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The reaction it catalyzes is: pyruvate + HCO − 3 + ATP → oxaloacetate + ADP + P. It is an important anaplerotic reaction that creates oxaloacetate from pyruvate. PC contains a biotin prosthetic group [1] and is typically localized to the mitochondria in eukaryotes with exceptions to some fungal species such as Aspergillus nidulans which have a cytosolic PC.
1559 72303 Ensembl ENSG00000138109 ENSMUSG00000067231 UniProt P11712 n/a RefSeq (mRNA) NM_000771 NM_028191 RefSeq (protein) NP_000762 n/a Location (UCSC) Chr 10: 94.94 – 94.99 Mb Chr 19: 39.05 – 39.08 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Cytochrome P450 family 2 subfamily C member 9 (abbreviated CYP2C9) is an enzyme protein. The enzyme is involved in the metabolism, by ...
Human enzymes start to denature quickly at temperatures above 40 °C. Enzymes from thermophilic archaea found in the hot springs are stable up to 100 °C. [13] However, the idea of an "optimum" rate of an enzyme reaction is misleading, as the rate observed at any temperature is the product of two rates, the reaction rate and the denaturation rate.
In biochemistry, an oxidoreductase is an enzyme that catalyzes the transfer of electrons from one molecule, the reductant, also called the electron donor, to another, the oxidant, also called the electron acceptor. This group of enzymes usually utilizes NADP+ or NAD+ as cofactors.
Lipoxygenases (EC 1.13.11.-) (LOX) are a family of (non-heme) iron-containing enzymes, more specifically oxidative enzymes, most of which catalyze the dioxygenation of polyunsaturated fatty acids in lipids containing a cis,cis-1,4-pentadiene into cell signaling agents that serve diverse roles as autocrine signals that regulate the function of their parent cells, paracrine signals that regulate ...
Nitrogenase is an enzyme responsible for catalyzing nitrogen fixation, which is the reduction of nitrogen (N 2) to ammonia (NH 3) and a process vital to sustaining life on Earth. [9] There are three types of nitrogenase found in various nitrogen-fixing bacteria: molybdenum (Mo) nitrogenase, vanadium (V) nitrogenase , and iron-only (Fe ...
The overall fold of the monomer is very similar to that of other PLP-dependent enzymes of the Beta-family. The enzyme contains a large catalytic domain that binds PLP and a small domain. The domains are linked by two residues 32-35 and 138-146, with the internal gap created being the space for the active site [1]