EC Number   |
General Information |
Reference |
|---|
   1.2.1.95 | malfunction |
enzyme-deficient mutants are defective in the biosynthesis of all known polyketides and nonribosomal peptides and hypersensitive to both iron depletion and oxidative stress. Enzyme disruption reduces germination speed on insect cuticles and results in significant loss of virulence. Enzyme inactivation slightly reduces mycelium hydrophobicity and has no significant effect on conidium hydrophobicity |
-, 763113 |
| 1.2.1.95 | metabolism |
the enzyme is involved in the fungal de novo L-lysine biosynthesis via ATP- and NADPH-dependent reduction of the intermediate L-alpha-aminoadipic acid into L-alpha-aminoadipate 6-semialdehyde as a multifunctional aminoacyl-adenylate-forming reductase, pathway overview |
742278 |
| 1.2.1.95 | more |
the enzyme has a multidomain composition but features a unique domain of elusive function, termed the adenylation activating (ADA) domain, that extends the reductase N-terminally. The activity of alpha-aminoadipate reductase and A domain depends on the N-terminally extending domain. ADA domain sequence comparison and protein interaction analysis, homology modeling, overview |
742278 |
| 1.2.1.95 | physiological function |
L-alpha-aminoadipic acid reductases catalyze the ATP- and NADPH-dependent reduction of L-alpha-aminoadipic acid to the corresponding 6-semialdehyde during fungal L-lysine biosynthesis |
742278 |
