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Ligand L-erythro-3,5-diaminohexanoate

Basic Ligand Information

Molecular Structure

Show all BRENDA pathways known for L-erythro-3,5-diaminohexanoate

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (4 results)

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Show Natural Substrate (4 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.4.1.11

L-erythro-3,5-diaminohexanoate + H2O + NAD+ = 5-amino-3-oxohexanoate + NH3 + NADH + H+

391432, 391434

-

1.4.1.B2

L-erythro-3,5-diaminohexanoate + H2O + NAD+ = 5-amino-3-oxohexanoate + NH3 + NADH + H+

696177

-

1.4.1.B2

L-erythro-3,5-diaminohexanoate + H2O + NADP+ = (S)-5-amino-3-oxohexanoate + NH3 + NADPH + H+

698741, 741483

-

1.4.1.B2

L-erythro-3,5-diaminohexanoate + H2O + NADP+ = 5-amino-3-oxohexanoate + NH3 + NADPH + H+

696177

-

1.4.1.B2

3 entries

In Vivo Product in Enzyme-catalyzed Reactions (1 result)

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Show Natural Product (1 entry)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

5.4.3.3

(3S)-3,6-diaminohexanoate = (3S,5S)-3,5-diaminohexanoate

0, 650175

-

Substrate in Enzyme-catalyzed Reactions (7 results)

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Show Substrate (7 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.4.1.11

L-erythro-3,5-diaminohexanoate + H2O + NAD+ = 5-amino-3-oxohexanoate + NADH + NH4+

391434

-

1.4.1.11

L-erythro-3,5-diaminohexanoate + H2O + NAD+ = 5-amino-3-oxohexanoate + NH3 + NADH + H+

391432, 391434

-

1.4.1.B2

L-erythro-3,5-diaminohexanoate + H2O + acetylpyridine-NAD+ = 5-amino-3-oxohexanoate + NH3 + acetylpyridine-NADH + H+

696177

-

1.4.1.B2

L-erythro-3,5-diaminohexanoate + H2O + deamino-NAD+ = 5-amino-3-oxohexanoate + NH3 + deamino-NADH + H+

696177

-

1.4.1.B2

L-erythro-3,5-diaminohexanoate + H2O + NAD+ = 5-amino-3-oxohexanoate + NH3 + NADH + H+

698741, 696177

-

1.4.1.B2

L-erythro-3,5-diaminohexanoate + H2O + NADP+ = (S)-5-amino-3-oxohexanoate + NH3 + NADPH + H+

698741, 741483, 762604

-

1.4.1.B2

L-erythro-3,5-diaminohexanoate + H2O + NADP+ = 5-amino-3-oxohexanoate + NH3 + NADPH + H+

696177

-

1.4.1.11

2 entries

1.4.1.B2

5 entries

Product in Enzyme-catalyzed Reactions (1 result)

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Show Product (1 entry)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

5.4.3.3

(3S)-3,6-diaminohexanoate = (3S,5S)-3,5-diaminohexanoate

0, 650175

-

Inhibitor in Enzyme-catalyzed Reactions (1 result)

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Show Inhibitors (1 entry)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.4.1.11

-

391432

-

Enzyme Kinetic Parameters

K_M Value (9 results)

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Show KM Value (9 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.4.1.11

0.18

-

pH 6.8, 24°C, tetrameric form of enzyme, pH 6.8

391434

1.4.1.11

0.22

-

pH 6.8, 24°C, tetrameric form of enzyme, above pH 6.8

391434

1.4.1.11

0.25

-

pH 6.6, 24°C, dimeric form of enzyme, pH 6.6

391434

1.4.1.11

0.75

-

pH 9.3

391432

1.4.1.11

0.77

-

pH 6.8, 24°C, tetrameric form of enzyme, pH 7.6 and pH 8.9

391434

1.4.1.B2

0.08

-

pH 7.4, in presence of 0.4 mM NADP+

696177

1.4.1.B2

0.16

-

pH 7.4, in presence of 0.4 mM NAD+

696177

1.4.1.B2

0.1978

-

in the presence of 1 mM NADP+

698741

1.4.1.B2

3.2

-

in the presence of 30 mM NAD+

698741

1.4.1.11

5 entries

1.4.1.B2

4 entries

References & Links

Literature References (7)

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Show Reference (7 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

391432

4692842

Aerobic metabolism of 3,5-diaminohexanoate in a Brevibacterium. Purification of 3,5-diaminohexanoate dehydrogenase and degradation of 3-keto-5-aminohexanoate

1973

Hong, S.C.L.; Barker, H.A.

J. Biol. Chem.

248

41-49

391434

4344229

Purification and properties of L-erythro-3,5-diaminohexanoate dehydrogenase from a lysine-fermenting Clostridium

1972

Baker, J.J.; Jeng, I.; Barker, H.A.

J. Biol. Chem.

247

7724-7734

650175

12093296

Identification of a novel pyridoxal 5'-phosphate binding site in adenosylcobalamin-dependent lysine 5,6-aminomutase from Porphyromonas gingivalis

2002

Tang, K.H.; Harms, A.; Frey, P.A.

Biochemistry

41

8767-8776

696177

4149230

Purification and properties of L-erythro-3,5-diaminohexanoate dehydrogenase from Clostridium sticklandii

1974

Baker, J.J.; van der Drift, C.

Biochemistry

13

292-299

698741

17166837

Identification of the last unknown genes in the fermentation pathway of lysine

2007

Kreimeyer, A.; Perret, A.; Lechaplais, C.; Vallenet, D.; Medigue, C.; Salanoubat, M.; Weissenbach, J.

J. Biol. Chem.

282

7191-7197

741483

-

Development of beta-amino acid dehydrogenase for the synthesis of beta-amino acids via reductive amination of beta-keto acids

2015

Zhang, D.; Chen, X.; Zhang, R.; Yao, P.; Wu, Q.; Zhu, D.

ACS Catal.

5

2220-2224

762604

33624917

Crystal structures and catalytic mechanism of L-erythro-3,5-diaminohexanoate dehydrogenase and rational engineering for asymmetric synthesis of beta-amino acids

2021

Liu, N.; Wu, L.; Feng, J.; Sheng, X.; Li, J.; Chen, X.; Li, J.; Liu, W.; Zhou, J.; Wu, Q.; Zhu, D.

Angew. Chem. Int. Ed. Engl.

60

10203-10210

Links to other databases for L-erythro-3,5-diaminohexanoate

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ChEBI

PubChem