bifunctional enzyme造句

• This gene encodes a bifunctional enzyme that alpha-aminoadipic semialdehyde.
• This activity is often found in a bifunctional enzyme with xanthine oxidase ( ) activity too.
• It is classified under and in mammals is found as part of a bifunctional enzyme that also has formimidoyltetrahydrofolate cyclodeaminase activity.
• Though not closely related to eukaryotic GPIs, the bifunctional enzyme is similar enough that the isomerization for the interconversion of G6P to F6P.
• This gene encodes a bifunctional enzyme that is involved in the biosynthesis of sphingolipids in human skin and in other phytosphingolipid-containing tissues.
• In some archaea and bacteria glucose-6-phosphate isomerase activity occurs via a bifunctional enzyme that also exhibits phosphomannose isomerase ( PMI ) activity.
• This bifunctional enzyme has two main domains, an orotate phosphoribosyltransferase ( OPRTase, ) subunit and an orotidine-5-phosphate decarboxylase ( ODCase, ) subunit.
• Some plants, mainly monocotyledonous, use tyrosine to synthesize p-coumaric acid by the action of the bifunctional enzyme Phenylalanine / tyrosine ammonia-lyase ( PTAL ).
• Thymidylate synthase is an enzyme of about 30 to 35 kDa in most species except in protozoan and plants where it exists as a bifunctional enzyme that includes a dihydrofolate reductase domain.
• The bacterial FAD synthetase that is part of the bifunctional enzyme has remote similarity to nucleotidyl transferases and, hence, it may be involved in the adenylylation reaction of FAD synthetases.
• As glucose and insulin levels rise, as during digestion of a meal, GK is released from GKRP and moves back to the cytoplasm, where much of it associates with the bifunctional enzyme.
• Together with Carbon monoxide dehydrogenase ( CODH ), it forms the bifunctional enzyme Acetyl-CoA Synthase / Carbon Monoxide Dehydrogenase ( ACS / CODH ) found in anaerobic organisms such as archaea and eubacteria.
• The overall structure is similar to the C-terminal domain of the bifunctional enzyme HpcE from Escherichia coli C, fumarylacetoacetate hydrolase from Mus musculus and to YcgM ( Apc5008 ) from E . coli 1262.
• In prokaryotes, this domain mostly occurs on its own, while in eukaryotes it is fused to a glutamate formiminotransferase domain ( which catalyses the previous step in the pathway ) to form the bifunctional enzyme formiminotransferase cyclodeaminase.
• While elongating, the HSGAG is dynamically modified, first by N-deacetylase, N-sulfotransferase ( NDST1 ), which is a bifunctional enzyme that cleaves the N-acetyl group from GlcNAc and subsequently sulfates the N-position.
• The purD genes often contain PurD RNA motif in their 5'UTR . In yeast, GARS is part of a bifunctional enzyme ( encoded by the ADE5 / 7 gene ) in conjunction with phosphoribosylformylglycinamidine cyclo-ligase ( AIRS ).
• The bifunctional enzyme prepilin peptidase ( PilD ) from " Pseudomonas aeruginosa " is a key determinant in both type-IV pilus biogenesis and extracellular protein secretion, in its roles as a leader peptidase and methyl transferase ( MTase ).
• Sirohydrochlorin ferrochelatase is a class II chelatase i . e . it does not require ATP for its activity unlike class I chelatases such as " Saccharomyces cerevisiae " the last two steps are carried out by a bifunctional enzyme called Met8p.
• As might be expected, the bifunctional enzymes from lower plants are larger ( 946 960 residues, 106 107 kDa ) than the monofunctional enzymes from higher plants ( 800 867 residues, 90 98 kDa ), although not by twice as much.
• In mammals, this enzyme can be found as part of a bifunctional enzyme in a single polypeptide with glutamate formimidoyltransferase ( EC 2.1 . 2.5 ), the enzyme activity that catalyses the previous step in the histidine catabolic pathway.