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In biology, a substrate is the surface on which an organism (such as a plant, fungus, or animal) lives.A substrate can include biotic or abiotic materials and animals. For example, encrusting algae that lives on a rock (its substrate) can be itself a substrate for an animal that lives on top of the algae.
In molecular biology, substrate presentation is a biological process that activates a protein. The protein is sequestered away from its substrate and then activated by release and exposure to its substrate. [1] [2] A substrate is typically the substance on which an enzyme acts but can also be a protein surface to which a ligand binds. In the ...
n/a Ensembl n/a n/a UniProt n a n/a RefSeq (mRNA) n/a n/a RefSeq (protein) n/a n/a Location (UCSC) n/a n/a PubMed search n/a n/a Wikidata View/Edit Human Glucose transporter 1 (or GLUT1), also known as solute carrier family 2, facilitated glucose transporter member 1 (SLC2A1), is a uniporter protein that in humans is encoded by the SLC2A1 gene. GLUT1 facilitates the transport of glucose across ...
Thiamine pyrophosphate (TPP or ThPP), or thiamine diphosphate (ThDP), or cocarboxylase [1] is a thiamine (vitamin B 1) derivative which is produced by the enzyme thiamine diphosphokinase. Thiamine pyrophosphate is a cofactor that is present in all living systems, in which it catalyzes several biochemical reactions.
Strain M.o.H.: 4 H 2 + CO 2 → Methane + 2 H 2 O (ΔG°' = -131 kJ per reaction) Co-culture: 2 Ethanol + CO 2 → 2 Acetate − + 2 H + + Methane (ΔG°' = -113 kJ per reaction) The oxidization of ethanol by organism S is made possible thanks to the methanogen M.o.H, which consumes the hydrogen produced by organism S, by turning the positive ...
In biology and biochemistry, the active site is the region of an enzyme where substrate molecules bind and undergo a chemical reaction. The active site consists of amino acid residues that form temporary bonds with the substrate, the binding site , and residues that catalyse a reaction of that substrate, the catalytic site .
[4] [22] The binding of a ligand to an allosteric site of a multimeric enzyme often induces positive cooperativity, that is the binding of one substrate induces a favorable conformation change and increases the enzyme's likelihood to bind to a second substrate. [23]
[1] Aspartic endopeptidases EC 3.4.23. of vertebrate, fungal and retroviral origin have been characterised. [2] More recently, aspartic endopeptidases associated with the processing of bacterial type 4 prepilin [3] and archaean preflagellin have been described. [4] [5] Eukaryotic aspartic proteases include pepsins, cathepsins, and renins. They ...