1.1.1.12: L-arabinitol 4-dehydrogenase

This is an abbreviated version, for detailed information about L-arabinitol 4-dehydrogenase, go to the full flat file.

Reaction

L-arabinitol
+
NAD+
=
L-xylulose
+
NADH
+
H+

Synonyms

dehydrogenase, L-arabinitol, L-arabitol dehydrogenase, LAD, pentitol-DPN dehydrogenase

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.12 L-arabinitol 4-dehydrogenase

Crystallization

Crystallization on EC 1.1.1.12 - L-arabinitol 4-dehydrogenase

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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
modelling of LadA on human SDH identifies residues M70 and Y318 in LadA, that may explain the absence of activity on D-sorbitol
-
molecular replacement method using the coordinates of human sorbitol dehydrogenase, PDB ID 1PL8. Each monomer contains a bidomain architecture composed of a large catalytic domain of residues Ala5 through Val167, and residues Arg308 through Leu362, and a smaller cofactor-binding domain with residues Ala168 through Tyr307, with a large cleft separating the two domains
docking study with the substrate L-arabinitol, Zn2+ and NAD+ reveals a catalytic Zn2+ binding domain involving residues Cys66, His91, Glu92 and Glu176, and a cofactor NAD+ binding domain involving residues Gly202, ILeu204, Gly205, Cys273, Arg229 and Val298, with strong hydrogen bonding contacts with the substrate and cofactor
-