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Literature summary extracted from

  • Kalb, D.; Lackner, G.; Rappe, M.; Hoffmeister, D.
    Activity of alpha-aminoadipate reductase depends on the N-terminally extending domain (2015), ChemBioChem, 16, 1426-1430 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.2.1.95 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

EC Number Protein Variants Comment Organism
1.2.1.95 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]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.2.1.95 132600
-
 about, recombinant truncated enzyme, sequence calculation Gelatoporia subvermispora

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.2.1.95 L-2-aminoadipate + NADPH + H+ + ATP Gelatoporia subvermispora
-
 (S)-2-amino-6-oxohexanoate + NADP+ + AMP + diphosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.2.1.95 Gelatoporia subvermispora A0A0S2LUS1
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.2.1.95 recombinant His-tagged truncated enzyme mutants from Escherichia coli strain KRX by nickel affinity chromatography and gel filtration Gelatoporia subvermispora

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.1.95 L-2-aminoadipate + NADPH + H+ + ATP
-
 Gelatoporia subvermispora (S)-2-amino-6-oxohexanoate + NADP+ + AMP + diphosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
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 depends on the N-terminally extending domain Gelatoporia subvermispora

Synonyms

EC Number Synonyms Comment Organism
1.2.1.95 alpha-aminoadipate reductase
-
 Gelatoporia subvermispora
1.2.1.95 L-alpha-aminoadipic acid reductase
-
 Gelatoporia subvermispora
1.2.1.95 LYS2
-
 Gelatoporia subvermispora
1.2.1.95 Nps3
-
 Gelatoporia subvermispora

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.1.95 ATP required Gelatoporia subvermispora
1.2.1.95 NADPH
-
 Gelatoporia subvermispora

General Information

EC Number General Information Comment Organism
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 Gelatoporia subvermispora
1.2.1.95 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
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 Gelatoporia subvermispora