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1.1.99.38: 2-deoxy-scyllo-inosamine dehydrogenase (AdoMet-dependent)

This is an abbreviated version!
For detailed information about 2-deoxy-scyllo-inosamine dehydrogenase (AdoMet-dependent), go to the full flat file.

Reaction

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2-deoxy-scyllo-inosamine
+
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S-adenosyl-L-methionine
=
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3-amino-2,3-dideoxy-scyllo-inosose
+
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5'-deoxyadenosine
+
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L-methionine

Synonyms

BtrN, DOIA dehydrogenase

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.99 With unknown physiological acceptors
                EC 1.1.99.381.1.99.38 2-deoxy-scyllo-inosamine dehydrogenase (AdoMet-dependent)

Crystallization

Crystallization on EC 1.1.99.38 - 2-deoxy-scyllo-inosamine dehydrogenase (AdoMet-dependent)

for references in articles please use BRENDA:EC1.1.99.38

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
analysis of electron paramagnetic resonance signals for free enzyme, the enzyme-S-adenosyl-L-methionine complex, and a rhombic signal presumably derived from the enzyme-S-adenosyl-L-methionine-substrate ternary complex show close interaction of both S-adenosyl-L-methione and 2-deoxy-scyllo-inosamine with the [4Fe-4S] cluster
in complex with AdoMet and substrate, to 1.56 A resolution. Structure displays a modification to the core AdoMet radical fold, instead of the canonical (beta/alpha)6 architecture, BtrN displays a (beta5/alpha4) motif. An auxiliary [4Fe-4S] cluster in BtrN, thought to bind substrate, is instead implicated in substrate-radical oxidation