A report on Cofactor (biochemistry)

The succinate dehydrogenase complex showing several cofactors, including flavin, iron–sulfur centers, and heme.
A simple [Fe2S2] cluster containing two iron atoms and two sulfur atoms, coordinated by four protein cysteine residues.
The redox reactions of nicotinamide adenine dinucleotide.

Non-protein chemical compound or metallic ion that is required for an enzyme's role as a catalyst .

- Cofactor (biochemistry)
The succinate dehydrogenase complex showing several cofactors, including flavin, iron–sulfur centers, and heme.

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Bacillus stearothermophilus adenylate kinase

Adenylate kinase

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Phosphotransferase enzyme that catalyzes the interconversion of the various adenosine phosphates (ATP, ADP, and AMP).

Phosphotransferase enzyme that catalyzes the interconversion of the various adenosine phosphates (ATP, ADP, and AMP).

Bacillus stearothermophilus adenylate kinase
PDB image 3HPQ showing the ADK enzyme skeleton in cartoon and the key residues as sticks and labeled according to their placement in E. coli, crystallized with Ap5A inhibitor.
Residues of ADKE. coli involved in substrate binding
Describes the generic kinetic cycle of the ADK enzyme family. Ternary complex is labeled.

A magnesium cofactor is also required, essential for increasing the electrophilicity of the phosphate on AMP, though this magnesium ion is only held in the active pocket by electrostatic interactions and dissociates easily.

4Fe-4S clusters serve as electron-relays in proteins.

Bioinorganic chemistry

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Field that examines the role of metals in biology.

Field that examines the role of metals in biology.

4Fe-4S clusters serve as electron-relays in proteins.
Myoglobin is a prominent subject in bioinorganic chemistry, with particular attention to the iron-heme complex that is anchored to the protein.
Structure of FeMoco, the catalytic center of nitrogenase.
Like many antibiotics, monensin-A is an ionophore that tightly bind Na+ (shown in yellow).

These metals are used as protein cofactors and signalling molecules.

Tryptophan tryptophylquinone

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Tryptophan tryptophylquinone (TTQ) is an enzyme cofactor, generated by posttranslational modification of amino acids within the protein.

Thalassiosira weissflogii

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Species of centric diatoms, a unicellular microalga.

Species of centric diatoms, a unicellular microalga.

If zinc is deficient in the environment, the diatom switches to a different version of carbonic anhydrase enzyme, which uses cadmium instead of zinc as a cofactor.

Euler-Chelpin, May 1934

Hans von Euler-Chelpin

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German-born Swedish biochemist.

German-born Swedish biochemist.

Euler-Chelpin, May 1934

Harden discovered that the enzyme zymase, discovered by Eduard Buchner, only produces fermentation in interaction with the coenzyme cozymase.