1.1.1.378: L-rhamnose 1-dehydrogenase [NAD(P)+]
This is an abbreviated version!
For detailed information about L-rhamnose 1-dehydrogenase [NAD(P)+], go to the full flat file.
Reaction
Synonyms
AvLRA1, AvRhaDH, EAT09360, L-rhamnose 1-dehydrogenase, LRA1, NAD(P)+-dependent L-rhamnose-1-dehydrogenase, RhaDH, SpLRA1
ECTree
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General Information
General Information on EC 1.1.1.378 - L-rhamnose 1-dehydrogenase [NAD(P)+]
for references in articles please use BRENDA:EC1.1.1.378
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evolution
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the enzyme belongs to the short-chain dehydrogenase/reductase superfamily
physiological function
additional information
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structure-function analysis, overview. The side chains of Ser146 and Tyr159, Ser148 and Gln156, Thr191, and Asn197 and one water molecular (Wat23) form hydrogen bonds with the hydroxyl groups of C1, C2, C3, and C4 of L-rhamnose, respectively. Wat23 also interacts with the side chains of Asp200, and Lys163 formed hydrogen bond network with the main chains of Ala94 and Asn117 via one water molecular (Wat41). Among these residues, Ser146-Tyr159-Lys163, corresponding to a motif of the catalytic triad, and Ala94 and Asn117 are completely conserved in SDR superfamily enzymes. Phe99 appears to be more important for enzyme catalysis than Ile196
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first enzyme of the non-phosphorylative L-rhamnose pathway in archaea, that is analogous to the Entner-Doudoroff pathway
physiological function
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several microorganisms can utilize L-rhamnose as a carbon and energy source through the non-phosphorylative metabolic pathway, in which L-rhamnose 1-dehydrogenase (RhaDH) catalyzes the NAD(P)+-dependent oxidization of Lrhamnose to L-rhamnono-1,4-lactone
physiological function
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first enzyme of the non-phosphorylative L-rhamnose pathway in archaea, that is analogous to the Entner-Doudoroff pathway
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