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
Synonyms
3,5-DAHDH, Kdd
ECTree
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Inhibitors
Inhibitors on EC 1.4.1.B2 - L-erythro-3,5-diaminohexanoate dehydrogenase (NADP+)
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arsenate
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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
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competitive with respect to L-erythro-3,5-diaminohexanoate and NAD+
Br-
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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+
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0.5 mM, 22% inhibition at pH 7.8, cofactor NADP+, activation at pH 8.9
Cl-
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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+
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0.5 mM, 71% inhibition at pH 7.8, cofactor NADP+, activation at pH 8.9
Cu2+
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0.5 mM, 35% inhibition at pH 7.8, 30% inhibition at pH 8.9, cofactor NADP+
Fe2+
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0.5 mM, 36% inhibition at pH 7.8, 9% inhibition at pH 8.9, cofactor NADP+
Fe3+
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0.5 mM, 8% inhibition at pH 8.9, no effect on activity at pH 7.8
Mg2+
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0.5 mM, 63% inhibition at pH 7.8, cofactor NADP+, activation at pH 8.9
Mn2+
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0.5 mM, 52% inhibition at pH 7.8, cofactor NADP+, activation at pH 8.9
NH4+
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10 mM NH4Cl and higher, inhibits the reaction, probably due to the effect of chloride on the activity
SO42-
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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
Zn2+
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0.5 mM, 49% inhibition at pH 7.8, cofactor NADP+, activation at pH 8.9
additional information
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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
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