Cloned (Comment) | Organism |
---|---|
recombinant expression of N-terminally His6-tagged truncated NPS3 enzyme mutant lacking the 247 amino acids of the N-terminal ADA domain from pET21a-based expression plasmid pMR1, recombinant expression of N-terminally His6-tagged truncated NPS3 enzyme mutant lacking the 152 amino acids of the N-terminal ADA domain from expression plasmid pDK22, and recombinant expression of the 102.8 kDa ADA-A didomain (lacking the C-terminal 515 amino acids) and the 75.7 kDa standalone NPS3A domain, respectively, in which the first 247 and terminal 515 amino acids are absent, from plasmids pDK24 and pDK25, both based on expression vector pET28a, all in Escherichia coli strain KRX | Gelatoporia subvermispora |
Protein Variants | Comment | Organism |
---|---|---|
additional information | truncated enzymes based on NPS3, the L-alpha-aminoadipic acid reductase of the basidiomycete Ceriporiopsis subvermispora, lacking the ADA domain either partially or entirely are tested for activity in vitro, together with an ADA-adenylation didomain and the ADA domain-less adenylation domain | Gelatoporia subvermispora |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
132600 | - |
about, recombinant truncated enzyme, sequence calculation | Gelatoporia subvermispora |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-2-aminoadipate + NADPH + H+ + ATP | Gelatoporia subvermispora | - |
(S)-2-amino-6-oxohexanoate + NADP+ + AMP + diphosphate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Gelatoporia subvermispora | A0A0S2LUS1 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant His-tagged truncated enzyme mutants from Escherichia coli strain KRX by nickel affinity chromatography and gel filtration | Gelatoporia subvermispora |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-2-aminoadipate + NADPH + H+ + ATP | - |
Gelatoporia subvermispora | (S)-2-amino-6-oxohexanoate + NADP+ + AMP + diphosphate | - |
? |
Subunits | Comment | Organism |
---|---|---|
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 depends on the N-terminally extending domain | Gelatoporia subvermispora |
Synonyms | Comment | Organism |
---|---|---|
alpha-aminoadipate reductase | - |
Gelatoporia subvermispora |
L-alpha-aminoadipic acid reductase | - |
Gelatoporia subvermispora |
LYS2 | - |
Gelatoporia subvermispora |
Nps3 | - |
Gelatoporia subvermispora |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | required | Gelatoporia subvermispora | |
NADPH | - |
Gelatoporia subvermispora |
General Information | Comment | Organism |
---|---|---|
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 | Gelatoporia subvermispora |
additional information | 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 | Gelatoporia subvermispora |
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 | Gelatoporia subvermispora |