cases with ketone:amine ratios as low as 1:1 (Ref.2). The cofactor NADPH, the carbonyl compound and the amine are added to the enzyme in that sequence, followed by the release of product, NADP+ being released at last (Ref.2). RedAm is also able to act in the reverse, oxidative direction and exhibits activity in the dehydrogenation of amines to yield imines (Ref.2). The highest activity is found for 1-methyl-tetrahydroquinoline and acyclic amines are also found to be transformed (Ref.2).
Cofactor
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
0.12 mM | NADPH | with cyclohexanone methylamine as saturated substrates | ||||
2.13 mM | cyclohexanone | with NADPH methylamine as saturated substrates | ||||
8.23 mM | methylamine (with cyclohexanone and NADPH as saturated substrates) | |||||
1.9 mM | cyclohexanone | with NADPH propargylamine as saturated substrates | ||||
2.31 mM | cyclohexanone | with NADPH allylamine as saturated substrates | ||||
2.06 mM | cyclohexanone | with NADPH pyrrolidine as saturated substrates | ||||
1.9 mM | cyclohexanone | with NADPH benzylamine as saturated substrates | ||||
2.15 mM | cyclohexanone (with NADPH and ammonia as saturated substrates) | |||||
0.04 mM | indanone | with NADPH propargylamine as saturated substrates | ||||
0.94 mM | 4-phenyl-2-butanone | with NADPH propargylamine as saturated substrates | ||||
0.09 mM | acetophenone | with NADPH propargylamine as saturated substrates | ||||
12.2 mM | 2-allyl cyclohexanone | with NADPH propargylamine as saturated substrates | ||||
1.92 mM | 1-tetralone | with NADPH propargylamine as saturated substrates | ||||
5.4 mM | propargylamine (with cyclohexanone and NADPH as saturated substrates) | |||||
15.33 mM | isopropylamine (with cyclohexanone and NADPH as saturated substrates) | |||||
25.12 mM | pyrrolidine (with cyclohexanone and NADPH as saturated substrates) | |||||
0.08 mM | NADP+ | with N-methylcyclohexylamine as saturated substrate | ||||
11.61 mM | N-methylcyclohexylamine (with NADP+ as saturated substrate) |
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | NADP binding | |
Molecular Function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameNADPH-dependent reductive aminase
- EC number
- Short namesRedAm
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Aspergillus > Aspergillus subgen. Circumdati
Accessions
- Primary accessionQ2TW47
Proteomes
Organism-specific databases
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 169 | Leads to a 30-fold decrease in reductive aminase activity. | ||||
Sequence: D → A or N | ||||||
Mutagenesis | 177 | Leads to a 200-fold decrease in reductive aminase activity. | ||||
Sequence: Y → A | ||||||
Mutagenesis | 210 | Displays a dramatic selectivity switch to yield the antipodal (S)-amine products with a variety of amine nucleophiles. | ||||
Sequence: W → A or S | ||||||
Mutagenesis | 240 | Displays significant improvements in (R)-selectivity for most substrates. | ||||
Sequence: Q → A or S |
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-18 | |||||
Sequence: MSKHIGIFGLGAMGTALA | ||||||
Chain | PRO_0000441988 | 19-295 | NADPH-dependent reductive aminase | |||
Sequence: AKYLEHGYKTSVWNRTTAKAIPLVEQGAKLASTISEGVNANDLIIICLLNNQVVEDALRDALQTLPSKTIVNLTNGTPNQARKLADFVTSHGARYIHGGIMAVPTMIGSPHAVLLYSGESLELFQSIESHLSLLGMSKYLGTDAGSASLHDLALLSGMYGLFSGFLHAVALIKSGQDTSTTATGLLPLLTPWLSAMTGYLSSIAKQIDDGDYATQGSNLGMQLAGVENIIRAGEEQRVSSQMILPIKALIEQAVGEGHGGEDLSALIEYFKVGKNVD |
Interaction
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length295
- Mass (Da)31,155
- Last updated2006-01-24 v1
- Checksum0F3524398534D0AB
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
BA000056 EMBL· GenBank· DDBJ | BAE66526.1 EMBL· GenBank· DDBJ | Genomic DNA |