Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

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

Show molfile
L-rhamnose
+
Show molfile
NAD(P)+
=
Show molfile
L-Rhamnono-1,4-lactone
+
Show molfile
NAD(P)H
+
Show molfile
H+

Synonyms

AvLRA1, AvRhaDH, EAT09360, L-rhamnose 1-dehydrogenase, LRA1, NAD(P)+-dependent L-rhamnose-1-dehydrogenase, RhaDH, SpLRA1

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                EC 1.1.1.3781.1.1.378 L-rhamnose 1-dehydrogenase [NAD(P)+]

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

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
-
the enzyme belongs to the short-chain dehydrogenase/reductase superfamily
physiological function
additional information
-
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