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1.4.1.B2: L-erythro-3,5-diaminohexanoate dehydrogenase (NADP+)

This is an abbreviated version!
For detailed information about L-erythro-3,5-diaminohexanoate dehydrogenase (NADP+), go to the full flat file.

Reaction

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

Synonyms

3,5-DAHDH, Kdd

ECTree

     1 Oxidoreductases
         1.4 Acting on the CH-NH2 group of donors
             1.4.1 With NAD+ or NADP+ as acceptor
                1.4.1.B2 L-erythro-3,5-diaminohexanoate dehydrogenase (NADP+)

Reference

Reference on EC 1.4.1.B2 - L-erythro-3,5-diaminohexanoate dehydrogenase (NADP+)

Please use the Reference Search for a specific query.
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Baker, J.J.; van der Drift, C.
Purification and properties of L-erythro-3,5-diaminohexanoate dehydrogenase from Clostridium sticklandii
Biochemistry
13
292-299
1974
Acetoanaerobium sticklandii
Manually annotated by BRENDA team
Kreimeyer, A.; Perret, A.; Lechaplais, C.; Vallenet, D.; Medigue, C.; Salanoubat, M.; Weissenbach, J.
Identification of the last unknown genes in the fermentation pathway of lysine
J. Biol. Chem.
282
7191-7197
2007
unidentified (A1X0G6)
Manually annotated by BRENDA team
Zhang, D.; Chen, X.; Zhang, R.; Yao, P.; Wu, Q.; Zhu, D.
Development of beta-amino acid dehydrogenase for the synthesis of beta-amino acids via reductive amination of beta-keto acids
ACS Catal.
5
2220-2224
2015
Candidatus Cloacimonas acidaminovorans
-
Manually annotated by BRENDA team
Liu, N.; Wu, L.; Feng, J.; Sheng, X.; Li, J.; Chen, X.; Li, J.; Liu, W.; Zhou, J.; Wu, Q.; Zhu, D.
Crystal structures and catalytic mechanism of L-erythro-3,5-diaminohexanoate dehydrogenase and rational engineering for asymmetric synthesis of beta-amino acids
Angew. Chem. Int. Ed. Engl.
60
10203-10210
2021
Candidatus Cloacimonas acidaminovorans (B0VJ11), Candidatus Cloacimonas acidaminovorans Evry (B0VJ11)
Manually annotated by BRENDA team