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Organic enzyme cofactors are involved in many enzyme reactions. Therefore, the analysis of cofactors is crucial to gain a better understanding of enzyme catalysis. To aid this, we have created the CoFactor database.
CoFactor provides a web interface to access hand-curated data extracted from the literature on organic enzyme cofactors in biocatalysis, as well as automatically collected information. CoFactor includes information on the conformational and solvent accessibility variation of the enzyme-bound cofactors, as well as mechanistic and structural information about the hosting enzymes.
The database is publicly available and can be accessed at http://www.ebi.ac.uk/thornton-srv/databases/CoFactor.
EMBL-EBI, Wellcome Trust Genome Campus, Hinxton, Cambridge CB10 1SD, UK.
This article was published in the following journal.
Name: Bioinformatics (Oxford, England)
RNA enzymes (ribozymes) have remarkably diverse biological roles despite having limited chemical diversity. Protein enzymes enhance their reactivity through recruitment of cofactors; likewise, the nat...
We introduce a strategy that expands the functionality of hemoproteins through orthogonal enzyme/heme pairs. By exploiting the ability of a natural heme transport protein, ChuA, to promiscuously impor...
'Heavy' (isotopically-labeled) enzyme isotope effects offer a direct experimental probe of the role of protein vibrations on enzyme-catalyzed reactions. Here we have developed a strategy to generate i...
Guanosine-5'-monophosphate reductase (GMPR) catalyzes the reduction of GMP to IMP and ammonia with concomitant oxidation of NADPH. Here we investigated the structure and dynamics of enzyme-bound subst...
Life originated in an anoxic, Fe2+-rich environment. We hypothesize that on early Earth, Fe2+ was a ubiquitous cofactor for nucleic acids, with roles in RNA folding and catalysis as well as in process...
The objectives of this trial are to determine if CoFactor in combination with 5-FU are effective in the treatment of metastatic colorectal cancer and to determine the side effects observed...
Molybdenum Cofactor Deficiency Type A (MoCD) is a very rare autosomal recessive disorder that is essentially fatal early in life. Naturally occurring cPMP is present in the body of all hea...
A multi-center, open-label, single-arm Phase II trial assessing the efficacy and safety of weekly bolus infusions of 5-fluorouracil combined with CoFactor (5-10 methylenetetrahydrofolate) ...
The study aims to evaluate the hypothesized benefits of a systematic organic diet for children, over those of a conventional diet. The specific objectives of this study are to: i) Demonstr...
Lactic acidosis is a potentially life-threatening disease associated with the treatment of chronic HIV infection. Although acidosis is rare, hyperlactatemia is common and may have long ter...
The protein components of enzyme complexes (HOLOENZYMES). An apoenzyme is the holoenzyme minus any cofactors (ENZYME COFACTORS) or prosthetic groups required for the enzymatic function.
An aldehyde oxidoreductase expressed predominantly in the LIVER; LUNGS; and KIDNEY. It catalyzes the oxidation of a variety of organic aldehydes and N-heterocyclic compounds to CARBOXYLIC ACIDS, and also oxidizes quinoline and pyridine derivatives. The enzyme utilizes molybdenum cofactor and FAD as cofactors.
Conversion of an inactive form of an enzyme to one possessing metabolic activity. It includes 1, activation by ions (activators); 2, activation by cofactors (coenzymes); and 3, conversion of an enzyme precursor (proenzyme or zymogen) to an active enzyme.
An iron-sulfur and MOLYBDENUM containing FLAVOPROTEIN that catalyzes the oxidation of nitrite to nitrate. This enzyme can use either NAD or NADP as cofactors. It is a key enzyme that is involved in the first step of nitrate assimilation in PLANTS; FUNGI; and BACTERIA. This enzyme was formerly classified as EC 22.214.171.124.
An enzyme found primarily in BACTERIA and FUNGI that catalyzes the oxidation of ammonium hydroxide to nitrite. It is an iron-sulfur HEME; FLAVOPROTEIN containing siroheme and can utilize both NAD and NADP as cofactors. This enzyme was formerly classified as EC 126.96.36.199.
Enzymes are proteins that catalyze (i.e., increase the rates of) chemical reactions. In enzymatic reactions, the molecules at the beginning of the process, called substrates, are converted into different molecules, called products. Almost all chemical re...
Bioinformatics is the application of computer software and hardware to the management of biological data to create useful information. Computers are used to gather, store, analyze and integrate biological and genetic information which can then be applied...