EC Number |
Substrates |
Organism |
Products |
Reversibility |
---|
1.2.1.32 | 2-aminomuconate 6-semialdehyde + NAD+ + H2O |
- |
Burkholderia cepacia |
2-aminomuconate + NADH + H+ |
- |
? |
1.2.1.32 | 2-aminomuconate 6-semialdehyde + NAD+ + H2O |
- |
Bordetella sp. |
2-aminomuconate + NADH + H+ |
- |
? |
1.2.1.32 | 2-aminomuconate 6-semialdehyde + NAD+ + H2O |
- |
Burkholderia cepacia J2315 |
2-aminomuconate + NADH + H+ |
- |
? |
1.2.1.32 | 2-aminomuconate 6-semialdehyde + NAD+ + H2O |
- |
Burkholderia cepacia |
2-aminomuconate + NADH + 2 H+ |
- |
? |
1.2.1.32 | 2-aminomuconate 6-semialdehyde + NAD+ + H2O |
- |
Homo sapiens |
2-aminomuconate + NADH + 2 H+ |
- |
? |
1.2.1.32 | 2-aminomuconate 6-semialdehyde + NAD+ + H2O |
- |
Pseudomonas fluorescens |
2-aminomuconate + NADH + 2 H+ |
- |
? |
1.2.1.32 | 2-aminomuconate 6-semialdehyde + NAD+ + H2O |
enzyme-substrate binding structure and catalytic mechanism, overview. Due to the unstable nature of its substrate 2-aminomuconate 6-semialdehyde, 2-AMS, the activity of AMSDH is detected using a coupled-enzyme assay that employs its upstream partner, alpha-amino beta-carboxymuconate epsilon-semialdehyde decarboxylase (ACMSD), to generate 2-AMS in situ |
Pseudomonas fluorescens |
2-aminomuconate + NADH + 2 H+ |
- |
? |
1.2.1.32 | 2-aminomuconate 6-semialdehyde + NAD+ + H2O |
- |
Pseudomonas fluorescens KU-7 |
2-aminomuconate + NADH + 2 H+ |
- |
? |
1.2.1.32 | 2-aminomuconate 6-semialdehyde + NAD+ + H2O |
enzyme-substrate binding structure and catalytic mechanism, overview. Due to the unstable nature of its substrate 2-aminomuconate 6-semialdehyde, 2-AMS, the activity of AMSDH is detected using a coupled-enzyme assay that employs its upstream partner, alpha-amino beta-carboxymuconate epsilon-semialdehyde decarboxylase (ACMSD), to generate 2-AMS in situ |
Pseudomonas fluorescens KU-7 |
2-aminomuconate + NADH + 2 H+ |
- |
? |
1.2.1.32 | 2-aminomuconate 6-semialdehyde + NAD+ + H2O |
- |
Burkholderia cepacia J2315 |
2-aminomuconate + NADH + 2 H+ |
- |
? |