MetaCyc Enzyme: ribitol dehydrogenase

Gene: rbtD Accession Number: G-9462 (MetaCyc)

Synonyms: ribitol 2-dehydrogenase

Species: Enterobacter aerogenes

Subunit composition of ribitol dehydrogenase = [RbtD]4
         ribitol dehydrogenase subunit = RbtD

The native molecular mass was determined by sedimentation equilibrium analysis [Taylor74].
The subunit molecular mass was determined by SDS-PAGE [Taylor74].

Molecular Weight of Polypeptide: 26.514 kD (from nucleotide sequence), 27 kD (experimental) [Taylor74 ]

Molecular Weight of Multimer: 118 kD (experimental) [Taylor74]

Unification Links: Protein Model Portal:P00335 , UniProt:P00335

Relationship Links: Entrez-Nucleotide:PART-OF:M25606 , InterPro:IN-FAMILY:IPR002198 , InterPro:IN-FAMILY:IPR002347 , InterPro:IN-FAMILY:IPR016040 , InterPro:IN-FAMILY:IPR020904 , Pfam:IN-FAMILY:PF00106 , Prints:IN-FAMILY:PR00081 , Prosite:IN-FAMILY:PS00061

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

Enzymatic reaction of: ribitol dehydrogenase

EC Number:

ribitol + NAD+ <=> D-ribulose + NADH + H+

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.

In Pathways: superpathway of pentose and pentitol degradation , ribitol degradation

NAD+ protected the enzyme against inhibition by o-phenanthroline, diethyldithiocarbamate, mercuric chloride, and p-chloromercuribenzoate [Taylor74].

Inhibitors (Competitive): L-dithiothreitol [Taylor74] , 2-mercaptoethanol [Taylor74]

Inhibitors (Unknown Mechanism): Hg2+ [Taylor74] , diethyldithiocarbamate [Taylor74] , o-phenanthroline [Taylor74] , p-chloromercuribenzoate [Taylor74]


Taylor74: Taylor SS, Rigby PW, Hartley BS (1974). "Ribitol dehydrogenase from Klebsiella aerogenes. Purification and subunit structure." Biochem J 141(3);693-700. PMID: 4618776

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Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
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