Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
Review
. 2011:77:307-60.
doi: 10.1002/9780470920541.ch7.

A survey of oxidative paracatalytic reactions catalyzed by enzymes that generate carbanionic intermediates: implications for ROS production, cancer etiology, and neurodegenerative diseases

Victoria I Bunik  1 , John V Schloss, John T Pinto, Natalia Dudareva, Arthur J L Cooper
Affiliations
Review

A survey of oxidative paracatalytic reactions catalyzed by enzymes that generate carbanionic intermediates: implications for ROS production, cancer etiology, and neurodegenerative diseases

Victoria I Bunik et al. Adv Enzymol Relat Areas Mol Biol. 2011.
No abstract available

PubMed Disclaimer

Figures

Figure 1
Figure 1
Proposed mechanism for the phenylacetaldehyde synthase (PAAS)-catalyzed reaction leading to biosynthesis of phenylacetaldehyde from l-phenylalanine. For details see the text. [Modified from (57).]
Figure 2
Figure 2
α-Ketoglutarate dehydrogenase complex (KGDHC)–catalyzed reaction. In the first step, KG reacts with the ThDP cofactor and is decarboxylated to generate CO2 and active aldehyde (carbanion) at the active site of E1k (step 1). In the second step, ThDP is regenerated in the E1k-catalyzed reductive transacylation reaction with the lipoyl residue covalently bound to E2k (step 2). This thio ester contains a high-energy bond as depicted by ~. In the next step, at the active site of E2k, coenzyme A reacts with the succinyl dihydrolipoyl thio ester to generate the high-energy compound succinyl CoA and a dihydrolipoyl residue (step 3). Subsequently, a disulfide linkage in the dihydrolipoyl residue is regenerated concomitant with the 2e− reduction of E3(S-S)·FAD (step 4), which in turn is reoxidized back with NAD+ (step 5). [From (115), with permission.]
Figure 3
Figure 3
Formation of KGDHC-dependent radical species and the thioredoxin-catalyzed dismutation of KGDHC-bound dihydrolipoyl radicals. For a detailed discussion, see the text. [Modified from (82).]
See this image and copyright information in PMC

Similar articles

See all similar articles

Cited by

See all "Cited by" articles

References

    1. Healy MJ, Christen P. Reaction of the carbanionic aldolase-substrate intermediate with tetranitromethane: identification of the products, hydroxypyruvaldehyde phosphate and D-5-ketofructose 1,6-diphosphate. J. Am. Chem. Soc. 1972;94:7911–7916. - PubMed
    1. Healy MJ, Christen P. Mechanistic probes for enzymatic reactions: oxidation–reduction indicators as oxidants of intermediary carbanions (studies with aldolase, aspartate aminotransferase, pyruvate decarboxylase, and 6-phosphogluconate dehydrogenase) Biochemistry. 1973;12:35–41. - PubMed
    1. Christen P, Anderson TK, Healy MJ. H2O2 oxidizes an aldolase dihydroxyacetone phosphate intermediate to hydroxymethylglyoxal phosphate. Experientia. 1974;30:603–605. - PubMed
    1. Christen P, Gasser A. Oxidation of the carbanion intermediate of transaldolase by hexacyanoferrate(III) J. Biol. Chem. 1976;251:4220–4223. - PubMed
    1. Christen P, Cogoli-Greuter M, Healy MJ, Lubini D. Specific irreversible inhibition of enzymes concomitant to the oxidation of carbanionic enzyme– substrate intermediates by hexacyanoferrate(III) Eur. J. Biochem. 1976;63:223–231. - PubMed

Publication types

LinkOut - more resources