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

BRENDA support

Literature summary for 1.1.99.37 extracted from

  • Kloosterman, H.; Vrijbloed, J.W.; Dijkhuizen, L.
    Molecular, biochemical, and functional characterization of a Nudix hydrolase protein that stimulates the activity of a nicotinoprotein alcohol dehydrogenase (2002), J. Biol. Chem., 277, 34785-34792.
    View publication on PubMed
Search for more literature for 1.1.99.37

Activating Compound

Activating Compound Comment Organism Structure
additional information the low coenzyme NAD-dependent activity of MDH with C1-C4 primary alcohols is strongly stimulated by Bacillus methanolicus protein ACT, in presence of NAD(H) cofactor and Mg2+-ions. In the deduced ACT amino acid sequence, the highly conserved amino acid sequence motif typical of Nudix hydrolase proteins is present. MDH activation by ACT involves hydrolytic removal of the nicotinamide mononucleotide NMN(H) moiety of the NAD(H) cofactor of MDH, changing its Ping-Pong type of reaction mechanism into a ternary complex reaction mechanism Bacillus methanolicus

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Bacillus methanolicus

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm
-
 Bacillus methanolicus 5737
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ one zinc and two magnesium ions per subunit. Mg2+ is essential for binding of the NAD(H) cofactor Bacillus methanolicus
Zn2+ one zinc and two magnesium ions per subunit Bacillus methanolicus

Organism

Organism UniProt Comment Textmining
Bacillus methanolicus
-
-
-

Reaction

Reaction Comment Organism Reaction ID
methanol + acceptor = formaldehyde + reduced acceptor the low coenzyme NAD-dependent activity of MDH with C1-C4 primary alcohols is strongly stimulated by Bacillus methanolicus protein ACT, in presence of NAD(H) cofactor and Mg2+-ions. MDH activation by ACT involves hydrolytic removal of the nicotinamide mononucleotide NMN(H) moiety of the NAD(H) cofactor of MDH, changing its Ping-Pong type of reaction mechanism into a ternary complex reaction mechanism Bacillus methanolicus
a

Synonyms

Synonyms Comment Organism
MDH
-
 Bacillus methanolicus

Cofactor

Cofactor Comment Organism Structure
NAD+ Mg2+ is essential for binding of the NAD(H) cofactor Bacillus methanolicus
NADH Mg2+ is essential for binding of the NAD(H) cofactor Bacillus methanolicus