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  • gene
  • gene, encoding Granule Bound Starch Synthase (GBSS) that synthesizes amylose, results in starch granules containing mostly amylopectin. (apsnet.org)
  • The regions of the placental mammals' genomes expected to code for malate synthase, as determined by comparison of the gene orders in vertebrate genomes, show clear similarity to the opossum MS sequence but contain stop codons, indicating that the MS gene became a pseudogene in placental mammals. (geuvadis.org)
  • Beta
  • In synthase II, each subunit consists of a five-stranded beta pleated sheet surrounded by multiple alpha helices, shown in the image below. (wikipedia.org)
  • enzymology
  • In enzymology, a pentalenene synthase (EC 4.2.3.7) is an enzyme that catalyzes the chemical reaction 2-trans,6-trans-farnesyl diphosphate ⇌ {\displaystyle \rightleftharpoons } pentalenene + diphosphate Hence, this enzyme has one substrate, 2-trans,6-trans-farnesyl diphosphate, and two products, pentalenene and diphosphate. (wikipedia.org)
  • In enzymology, a sphingomyelin synthase (EC 2.7.8.27) is an enzyme that catalyzes the chemical reaction a ceramide + a phosphatidylcholine ⇌ {\displaystyle \rightleftharpoons } a sphingomyelin + a 1,2-diacyl-sn-glycerol Thus, the two substrates of this enzyme are ceramide and phosphatidylcholine, whereas its two products are sphingomyelin and 1,2-diacyl-sn-glycerol. (wikipedia.org)
  • In enzymology, a biotin synthase (EC 2.8.1.6) is an enzyme that catalyzes the chemical reaction dethiobiotin + sulfur + 2 S-adenosyl-L-methionine ⇌ {\displaystyle \rightleftharpoons } biotin + 2 L-methionine + 2 5'-deoxyadenosine The 3 substrates of this enzyme are dethiobiotin, sulfur, and S-adenosyl-L-methionine, whereas its 3 products are biotin, L-methionine, and 5'-deoxyadenosine. (wikipedia.org)
  • In enzymology, a pterocarpin synthase (EC 1.1.1.246) is an enzyme that catalyzes the chemical reaction medicarpin + NADP+ + H2O ⇌ {\displaystyle \rightleftharpoons } vestitone + NADPH + H+ The 3 substrates of this enzyme are medicarpin, NADP+, and H2O, whereas its 3 products are vestitone, NADPH, and H+. (wikipedia.org)
  • Mechanism
  • Crystal structure of Mycobacterium tuberculosis 7,8-dihydropteroate synthase in complex with pterin monophosphate: new insight into the enzymatic mechanism and sulfa-drug action. (ebi.ac.uk)
  • Mitochondrial
  • Mitochondrial adenosine triphosphate (ATP) synthase produces the majority of ATP in eukaryotic cells, and its dimerization is necessary to create the inner membrane folds, or cristae, characteristic of mitochondria. (sciencemag.org)
  • mammalian
  • Type I systems utilise a single large, multifunctional polypeptide and are common to both mammals and fungi (although the structural arrangement of fungal and mammalian synthases differ). (wikipedia.org)
  • dehydratase
  • Porphobilinogen synthase (or ALA dehydratase, or aminolevulinate dehydratase) synthesizes porphobilinogen through the asymmetric condensation of two molecules of aminolevulinic acid. (wikipedia.org)
  • Hereditary insufficiency of porphobilinogen synthase is called porphobilinogen synthase (or ALA dehydratase) deficiency poprhyria. (wikipedia.org)
  • condensation
  • Since the condensation of tryptamine and secologanin is the first committed step in alkaloid synthesis, strictosidine synthase plays a fundamental role for the great majority of the indole-alkaloid pathways. (wikipedia.org)
  • monomer
  • Studies have suggested that one metal ion bonds to each monomer of DAHP synthase. (wikipedia.org)
  • The enzyme from different species adopts different quaternary structures, from monomeric to 60 subunits Two 6,7-dimethyl-8-ribityllumazine (Lumazine synthase) molecules are hydrogen bound to each monomer as the two domains are topologically similar. (wikipedia.org)
  • inhibitor
  • The most potent riboflavin synthase inhibitor is 9-D-ribityl-1,3,7-trihydropurine-2,6,8-trione, with Ki value of 0.61 μM. (wikipedia.org)
  • No additional cofactors are needed for strictosidine synthase to achieve optimal activity, although early studies of the enzyme derived from Apocynaceae plants identified p-chloromercuribenzoate as a potent inhibitor. (wikipedia.org)
  • structural
  • According to structural studies of strictosidine synthase from Rauvolfia serpentina, tryptamine is located at the bottom of the pocket, where Glu 309 forms a hydrogen bond with the substrate's primary amine group. (wikipedia.org)
  • ions
  • Metal ions are required in order for DAHP synthase to catalyze reactions. (wikipedia.org)
  • In DAHP synthase, it has been shown that binding site contains patterns of cysteine and histidine residues bound to metal ions in a Cys-X-X-His fashion. (wikipedia.org)
  • Chelation of cadmium ions by phytochelatin synthase: role of the cysteine-rich C-terminal. (ebi.ac.uk)
  • amino acids
  • The linear tripeptide δ-(L-α-aminoadipoyl)-L-cysteinyl-D-valine (LLD-ACV) must first be assembled from its component amino acids by N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase (ACV synthase). (wikipedia.org)