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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+)

Inhibitors

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

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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,4-Diaminopentanoate
-
-
2,5-Diaminohexanoate
-
-
5-amino-3-oxohexanoate
-
competitive inhibition
ADP
-
about half as effective as ATP
AMP
-
32% as effective as ATP
arsenate
-
addition of any of the neutral salts causes a parabolic inhibition. A direct comparison of arsenate and chloride ion shows that arsenate is not as inhibitory even though it has a higher ionic strength. Arsenate interacts with the enzyme differently from chloride and bromide. Sulfate, which is a large ion like arsenate, is as inhibitory as chloride (at equivalent ionic strength) with NAD+ as coenzyme, but it is much less effective than chloride with NADP+ as coenzyme
ATP
-
competitive with respect to L-erythro-3,5-diaminohexanoate and NAD+
Br-
-
addition of any of the neutral salts causes a parabolic inhibition. A direct comparison of arsenate and chloride ion shows that arsenate is not as inhibitory even though it has a higher ionic strength. Arsenate interacts with the enzyme differently from chloride and bromide. Sulfate, which is a large ion like arsenate, is as inhibitory as chloride (at equivalent ionic strength) with NAD+ as coenzyme, but it is much less effective than chloride with NADP+ as coenzyme
Ca2+
-
0.5 mM, 22% inhibition at pH 7.8, cofactor NADP+, activation at pH 8.9
Cl-
-
addition of any of the neutral salts causes a parabolic inhibition. A direct comparison of arsenate and chloride ion shows that arsenate is not as inhibitory even though it has a higher ionic strength. Arsenate interacts with the enzyme differently from chloride and bromide. Sulfate, which is a large ion like arsenate, is as inhibitory as chloride (at equivalent ionic strength) with NAD+ as coenzyme, but it is much less effective than chloride with NADP+ as coenzyme
Co2+
-
0.5 mM, 71% inhibition at pH 7.8, cofactor NADP+, activation at pH 8.9
CTP
-
about half as effective as ATP
Cu2+
-
0.5 mM, 35% inhibition at pH 7.8, 30% inhibition at pH 8.9, cofactor NADP+
D-erythro-3,5-diaminohexanoate
-
-
DL-beta-aminobutyrate
-
-
Fe2+
-
0.5 mM, 36% inhibition at pH 7.8, 9% inhibition at pH 8.9, cofactor NADP+
Fe3+
-
0.5 mM, 8% inhibition at pH 8.9, no effect on activity at pH 7.8
GTP
-
inhibits as effectively as ATP
Mg2+
-
0.5 mM, 63% inhibition at pH 7.8, cofactor NADP+, activation at pH 8.9
Mn2+
-
0.5 mM, 52% inhibition at pH 7.8, cofactor NADP+, activation at pH 8.9
NADH
-
competitive inhibition
NADPH
NH4+
-
10 mM NH4Cl and higher, inhibits the reaction, probably due to the effect of chloride on the activity
SO42-
-
addition of any of the neutral salts causes a parabolic inhibition. A direct comparison of arsenate and chloride ion shows that arsenate is not as inhibitory even though it has a higher ionic strength. Arsenate interacts with the enzyme differently from chloride and bromide. Sulfate, which is a large ion like arsenate, is as inhibitory as chloride (at equivalent ionic strength) with NAD+ as coenzyme, but it is much less effective than chloride with NADP+ as coenzyme
UTP
-
16% as effective as ATP
Zn2+
-
0.5 mM, 49% inhibition at pH 7.8, cofactor NADP+, activation at pH 8.9
additional information
-
the lactams of DL-erythro-3,5-diaminohexanoate and DL-threo-3,5-diaminohexanoatae and 2-methylpyrrolidone-5-carboxylic acid have no effect on activity. Acetate (10 mM), butyrate (10 mM), acetyl phosphate (2 mM), or acetyl-CoA (0.62 mM) have no effect on enzyme activity
-