1.2.1.95: L-2-aminoadipate reductase

This is an abbreviated version!
For detailed information about L-2-aminoadipate reductase, go to the full flat file.

Reaction

Synonyms

AAR, AarA, AasS, alpha-AAR, alpha-aminoadipate delta-semialdehyde synthase, alpha-aminoadipate reductase, L-alpha-aminoadipic acid reductase, Lys1+, LYS2, Nps3

ECTree

     1 Oxidoreductases

         1.2 Acting on the aldehyde or oxo group of donors

             1.2.1 With NAD⁺ or NADP⁺ as acceptor

                1.2.1.95 L-2-aminoadipate reductase

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Results	in table
1	Activating Compound
1274	AA Sequence
2	Application
7	Cloned(Commentary)
5	Cofactor
3	Expression
5	General Information
5	Inhibitors
4	kcat/KM [mM/s]
1	Ki Value [mM]
11	KM Value [mM]
4	Metals/Ions
6	Molecular Weight [Da]
1	Natural Substrates/ Products (Substrates)
17	Organism
3	Pathway
1	pH Optimum
1	pH Range
3	Posttranslational Modification
73	Protein Variants
2	Purification (Commentary)
3	Reaction
17	Reference
1	Source Tissue
2	Storage Stability
13	Substrates and Products (Substrate)
4	Subunits
25	Synonyms
1	Systematic Name
1	Temperature Optimum [°C]
1	Temperature Range [°C]
2	Temperature Stability [°C]
5	Turnover Number [1/s]

General Information

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General Information on EC 1.2.1.95 - L-2-aminoadipate reductase

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GENERAL INFORMATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

malfunction

2 entries

metabolism

Gelatoporia subvermispora

A0A0S2LUS1

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

physiological function

Gelatoporia subvermispora

A0A0S2LUS1

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

additional information

Gelatoporia subvermispora

A0A0S2LUS1

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

malfunction

Metarhizium robertsii

A0A0A1V264

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

malfunction

Metarhizium robertsii ARSEF 2575

-

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

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