Literature summary for 1.2.1.95 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 .

Cloned(Commentary)

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

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

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

Natural Substrates/ Products (Substrates)

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

Organism	UniProt	Comment	Textmining
Gelatoporia subvermispora	A0A0S2LUS1	-	-

Purification (Commentary)

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

Substrates and Products (Substrate)

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

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

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

Cofactor

Cofactor	Comment	Organism	Structure
ATP	required	Gelatoporia subvermispora
NADPH	-	Gelatoporia subvermispora

General Information

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