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Ligand L-2-aminoadipic acid

Basic Ligand Information

Molecular Structure

Pathway Source

Pathways

BRENDA

lysine metabolism

KEGG

2-Oxocarboxylic acid metabolism, Biosynthesis of amino acids, Biosynthesis of secondary metabolites, Lysine biosynthesis, Lysine degradation, Penicillin and cephalosporin biosynthesis more

MetaCyc

isopenicillin N biosynthesis, L-lysine biosynthesis IV, L-lysine biosynthesis V, L-lysine degradation II (L-pipecolate pathway), L-lysine degradation V, L-lysine degradation VI, L-lysine degradation XI, penicillin G and penicillin V biosynthesis, penicillin K biosynthesis more

Show all BRENDA pathways known for L-2-aminoadipic acid

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (15 results)

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Show Natural Substrate (15 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.2.1.31

L-2-aminoadipate + NADPH + H+ = L-2-aminoadipate 6-semialdehyde + NADP+ + H2O

657420, 654293

4zul, 3D-view

1.2.1.31

L-2-aminoadipate + NADPH + H+ = L-2-aminoadipate 6-semialdehyde + NADP+ + H2O

657420, 654293

6o4f, 3D-view

1.2.1.31

L-2-aminoadipate + NADPH + H+ = L-2-aminoadipate 6-semialdehyde + NADP+ + H2O

657420, 654293

6o4g, 3D-view

1.2.1.31

L-2-aminoadipate + NADPH + H+ = L-2-aminoadipate 6-semialdehyde + NADP+ + H2O

657420, 654293

6o4i, 3D-view

1.2.1.31

L-alpha-aminoadipate + NAD(P)H = L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O

288201, 288204, 288203, 288189, 288192, 288185, 288190

4zul, 3D-view

1.2.1.31

L-alpha-aminoadipate + NAD(P)H = L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O

288201, 288204, 288203, 288189, 288192, 288185, 288190

6o4f, 3D-view

1.2.1.31

L-alpha-aminoadipate + NAD(P)H = L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O

288201, 288204, 288203, 288189, 288192, 288185, 288190

6o4g, 3D-view

1.2.1.31

L-alpha-aminoadipate + NAD(P)H = L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O

288201, 288204, 288203, 288189, 288192, 288185, 288190

6o4i, 3D-view

1.2.1.31

8 entries

1.2.1.95

L-2-aminoadipate + NADPH + H+ + ATP = (S)-2-amino-6-oxohexanoate + NADP+ + AMP + diphosphate

742278

-

2.6.1.39

L-2-aminoadipate + 2-oxoglutarate = 2-oxoadipate + L-glutamate

636620, 639974, 639985, 636621, 639975, 639976, 639979, 636625, 639983

-

5.1.1.3

L-2-aminoadipic acid = D-2-aminoadipic acid

701927

-

6.3.2.26

3 ATP + L-2-aminohexanedioate + L-cysteine + L-valine + H2O = 3 AMP + 3 diphosphate + N-[L-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine

726783, 727108

-

6.3.2.43

ATP + an [amino group carrier protein]-C-terminal-L-glutamate + L-2-aminoadipate = ADP + phosphate + an [amino group carrier protein]-C-terminal-N-(1,5-dicarboxypentan-1-yl)-L-glutamine

745351

-

6.3.2.43

ATP + [LysW]-C-terminal-L-glutamate + L-2-aminoadipate = ADP + phosphate + [LysW]-gamma-(L-2-aminoadip-2-yl)-L-glutamate

726025

-

6.3.2.43

ATP + [LysW]-C-terminal-L-glutamate54 + L-2-aminoadipate = ADP + phosphate + [LysW]-C-terminal-gamma-(L-2-aminoadip-2-yl)-L-glutamate54

726024

-

6.3.2.43

3 entries

In Vivo Product in Enzyme-catalyzed Reactions (22 results)

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Show Natural Product (22 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.2.1.31

(S)-2-amino-6-oxohexanoate + NAD+ + H2O = L-2-aminoadipate + NADH + H+

0

4zul, 3D-view

1.2.1.31

(S)-2-amino-6-oxohexanoate + NAD+ + H2O = L-2-aminoadipate + NADH + H+

0

6o4f, 3D-view

1.2.1.31

(S)-2-amino-6-oxohexanoate + NAD+ + H2O = L-2-aminoadipate + NADH + H+

0

6o4g, 3D-view

1.2.1.31

(S)-2-amino-6-oxohexanoate + NAD+ + H2O = L-2-aminoadipate + NADH + H+

0

6o4i, 3D-view

1.2.1.31

(S)-2-amino-6-oxohexanoate + NADP+ + H2O = L-2-aminoadipate + NADPH + H+

0

4zul, 3D-view

1.2.1.31

(S)-2-amino-6-oxohexanoate + NADP+ + H2O = L-2-aminoadipate + NADPH + H+

0

6o4f, 3D-view

1.2.1.31

(S)-2-amino-6-oxohexanoate + NADP+ + H2O = L-2-aminoadipate + NADPH + H+

0

6o4g, 3D-view

1.2.1.31

(S)-2-amino-6-oxohexanoate + NADP+ + H2O = L-2-aminoadipate + NADPH + H+

0

6o4i, 3D-view

1.2.1.31

alpha-aminoadipate semialdehyde + NAD(P)+ + H2O = L-2-aminoadipate + NAD(P)H + H+

0

4zul, 3D-view

1.2.1.31

alpha-aminoadipate semialdehyde + NAD(P)+ + H2O = L-2-aminoadipate + NAD(P)H + H+

0

6o4f, 3D-view

1.2.1.31

alpha-aminoadipate semialdehyde + NAD(P)+ + H2O = L-2-aminoadipate + NAD(P)H + H+

0

6o4g, 3D-view

1.2.1.31

alpha-aminoadipate semialdehyde + NAD(P)+ + H2O = L-2-aminoadipate + NAD(P)H + H+

0

6o4i, 3D-view

1.2.1.31

L-2-aminoadipate 6-semialdehyde + NAD(P)+ + H2O = L-2-aminoadipate + NAD(P)H + H+

0

4zul, 3D-view

1.2.1.31

L-2-aminoadipate 6-semialdehyde + NAD(P)+ + H2O = L-2-aminoadipate + NAD(P)H + H+

0

6o4f, 3D-view

1.2.1.31

L-2-aminoadipate 6-semialdehyde + NAD(P)+ + H2O = L-2-aminoadipate + NAD(P)H + H+

0

6o4g, 3D-view

1.2.1.31

L-2-aminoadipate 6-semialdehyde + NAD(P)+ + H2O = L-2-aminoadipate + NAD(P)H + H+

0

6o4i, 3D-view

1.2.1.31

L-2-aminoadipate-semialdehyde + NAD+ = L-2-aminoadipate + NADH

288194, 288193

4zul, 3D-view

1.2.1.31

L-2-aminoadipate-semialdehyde + NAD+ = L-2-aminoadipate + NADH

288194, 288193

6o4f, 3D-view

1.2.1.31

L-2-aminoadipate-semialdehyde + NAD+ = L-2-aminoadipate + NADH

288194, 288193

6o4g, 3D-view

1.2.1.31

L-2-aminoadipate-semialdehyde + NAD+ = L-2-aminoadipate + NADH

288194, 288193

6o4i, 3D-view

2.3.1.164

phenylacetyl-CoA + isopenicillin N + H2O = CoA + benzylpenicillin + L-2-aminohexanedioate

441304

-

2.3.1.164

phenylacetyl-CoA + isopenicillin N + H2O = CoA + penicillin G + L-2-aminohexanedioate

0

-

1.2.1.31

20 entries

2.3.1.164

2 entries

Substrate in Enzyme-catalyzed Reactions (37 results)

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Show Substrate (37 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.2.1.31

L-2-aminoadipate + NADPH + H+ = L-2-aminoadipate 6-semialdehyde + NADP+ + H2O

654293, 657420, 656194

4zul, 3D-view

1.2.1.31

L-2-aminoadipate + NADPH + H+ = L-2-aminoadipate 6-semialdehyde + NADP+ + H2O

654293, 657420, 656194

6o4f, 3D-view

1.2.1.31

L-2-aminoadipate + NADPH + H+ = L-2-aminoadipate 6-semialdehyde + NADP+ + H2O

654293, 657420, 656194

6o4g, 3D-view

1.2.1.31

L-2-aminoadipate + NADPH + H+ = L-2-aminoadipate 6-semialdehyde + NADP+ + H2O

654293, 657420, 656194

6o4i, 3D-view

1.2.1.31

L-2-aminoadipate + NADPH = L-2-aminoadipate 6-semialdehyde + NADP+ + H2O

288201, 288203, 288189, 288198, 288192, 288185, 288195

4zul, 3D-view

1.2.1.31

L-2-aminoadipate + NADPH = L-2-aminoadipate 6-semialdehyde + NADP+ + H2O

288201, 288203, 288189, 288198, 288192, 288185, 288195

6o4f, 3D-view

1.2.1.31

L-2-aminoadipate + NADPH = L-2-aminoadipate 6-semialdehyde + NADP+ + H2O

288201, 288203, 288189, 288198, 288192, 288185, 288195

6o4g, 3D-view

1.2.1.31

L-2-aminoadipate + NADPH = L-2-aminoadipate 6-semialdehyde + NADP+ + H2O

288201, 288203, 288189, 288198, 288192, 288185, 288195

6o4i, 3D-view

1.2.1.31

L-alpha-aminoadipate + NAD(P)H = L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O

288201, 288204, 288203, 288189, 288192, 288185, 288190

4zul, 3D-view

1.2.1.31

L-alpha-aminoadipate + NAD(P)H = L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O

288201, 288204, 288203, 288189, 288192, 288185, 288190

6o4f, 3D-view

1.2.1.31

L-alpha-aminoadipate + NAD(P)H = L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O

288201, 288204, 288203, 288189, 288192, 288185, 288190

6o4g, 3D-view

1.2.1.31

L-alpha-aminoadipate + NAD(P)H = L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O

288201, 288204, 288203, 288189, 288192, 288185, 288190

6o4i, 3D-view

1.2.1.31

12 entries

1.2.1.95

L-2-aminoadipate + NADPH + H+ + ATP = (S)-2-amino-6-oxohexanoate + NADP+ + AMP + diphosphate

656194, 733888, 288201, 288203, 742278

-

2.3.1.1

acetyl-CoA + L-2-aminoadipate = CoA + 2-acetylaminohexanedioate

486061, 486071

-

2.6.1.39

2-oxoglutarate + L-2-aminoadipate = 2-oxoadipate + L-glutamate

721430

-

2.6.1.39

L-2-aminoadipate + 2-oxoglutarate = 2-oxoadipate + L-glutamate

639983, 639985, 636620, 636621, 639975, 639976, 639979, 639974, 636625, 702779, 702069, 737334, 703133

-

2.6.1.39

L-2-aminoadipate + 4-hydroxyphenylpyruvate = 2-oxoadipate + L-tyrosine

721430

-

2.6.1.39

3 entries

2.6.1.7

L-2-aminohexane-1,6-dioate + 2-oxoglutarate = 2-oxohexane-1,6-dioate + L-glutamate

636614

-

2.6.1.9

3-(imidazol-4-yl)-2-oxopropyl phosphate + L-2-aminoadipate = L-histidinol phosphate + 2-oxoadipate

637142

-

4.1.99.2

L-2-aminoadipate + H2O = ?

33472

-

5.1.1.3

L-2-aminoadipic acid = D-2-aminoadipic acid

701927

-

6.3.2.26

L-2-aminoadipate + allylglycine + L-valine + ATP = L-delta-(aminoadipyl)-L-allylglycinyl-D-valine + AMP + diphosphate

440077

-

6.3.2.26

L-2-aminoadipate + L-cystathionine + L-valine + ATP = N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine + AMP + diphosphate

440082

-

6.3.2.26

L-2-aminoadipate + L-cysteine + L-allo-isoleucine + ATP = L-delta-(aminoadipyl)-L-cysteinyl-D-allo-isoleucine + AMP + diphosphate

440077, 440081

-

6.3.2.26

L-2-aminoadipate + L-cysteine + L-isoleucine + ATP = L-delta-(aminoadipyl)-L-cysteinyl-D-isoleucine + AMP + diphosphate

440081

-

6.3.2.26

L-2-aminoadipate + L-cysteine + L-valine + ATP = N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine + AMP + diphosphate

440075, 440085, 440086, 440084, 440082, 440073, 440074, 440076, 440077, 440078, 440079, 440080, 440083, 440081

-

6.3.2.26

L-2-aminoadipate + L-homocysteine + L-valine + ATP = N-(5-amino-5-carboxypentanoyl)-L-homocysteinyl-D-valine + AMP + diphosphate

440081

-

6.3.2.26

L-2-aminoadipate + vinylglycine + L-valine + ATP = L-delta-(aminoadipyl)-L-vinylglycinyl-D-valine + AMP + diphosphate

440077

-

6.3.2.26

3 ATP + L-2-aminohexanedioate + L-cysteine + L-valine + H2O = 3 AMP + 3 diphosphate + N-[L-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine

726783, 727108

-

6.3.2.26

DL-valine + L-O-(methylserine) + L-2-aminohexanedioate + ATP = L-O-(methylserinyl)-D-valine + L-O-(methylserinyl)-D-valine + AMP + diphosphate

440077, 440080

-

6.3.2.43

ATP + an [amino group carrier protein]-C-terminal-L-glutamate + L-2-aminoadipate = ADP + phosphate + an [amino group carrier protein]-C-terminal-N-(1,5-dicarboxypentan-1-yl)-L-glutamine

745351

-

6.3.2.43

ATP + [lysine-biosynthesis-protein LysW]-C-terminal-L-glutamate + L-2-aminoadipate = ADP + phosphate + [lysine-biosynthesis-protein LysW]-C-terminal-gamma-(L-2-aminoadip-2-yl)-L-glutamate

745351

-

6.3.2.43

ATP + [LysW mutant E42R]-C-terminal-L-glutamate + L-2-aminoadipate = ADP + phosphate + [LysW mutant E42R]-C-terminal-N-(1,5-dicarboxypentan-1-yl)-L-glutamine

745351

-

6.3.2.43

ATP + [LysW]-C-terminal-L-glutamate + L-2-aminoadipate = ADP + phosphate + [LysW]-C-terminal-gamma-(L-2-aminoadip-2-yl)-L-glutamate

726025

-

6.3.2.43

ATP + [LysW]-C-terminal-L-glutamate + L-2-aminoadipate = ADP + phosphate + [LysW]-C-terminal-N-(1,4-dicarboxybutan-1-yl)-L-glutamine

745351

-

6.3.2.43

ATP + [LysW]-C-terminal-L-glutamate + L-2-aminoadipate = ADP + phosphate + [LysW]-gamma-(L-2-aminoadip-2-yl)-L-glutamate

726025

-

6.3.2.43

ATP + [LysW]-C-terminal-L-glutamate54 + L-2-aminoadipate = ADP + phosphate + [LysW]-C-terminal-gamma-(L-2-aminoadip-2-yl)-L-glutamate54

726024

-

6.3.2.26

9 entries

6.3.2.43

7 entries

Product in Enzyme-catalyzed Reactions (44 results)

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Show Product (44 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.2.1.31

(S)-2,3,4,5-tetrahydropyridine-2-carboxylate + NAD+ + H2O = L-2-aminoadipate + NADH

288195, 288194

4zul, 3D-view

1.2.1.31

(S)-2,3,4,5-tetrahydropyridine-2-carboxylate + NAD+ + H2O = L-2-aminoadipate + NADH

288195, 288194

6o4f, 3D-view

1.2.1.31

(S)-2,3,4,5-tetrahydropyridine-2-carboxylate + NAD+ + H2O = L-2-aminoadipate + NADH

288195, 288194

6o4g, 3D-view

1.2.1.31

(S)-2,3,4,5-tetrahydropyridine-2-carboxylate + NAD+ + H2O = L-2-aminoadipate + NADH

288195, 288194

6o4i, 3D-view

1.2.1.31

(S)-2-amino-6-oxohexanoate + NAD+ + H2O = L-2-aminoadipate + NADH + H+

0

4zul, 3D-view

1.2.1.31

(S)-2-amino-6-oxohexanoate + NAD+ + H2O = L-2-aminoadipate + NADH + H+

0

6o4f, 3D-view

1.2.1.31

(S)-2-amino-6-oxohexanoate + NAD+ + H2O = L-2-aminoadipate + NADH + H+

0

6o4g, 3D-view

1.2.1.31

(S)-2-amino-6-oxohexanoate + NAD+ + H2O = L-2-aminoadipate + NADH + H+

0

6o4i, 3D-view

1.2.1.31

(S)-2-amino-6-oxohexanoate + NADP+ + H2O = L-2-aminoadipate + NADPH + H+

0

4zul, 3D-view

1.2.1.31

(S)-2-amino-6-oxohexanoate + NADP+ + H2O = L-2-aminoadipate + NADPH + H+

0

6o4f, 3D-view

1.2.1.31

(S)-2-amino-6-oxohexanoate + NADP+ + H2O = L-2-aminoadipate + NADPH + H+

0

6o4g, 3D-view

1.2.1.31

(S)-2-amino-6-oxohexanoate + NADP+ + H2O = L-2-aminoadipate + NADPH + H+

0

6o4i, 3D-view

1.2.1.31

alpha-aminoadipate semialdehyde + NAD(P)+ + H2O = L-2-aminoadipate + NAD(P)H + H+

0

4zul, 3D-view

1.2.1.31

alpha-aminoadipate semialdehyde + NAD(P)+ + H2O = L-2-aminoadipate + NAD(P)H + H+

0

6o4f, 3D-view

1.2.1.31

alpha-aminoadipate semialdehyde + NAD(P)+ + H2O = L-2-aminoadipate + NAD(P)H + H+

0

6o4g, 3D-view

1.2.1.31

alpha-aminoadipate semialdehyde + NAD(P)+ + H2O = L-2-aminoadipate + NAD(P)H + H+

0

6o4i, 3D-view

1.2.1.31

L-2-aminoadipate 6-semialdehyde + NAD(P)+ + H2O = L-2-aminoadipate + NAD(P)H + H+

0

4zul, 3D-view

1.2.1.31

L-2-aminoadipate 6-semialdehyde + NAD(P)+ + H2O = L-2-aminoadipate + NAD(P)H + H+

0

6o4f, 3D-view

1.2.1.31

L-2-aminoadipate 6-semialdehyde + NAD(P)+ + H2O = L-2-aminoadipate + NAD(P)H + H+

0

6o4g, 3D-view

1.2.1.31

L-2-aminoadipate 6-semialdehyde + NAD(P)+ + H2O = L-2-aminoadipate + NAD(P)H + H+

0

6o4i, 3D-view

1.2.1.31

L-2-aminoadipate 6-semialdehyde + NAD+ + H2O = L-2-aminoadipate + NADH

288186, 288193, 288195, 288194

4zul, 3D-view

1.2.1.31

L-2-aminoadipate 6-semialdehyde + NAD+ + H2O = L-2-aminoadipate + NADH

288186, 288193, 288195, 288194

6o4f, 3D-view

1.2.1.31

L-2-aminoadipate 6-semialdehyde + NAD+ + H2O = L-2-aminoadipate + NADH

288186, 288193, 288195, 288194

6o4g, 3D-view

1.2.1.31

L-2-aminoadipate 6-semialdehyde + NAD+ + H2O = L-2-aminoadipate + NADH

288186, 288193, 288195, 288194

6o4i, 3D-view

1.2.1.31

L-2-aminoadipate-semialdehyde + NAD+ = L-2-aminoadipate + NADH

288194, 288193

4zul, 3D-view

1.2.1.31

L-2-aminoadipate-semialdehyde + NAD+ = L-2-aminoadipate + NADH

288194, 288193

6o4f, 3D-view

1.2.1.31

L-2-aminoadipate-semialdehyde + NAD+ = L-2-aminoadipate + NADH

288194, 288193

6o4g, 3D-view

1.2.1.31

L-2-aminoadipate-semialdehyde + NAD+ = L-2-aminoadipate + NADH

288194, 288193

6o4i, 3D-view

1.2.1.31

DELTA1-piperidine 6-carboxylate + NAD+ + H2O = L-alpha-aminoadipate + NADH + H+

0

4zul, 3D-view

1.2.1.31

DELTA1-piperidine 6-carboxylate + NAD+ + H2O = L-alpha-aminoadipate + NADH + H+

0

6o4f, 3D-view

1.2.1.31

DELTA1-piperidine 6-carboxylate + NAD+ + H2O = L-alpha-aminoadipate + NADH + H+

0

6o4g, 3D-view

1.2.1.31

DELTA1-piperidine 6-carboxylate + NAD+ + H2O = L-alpha-aminoadipate + NADH + H+

0

6o4i, 3D-view

1.2.1.31

L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O = L-alpha-aminoadipate + NAD(P)H + H+

0

4zul, 3D-view

1.2.1.31

L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O = L-alpha-aminoadipate + NAD(P)H + H+

0

6o4f, 3D-view

1.2.1.31

L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O = L-alpha-aminoadipate + NAD(P)H + H+

0

6o4g, 3D-view

1.2.1.31

L-alpha-aminoadipate-semialdehyde + NAD(P)+ + H2O = L-alpha-aminoadipate + NAD(P)H + H+

0

6o4i, 3D-view

1.2.1.31

36 entries

1.2.1.95

(S)-2-amino-6-oxohexanoate + NADP+ + AMP + diphosphate = L-2-aminoadipate + NADPH + H+ + ATP

0

-

1.4.1.4

2-oxoadipate + NADPH + NH3 = L-2-aminoadipate + NADP+ + H2O

0

-

2.3.1.164

phenoxyacetyl-CoA + isopenicillin N + H2O = CoA + penicillin V + L-2-aminohexanedioate

0

-

2.3.1.164

phenylacetyl-CoA + isopenicillin N + H2O = CoA + benzylpenicillin + L-2-aminohexanedioate

441304

-

2.3.1.164

phenylacetyl-CoA + isopenicillin N + H2O = CoA + penicillin G + L-2-aminohexanedioate

0

-

2.3.1.164

3 entries

2.6.1.39

2-oxoadipate + L-glutamate = L-2-aminoadipate + 2-oxoglutarate

0

-

2.6.1.50

L-glutamine + 2-oxoadipate = 2-oxoglutaramate + L-2-amino-1,6-hexandioate

0

-

2.6.1.57

L-phenylalanine + 2-oxoadipate = phenylpyruvate + L-2-aminoadipate

0

-

Inhibitor in Enzyme-catalyzed Reactions (3 results)

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Show Inhibitors (3 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

2.6.1.7

-

722912

-

5.1.1.3

-

2120

-

6.3.2.2

i.e. L-alpha-aminoadipate

1132

-

3D Structure of Enzyme-Ligand-Complex (PDB) (137 results)

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Show 3D Structure of Enzyme-Ligand-Complex (PDB) (137 entries)

EC NUMBER

ENZYME 3D STRUCTURE

1.2.1.3

4zul, 3D-view

1.2.1.3

6o4f, 3D-view

1.2.1.3

6o4g, 3D-view

1.2.1.3

6o4i, 3D-view

1.2.1.3

4zul, 3D-view

1.2.1.3

6o4f, 3D-view

1.2.1.3

6o4g, 3D-view

1.2.1.3

6o4i, 3D-view

1.2.1.3

4zul, 3D-view

1.2.1.3

6o4f, 3D-view

1.2.1.3

6o4g, 3D-view

1.2.1.3

6o4i, 3D-view

1.2.1.3

4zul, 3D-view

1.2.1.3

6o4f, 3D-view

1.2.1.3

6o4g, 3D-view

1.2.1.3

6o4i, 3D-view

1.2.1.3

4zul, 3D-view

1.2.1.3

6o4f, 3D-view

1.2.1.3

6o4g, 3D-view

1.2.1.3

6o4i, 3D-view

1.2.1.3

4zul, 3D-view

1.2.1.3

6o4f, 3D-view

1.2.1.3

6o4g, 3D-view

1.2.1.3

6o4i, 3D-view

1.2.1.3

4zul, 3D-view

1.2.1.3

6o4f, 3D-view

1.2.1.3

6o4g, 3D-view

1.2.1.3

6o4i, 3D-view

1.2.1.3

4zul, 3D-view

1.2.1.3

6o4f, 3D-view

1.2.1.3

6o4g, 3D-view

1.2.1.3

6o4i, 3D-view

1.2.1.3

4zul, 3D-view

1.2.1.3

6o4f, 3D-view

1.2.1.3

6o4g, 3D-view

1.2.1.3

6o4i, 3D-view

1.2.1.31

4zul, 3D-view

1.2.1.31

6o4f, 3D-view

1.2.1.31

6o4g, 3D-view

1.2.1.31

6o4i, 3D-view

1.2.1.31

4zul, 3D-view

1.2.1.31

6o4f, 3D-view

1.2.1.31

6o4g, 3D-view

1.2.1.31

6o4i, 3D-view

1.2.1.31

4zul, 3D-view

1.2.1.31

6o4f, 3D-view

1.2.1.31

6o4g, 3D-view

1.2.1.31

6o4i, 3D-view

1.2.1.31

4zul, 3D-view

1.2.1.31

6o4f, 3D-view

1.2.1.31

6o4g, 3D-view

1.2.1.31

6o4i, 3D-view

1.2.1.31

4zul, 3D-view

1.2.1.31

6o4f, 3D-view

1.2.1.31

6o4g, 3D-view

1.2.1.31

6o4i, 3D-view

1.2.1.31

4zul, 3D-view

1.2.1.31

6o4f, 3D-view

1.2.1.31

6o4g, 3D-view

1.2.1.31

6o4i, 3D-view

1.2.1.31

4zul, 3D-view

1.2.1.31

6o4f, 3D-view

1.2.1.31

6o4g, 3D-view

1.2.1.31

6o4i, 3D-view

1.2.1.31

4zul, 3D-view

1.2.1.31

6o4f, 3D-view

1.2.1.31

6o4g, 3D-view

1.2.1.31

6o4i, 3D-view

1.2.1.31

4zul, 3D-view

1.2.1.31

6o4f, 3D-view

1.2.1.31

6o4g, 3D-view

1.2.1.31

6o4i, 3D-view

1.2.1.3

36 entries

1.2.1.31

36 entries

1.2.1.38

5ein, 3D-view

1.2.1.8

4zul, 3D-view

1.2.1.8

6o4f, 3D-view

1.2.1.8

6o4g, 3D-view

1.2.1.8

6o4i, 3D-view

1.2.1.8

4zul, 3D-view

1.2.1.8

6o4f, 3D-view

1.2.1.8

6o4g, 3D-view

1.2.1.8

6o4i, 3D-view

1.2.1.8

4zul, 3D-view

1.2.1.8

6o4f, 3D-view

1.2.1.8

6o4g, 3D-view

1.2.1.8

6o4i, 3D-view

1.2.1.8

4zul, 3D-view

1.2.1.8

6o4f, 3D-view

1.2.1.8

6o4g, 3D-view

1.2.1.8

6o4i, 3D-view

1.2.1.8

4zul, 3D-view

1.2.1.8

6o4f, 3D-view

1.2.1.8

6o4g, 3D-view

1.2.1.8

6o4i, 3D-view

1.2.1.8

4zul, 3D-view

1.2.1.8

6o4f, 3D-view

1.2.1.8

6o4g, 3D-view

1.2.1.8

6o4i, 3D-view

1.2.1.8

4zul, 3D-view

1.2.1.8

6o4f, 3D-view

1.2.1.8

6o4g, 3D-view

1.2.1.8

6o4i, 3D-view

1.2.1.8

4zul, 3D-view

1.2.1.8

6o4f, 3D-view

1.2.1.8

6o4g, 3D-view

1.2.1.8

6o4i, 3D-view

1.2.1.8

4zul, 3D-view

1.2.1.8

6o4f, 3D-view

1.2.1.8

6o4g, 3D-view

1.2.1.8

6o4i, 3D-view

1.2.1.8

36 entries

1.21.3.1

7p3l, 3D-view

3.2.1.14

1h0g, 3D-view

3.2.1.14

1w9u, 3D-view

3.2.1.14

1waw, 3D-view

3.2.1.14

1h0g, 3D-view

3.2.1.14

1w9u, 3D-view

3.2.1.14

1waw, 3D-view

3.2.1.14

1h0g, 3D-view

3.2.1.14

1w9u, 3D-view

3.2.1.14

1waw, 3D-view

3.2.1.14

1h0g, 3D-view

3.2.1.14

1w9u, 3D-view

3.2.1.14

1waw, 3D-view

3.2.1.14

1h0g, 3D-view

3.2.1.14

1w9u, 3D-view

3.2.1.14

1waw, 3D-view

3.2.1.14

1h0g, 3D-view

3.2.1.14

1w9u, 3D-view

3.2.1.14

1waw, 3D-view

3.2.1.14

1h0g, 3D-view

3.2.1.14

1w9u, 3D-view

3.2.1.14

1waw, 3D-view

3.2.1.14

1h0g, 3D-view

3.2.1.14

1w9u, 3D-view

3.2.1.14

1waw, 3D-view

3.2.1.14

1h0g, 3D-view

3.2.1.14

1w9u, 3D-view

3.2.1.14

1waw, 3D-view

3.2.1.14

27 entries

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (10 results)

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Show Turnover Number (10 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.2.1.31

66

-

pH 8, 30°C

656194

1.2.1.95

1.1

-

pH 9.0, 30°C

656194

1.2.1.95

41.7

-

pH 8.8, 37°C

288201

2.6.1.39

0.011

-

mutant enzyme R23A, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C

702069

2.6.1.39

0.04

-

mutant enzyme S20E, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C

702069

2.6.1.39

0.083

-

mutant enzyme R23Q, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C

702069

2.6.1.39

6.7

-

wild type enzyme, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C

702069

2.6.1.39

18.4

-

pH 7.0, temperature not specified in the publication

721430

1.2.1.95

2 entries

2.6.1.39

5 entries

5.1.1.3

2.4

-

His-tagged recombinant FnGR, in potassium phosphate buffer (10 mM, pH 8.0)

701927

6.3.2.43

0.85

-

pH 8.0, 60°C

726024

K_M Value (17 results)

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Show KM Value (17 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.2.1.31

1.4

-

pH 8, 30°C

656194

1.2.1.95

0.3

-

pH not specified in the publication, temperature not specified in the publication

733888

1.2.1.95

0.47

-

pH 8.8, 37°C

288201

1.2.1.95

1.4

-

pH 9.0, 30°C

656194

2.6.1.39

0.02

-

pH 7.0, 22°C

737334

2.6.1.39

0.25

-

pH 8.0, 37°C isoenzyme AadAT-II

639983

2.6.1.39

0.81

-

wild type enzyme, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C

702069

2.6.1.39

3.3

-

mutant enzyme R23A, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C

702069

2.6.1.39

7

-

mutant enzyme S20E, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C

702069

2.6.1.39

8.8

-

pH 7.0, temperature not specified in the publication

721430

2.6.1.39

11

-

mutant enzyme R23Q, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C

702069

2.6.1.39

20

-

pH 8.0, 37°C

639983

1.2.1.95

3 entries

2.6.1.39

8 entries

5.1.1.3

26

-

His-tagged recombinant FnGR, in potassium phosphate buffer (10 mM, pH 8.0)

701927

6.3.2.26

0.045

-

-

440084

6.3.2.26

0.17

-

-

440076

6.3.2.26

0.63

-

-

440081

6.3.2.26

3 entries

6.3.2.43

2.1

-

pH 8.0, 60°C

726024

References & Links

Literature References (60)

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Show Reference (60 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

1132

15992

gamma-Glutamylcysteine synthetase. Further purification, half of the sites" reactivity, subunits, and specificity

1977

Sekura, R.; Meister, A.

J. Biol. Chem.

252

2599-2605

2120

-

Distribution of glutamate racemase in lactic acid bacteria and further characterization of the enzyme from Pediococcus pentosaceus

1988

Nakajima, N.; Tanizawa, K.; Tanaka, H.; Soda, K.

Agric. Biol. Chem.

52

3099-3104

33472

9880502

Conversion of tyrosine phenol-lyase to dicarboxylic amino acid beta-lyase, an enzyme not found in nature

1999

Mouratou, B.; Kasper, P.; Gehring, H.; Christen, P.

J. Biol. Chem.

274

1320-1325

288185

1975789

Inhibition of alpha-aminoadipate-semialdehyde dehydrogenase from Trichosporon adeninovorans by lysine and lysine analogues

1990

Schmidt, H.; Bode, R.; Birnbaum D.

FEMS Microbiol. Lett.

70

41-44

288186

2160277

L-pipecolic acid metabolism in human liver: L-alpha-aminoadipate delta-semialdehyde oxidoreductase

1990

Chang, Y.F.; Ghosh, P.; Rao, V.V.

Biochim. Biophys. Acta

1038

300-305

288189

2499333

Properties of revertants of lys2 and lys5 mutants as well as alpha-aminoadipate-semialdehyde dehydrogenase from Saccharomyces cerevisiae

1989

Storts, D.R.; Bhattacharjee, J.K.

Biochem. Biophys. Res. Commun.

161

182-186

288190

3142867

Lysine biosynthesis pathway and biochemical blocks of lysine auxotrophs of Schizosaccharomyces pombe

1988

Ye, Z.H.; Bhattacharjee, J.K.

J. Bacteriol.

170

5968-5970

288192

-

Lysine biosynthesis in the yeast Candida maltosa: properties of some enzymes and regulation of the biosynthetic pathway

1985

Schmidt, H.; Bode, R.; Lindner, M.; Birnbaum, D.

J. Basic Microbiol.

25

675-681

288193

4369906

Degradation of O-phosphohydroxylysine in rat liver. Purification and properties of 2-aminoadipic semialdehyde dehydrogenase

1974

Tsai, C.H.; Henderson, L.M.

J. Biol. Chem.

249

5790-5792

288194

-

delta1-piperideine-6-carboxylic acid and alpha-aminoadipic acid delta-semialdehyde

1971

Rodwell, V.W.

Methods Enzymol.

17B

188-199

288195

4285660

Metabolism of pipecolic acid in a Pseudomonas species. 3. L-alpha-aminoadipate delta-semialdehyde:nicotinamide adenine dinucleotide oxidoreductase

1966

Calvert, A.F.; Rodwell, V.W.

J. Biol. Chem.

241

409-414

288198

8590464

Molecular properties of the lys1+ gene and the regulation of.alpha-aminoadipate reductase in Schizosaccharomyces pombe

1995

Ford, R.A.; Bhattacharjee, J.K.

Curr. Genet.

28

131-137

288201

10320345

Lysine biosynthesis in Saccharomyces cerevisiae: mechanism of alpha-aminoadipate reductase (Lys2) involves posttranslational phosphopantetheinylation by Lys5

1999

Ehmann, D.E.; Gehring, A.M.; Walsh, C.T.

Biochemistry

38

6171-6177

288203

11254122

Characterization of the lys2 gene of Acremonium chrysogenum encoding a functional.alpha-aminoadipate activating and reducing enzyme

2001

Hijarrubia, M.J.; Aparicio, J.F.; Casqueiro, J.; Martin, J.F.

Mol. Gen. Genet.

264

755-762

288204

11717270

Novel posttranslational activation of the LYS2-encoded.alpha-aminoadipate reductase for biosynthesis of lysine and site-directed mutational analysis of conserved amino acid residues in the activation domain of Candida albicans

2001

Guo, S.; Evans, S.A.; Wilkes, M.B.; Bhattacharjee, J.K.

J. Bacteriol.

183

7120-7125

440073

9305735

Penicillin biosynthesis: intermediates of biosynthesis of delta-L-alpha-aminoadipyl-L-cysteinyl-D-valine formed by ACV synthetase from Acremonium chrysogenum

1997

Kallow, W.; Neuhof, T.; Arezi, B.; Jungblut, P.; von Doehren, H.

FEBS Lett.

414

74-78

440074

9558329

Penicillin biosynthesis: energy requirement for tripeptide precursor formation by delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase from Acremonium chrysogenum

1998

Kallow, W.; Von Dohren, H.; Kleinkauf, H.

Biochemistry

37

5947-5952

440075

2061333

delta-(L-alpha-Aminoadipyl)-L-cysteinyl-D-valine synthetase from Aspergillus nidulans. Molecular characterization of the acvA gene encoding the first enzyme of the penicillin biosynthetic pathway

1991

MacCabe, A.P.; Van Liempt, H.; Palissa, H.; Unkles, S.E.; Riach, M.B.R.; Pfeifer, E.; Von Doehren, H.; Kinghorn, J.R.

J. Biol. Chem.

266

12646-12654

440076

-

delta-(L-alpha-Aminoadipyl)-L-cysteinyl-D-valine synthetase (ACV synthetase): a multifunctional enzyme with broad substrate specificity for the synthesis of penicillin and cephalosporin precursors

1987

Banko, G.; Demain, A.L.; Wolfe, S.

J. Am. Chem. Soc.

109

2858-2860

440077

-

Substrate specificity of L-delta-(alpha-aminoadipoyl)-L-cysteinyl-D-valine synthetase from Cephalosporium acremonium: demonstration of the structure of several unnatural tripeptide products

1994

Baldwin, J.E.; Shiau, C.Y.; Byford, M.F.; Schofield, C.J.

Biochem. J.

301

367-372

440078

-

Regulation of ACV synthetase activity in the beta-lactam biosynthetic pathway by carbon sources and their metabolites

1992

Zhang, J.; Demain, A.L.

Arch. Microbiol.

158

364-369

440079

8654814

Molecular mechanism of the multifunctional enzyme L-delta-(alpha-aminoadipoyl)-L-cysteinyl-D-valine (ACV) synthetase

1995

Shiau, C.Y.; Byford, M.F.; Baldwin, J.E.; Schofield, C.J.

Biochem. Soc. Trans.

23

629S

440080

9220966

L-delta-(alpha-Aminoadipoyl)-L-cysteinyl-D-valine synthetase: thioesterification of valine is not obligatory for peptide bond formation

1997

Shiau, C.Y.; Byford, M.F.; Aplin, R.T.; Baldwin, J.E.; Schofield, C.J.

Biochemistry

36

8798-8806

440081

1590759

Biochemical studies on the activity of delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase from Streptomyces clavuligerus

1992

Zhang, J.; Wolfe, S.; Demain, A.L.

Biochem. J.

283

691-698

440082

8973642

Overexpression of the Nocardia lactamdurans alpha-aminoadipyl-cysteinyl-valine synthetase in Streptomyces lividans. The purified multienzyme uses cystathionine and 6-oxopiperidine 2-carboxylate as substrates for synthesis of the tripeptide

1996

Coque, J.J.R.; De la Fuente, J.L.; Liras, P.; Martin, J.F.

Eur. J. Biochem.

242

264-270

440083

-

In vitro stabilization of ACV synthetase activity from Streptomyces clavuligerus

1992

Zhang, J.; Demain, A.L.

Appl. Biochem. Biotechnol.

37

97-110

440084

-

Purification and characterization of delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase from Penicillium chrysogenum

1997

Theilgaard, H.B.A.; Kristiansen, K.N.; Henriksen, C.M.; Nielsen, J.

Biochem. J.

327

185-191

440085

7763859

delta-(L-alpha-Aminoadipyl)-L-cysteinyl-D-valine synthetase, the multienzyme integrating the four primary reactions in b-lactam biosynthesis, as a model peptide synthetase

1993

Aharonowitz, Y.; Bergmeyer, J.; Cantoral, J.M.; Cohen, G.; Demain, A.L.; Fink, U.; Kinghorn, J.; Kleinkauf, H.; MacCabe, A.; et al.

Bio/Technology

11

807-810

440086

11851475

The mechanism of ACV synthetase

1997

Byford, M.F.; Baldwin, J.E.; Shiau, C.Y.; Schofield, C.J.

Chem. Rev.

97

2631-2649

441304

8082826

Acyl-coenzyme A:isopenicillin N acyltransferase from Penicillium chrysogenum: effect of amino acid substitutions at Ser227, Ser230 and Ser309 on proenzyme cleavage and activity

1994

Tobin, M.B.; Cole, S.C.J.; Kovacevic, S.; Miller, J.R.; Baldwin, J.E.; Sutherland, J.D.

FEMS Microbiol. Lett.

121

39-46

486061

3911000

N-Acetylglutamate synthase

1985

Powers-Lee, S.G.

Methods Enzymol.

113

27-35

486071

6885773

Purification of N-acetyl-L-glutamate synthetase from rat liver mitochondria and substrate and activator specificity of the enzyme

1983

Sonoda, T.; Tatibana, M.

J. Biol. Chem.

258

9839-9844

636614

3003516

L-Kynurenine transaminase from Hansenula schneggii

1985

Tanizawa, K.; Asada, Y.; Soda, K.

Methods Enzymol.

113

90-95

636620

3003514

Kynurenine aminotransferase from kidney supernatant

1985

Hartline, R.A.

Methods Enzymol.

113

664-672

636621

-

Purification and properties of kynurenine aminotransferase from rat kidney

1991

Mawal, M.R.; Mukhopadhyay, A.; Deshmukh, D.R.

Biochem. J.

279

595-599

636625

7493966

Cloning and functional expression of a soluble form of kynurenine/alpha-aminoadipate aminotransferase from rat kidney

1995

Buchli, R.; Alberati-Giani, D.; Malherbe, P.; Kohler, C.; Broger, C.; Cesura, A.M.

J. Biol. Chem.

270

29330-29335

637142

13319331

Biosynthesis of histidine: imidazoleacetol phosphate transaminase

1956

Ames, B.N.; Horecker, B.L.

J. Biol. Chem.

220

113-128

639974

5792664

Separation and specificity of the yeast glutamate-alpha-ketoadipate transaminase

1969

Matsuda, M.; Ogur, M.

J. Biol. Chem.

244

3352-3358

639975

1111529

L-kynurenine aminotransferase and L-alpha-aminoadipate aminotransferase. I. Evidence for identity

1975

Tobes, M.C.; Mason, M.

Biochem. Biophys. Res. Commun.

62

390-397

639976

873907

alpha-Aminoadipate aminotransferase and kynurenine aminotransferase. Purification, characterization, and further evidence for identity

1977

Tobes, M.C.; Mason, M.

J. Biol. Chem.

252

4591-4599

639979

2803240

Purification and properties of 2-aminoadipate: 2-oxoglutarate aminotransferase from bovine kidney

1989

Deshmukh, D.R.; Mungre, S.M.

Biochem. J.

261

761-768

639983

8087205

2-Aminoadipate-2-oxoglutarate aminotransferase isoenzymes in human liver: a plausible physiological role in lysine and tryptophan metabolism

1993

Okuno, E.; Tsujimoto, M.; Nakamura, M.; Kido, R.

Enzyme Protein

47

136-148

639985

12126930

Characterization of the human gene encoding alpha-aminoadipate aminotransferase (AADAT)

2002

Goh, D.L.; Patel, A.; Thomas, G.H.; Salomons, G.S.; Schor, D.S.; Jakobs, C.; Geraghty, M.T.

Mol. Genet. Metab.

76

172-180

654293

12111157

Nitrate regulation of alpha-aminoadipate reductase formation and lysine inhibition of its activity in Penicillium chrysogenum and Acremonium chrysogenum

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Guo, S.; Bhattacharjee, J.K.

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Substrate specificity and structure of human aminoadipate aminotransferase/kynurenine aminotransferase II

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Lysine and arginine biosyntheses mediated by a common carrier protein in Sulfolobus

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Ouchi, T.; Tomita, T.; Horie, A.; Yoshida, A.; Takahashi, K.; Nishida, H.; Lassak, K.; Taka, H.; Mineki, R.; Fujimura, T.; Kosono, S.; Nishiyama, C.; Masui, R.; Kuramitsu, S.; Albers, S.V.; Kuzuyama, T.; Nishiyama, M.

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A vacuolar membrane protein affects drastically the biosynthesis of the ACV tripeptide and the beta-lactam pathway of Penicillium chrysogenum

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Wu, X.; Garcia-Estrada, C.; Vaca, I.; Martin, J.F.

Biochimie

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733888

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Lysine biosynthesis in Penicillium chrysogenum is regulated by feedback inhibition of alpha-aminoadipate reductase

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Affenzeller, K.; Jaklitsch, W.; Hönlinger, C.; Kubicek, C.

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Characterization of two aminotransferases from Candida albicans

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742278

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Activity of alpha-aminoadipate reductase depends on the N-terminally extending domain

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Kalb, D.; Lackner, G.; Rappe, M.; Hoffmeister, D.

ChemBioChem

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Lysine biosynthesis of Thermococcus kodakarensis with the capacity to function as an ornithine biosynthetic system

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Links to other databases for L-2-aminoadipic acid

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