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T. maritima Browser
1vk6
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Protein Summary
The gene 1790429 from Escherichia coli encodes the enzyme NADH pyrophosphatase E.C.3.6.1.22, a member of an NADH pyrophosphatase subfamily of the Nudix hydrolases PF00293. The enzyme catalyzes the cleavage of NADH into reduced nicotinamide mononucleotide (NMNH) and AMP. Like other members of the Nudix family, it requires a divalent cation, such as Mg2+ or Mn2+, for activity. The amino acid motif getleqavarevmeesgi is highly conserved among family members and functions as a metal binding and catalytic site. The E.coli enzyme contains three cleary defined structural domains with specific functions: a rudimentary NUDIX-like domain PF09296, a NADH pyrophosphatase zinc ribbon domain PF09297, and NUDIX domain. It appears to be the first structure available with such a quaternary arrangement of these domains. The structure of this enzyme has also been solved in a different crystal form 2GB5. The two structures present a similar dimeric architecture (for 1vk6 the second subunit is generated by crystallographic symmetry). All three domains contribute to the dimerization interface.
Ligand Summary
References
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References
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