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5′-Nucleotidase (EC 3.1.3.5) is an enzyme which catalyzes the phosphorylytic cleavage of 5′-nucleotides. [2] Although originally found in snake venom, [ 3 ] the activity of 5'nucleotidase has been described for bacteria and plant cells, and is widely distributed in vertebrate tissue. [ 4 ]
In biochemistry, isozymes (also known as isoenzymes or more generally as multiple forms of enzymes) are enzymes that differ in amino acid sequence but catalyze the same chemical reaction. Isozymes usually have different kinetic parameters (e.g. different K M values), or are regulated differently.
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 ...
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.
Adenosine triphosphate Adenosine diphosphate Adenosine monophosphate. ATPases (EC 3.6.1.3, Adenosine 5'-TriPhosphatase, adenylpyrophosphatase, ATP monophosphatase, triphosphatase, SV40 T-antigen, ATP hydrolase, complex V (mitochondrial electron transport), (Ca 2+ + Mg 2+)-ATPase, HCO 3 −-ATPase, adenosine triphosphatase) are a class of enzymes that catalyze the decomposition of ATP into ADP ...
Thus, the two substrates of this enzyme are pyruvate and d-glyceraldehyde 3-phosphate, whereas its two products are 1-deoxy-d-xylulose 5-phosphate and CO 2. This enzyme belongs to the family of transferases, specifically those transferring aldehyde or ketonic groups (transaldolases and transketolases, respectively). The systematic name of this ...
The Klenow fragment is a large protein fragment produced when DNA polymerase I from E. coli is enzymatically cleaved by the protease subtilisin.First reported in 1970, [1] it retains the 5' → 3' polymerase activity and the 3’ → 5’ exonuclease activity for removal of precoding nucleotides and proofreading, but loses its 5' → 3' exonuclease activity.