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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
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MetaCyc Enzyme: NAD-dependent formate dehydrogenase

Species: Gottschalkia acidurici

Subunit composition of NAD-dependent formate dehydrogenase = [NAD-dependent formate dehydrogenase subunit]

Summary:
NAD-dependent formate dehydrogenase from Gottschalkia acidurici catalyzes a reversible reaction. While it catalyzes the oxidation of formate to CO2 as shown in the pathway purine nucleobases degradation II (anaerobic), it also catalyzes the reduction of the later to formate, which is then converted to acetate [Thauer73].

The enzyme has been partially purified and found to be a large enzyme complex (molecular weight of at least 200 kDa) that is very sensitive to oxygen and light [Kearny72]. The enzyme contains a L-selenocysteine [Heider93].

Crude preparations of the enzyme could be coupled to NAD reduction during formate oxidation through ferredoxin [Kearny72, Thauer73]. When the artificial electron acceptor methyl viologen was used instead of NAD, ferredoxin was not required [Kearny72]. Cyanide inhibited the enzyme 90%.

Basal formate oxidation activity in cell extracts was 0.85 μmol/min/mg protein, but increased 12 fold upon the addition of tungstate and selenite [Wagner77].

Interestingly, the enzyme from the related organism Clostridium cylindrosporum, while having a similar requirement for selenite, requires molybdate rather than tungstate, which has an antagonistic effect on it.

Molecular Weight of Multimer: 200 kD (experimental) [Kearny72]

Gene-Reaction Schematic: ?

Credits:
Created 30-Mar-2007 by Caspi R , SRI International


Enzymatic reaction of: NAD-dependent formate dehydrogenase

EC Number: 1.2.1.2

formate + NAD+ <=> CO2 + NADH

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction of enzyme catalysis.

This reaction is reversible.

In Pathways: purine nucleobases degradation I (anaerobic) , purine nucleobases degradation II (anaerobic)

Cofactors or Prosthetic Groups: W+6 [Wagner77]

Activators (Unknown Mechanism): Se0 [Wagner77]

Inhibitors (Other): hydrogen cyanide [Kearny72] , EDTA [Kearny72] , oxygen [Kearny72] , [Kearny72]

Kinetic Parameters:

Substrate
Km (μM)
Citations
formate
3100.0
[Kearny72]

pH(opt): 7.8-8.2 [Kearny72]


References

Heider93: Heider J, Bock A (1993). "Selenium metabolism in micro-organisms." Adv Microb Physiol 35;71-109. PMID: 8310883

Kearny72: Kearny JJ, Sagers RD (1972). "Formate dehydrogenase from Clostridium acidiurici." J Bacteriol 109(1);152-61. PMID: 4333376

Thauer73: Thauer RK (1973). "CO 2 reduction to formate in Clostridium acidi-urici." J Bacteriol 114(1);443-4. PMID: 4349033

Wagner77: Wagner R, Andreesen JR (1977). "Differentiation between Clostridium acidiurici and Clostridium cylindrosporum on the basis of specific metal requirements for formate dehydrogenase formation." Arch Microbiol 114(3);219-24. PMID: 911212


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Mon Dec 22, 2014, biocyc13.