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The biochemical pathways required to utilize glucose as a carbon and energy source are highly conserved from bacteria to humans. PGM1 is an evolutionarily conserved enzyme that regulates one of the most important metabolic carbohydrate trafficking points in prokaryotic and eukaryotic organisms, catalyzing the bi-directional interconversion of glucose 1-phosphate (G-1-P) and glucose 6-phosphate ...
Aspartate transaminase (AST) or aspartate aminotransferase, also known as AspAT/ASAT/AAT or (serum) glutamic oxaloacetic transaminase (GOT, SGOT), is a pyridoxal phosphate (PLP)-dependent transaminase enzyme (EC 2.6.1.1) that was first described by Arthur Karmen and colleagues in 1954.
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 ...
Aspartoacylase is a hydrolytic enzyme (EC 3.5.1.15, also called aminoacylase II, ASPA and other names [a]) that in humans is encoded by the ASPA gene.ASPA catalyzes the deacylation of N-acetyl-l-aspartate (N-acetylaspartate) into aspartate and acetate.
952 12494 Ensembl ENSG00000004468 ENSMUSG00000029084 UniProt P28907 P56528 RefSeq (mRNA) NM_001775 NM_007646 RefSeq (protein) NP_001766 NP_031672 Location (UCSC) Chr 4: 15.78 – 15.85 Mb Chr 5: 44.03 – 44.07 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse CD38 (cluster of differentiation 38), also known as cyclic ADP ribose hydrolase, is a glycoprotein found on the surface of many ...
The systematic name of this enzyme class is 2-methylacyl-CoA 2-epimerase. In vitro experiments with the human enzyme AMACR 1A show that both (2S)- and (2R)-methyldecanoyl-CoA esters are substrates and are converted by the enzyme with very similar efficiency. Prolonged incubation of either substrate with the enzyme establishes an equilibrium ...
Stromelysin-1 also known as matrix metalloproteinase-3 (MMP-3) is an enzyme that in humans is encoded by the MMP3 gene. The MMP3 gene is part of a cluster of MMP genes which localize to chromosome 11q22.3. [5] MMP-3 has an estimated molecular weight of 54 kDa. [6]
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]