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  • enzymology
  • In enzymology, a holo-[acyl-carrier-protein] synthase (EC 2.7.8.7) is an enzyme that catalyzes the chemical reaction: CoA-[4'-phosphopantetheine] + apo-acyl carrier protein ⇌ {\displaystyle \rightleftharpoons } adenosine 3',5'-bisphosphate + holo-acyl carrier protein This enzyme belongs to the family of transferases, specifically those transferring non-standard substituted phosphate groups. (wikipedia.org)
  • In enzymology, an aerobactin synthase (EC 6.3.2.39) is an enzyme that catalyzes the chemical reaction 4 ATP + citrate + 2 N6-acetyl-N6-hydroxy-L-lysine + 2 H2O ⇌ {\displaystyle \rightleftharpoons } 4 ADP + 4 phosphate + aerobactin The 4 substrates of this enzyme are ATP, citrate, N6-acetyl-N6-hydroxy-L-lysine, and H2O, whereas its 3 products are ADP, phosphate, and aerobactin. (wikipedia.org)
  • enzyme
  • Both this enzyme and EC 6.3.2.29 , cyanophycin synthase (L-aspartate-adding), are required for the elongation of cyanophycin, which is a protein-like cell inclusion that is unique to cyanobacteria and acts as a temporary nitrogen store . (genome.jp)
  • This reaction is catalyzed by a prenyltransferase enzyme (Prenyltransferase 4-dimethylallyltryptophan synthase) named FgaPT2 in A. fumigatus. (wikipedia.org)
  • This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-amino-acid ligases (peptide synthases). (wikipedia.org)
  • Carnosine synthase (EC 6.3.2.11) is an enzyme that catalyzes the chemical reaction ATP + L-histidine + beta-alanine ⇌ {\displaystyle \rightleftharpoons } ADP + phosphate + carnosine The 3 substrates of this enzyme are ATP, L-histidine, and beta-alanine, whereas its 3 products are ADP (previously thought to form AMP), diphosphate, and carnosine. (wikipedia.org)
  • production
  • The production of ATP is subsequently inhibited, as protons are unable to flow through the ATP synthase complex in the absence of a proton gradient. (wikipedia.org)
  • structure
  • Polyketide synthases can be categorized into three different types (I, II and III), which have the same enzymatic functions, but difference in quaternary structure and chain initiation and termination. (mdpi.com)
  • Amino Acids
  • Enzymes involved in this biosynthesis include: Acetolactate synthase (also known as acetohydroxy acid synthase) Acetohydroxy acid isomeroreductase Dihydroxyacid dehydratase Valine aminotransferase Like other branched-chain amino acids, the catabolism of valine starts with the removal of the amino group by transamination, giving alpha-ketoisovalerate, an alpha-keto acid, which is converted to isobutyryl-CoA through oxidative decarboxylation by the branched-chain α-ketoacid dehydrogenase complex. (wikipedia.org)
  • Nonribosomal peptides and polyketides are synthesized from amino acids and short carboxylic acids by NRPSs and PKSs, respectively. (wikipedia.org)
  • diphthine
  • Dph6 is therefore a candidate for the elusive amidase, while Dph7 apparently couples diphthine synthase (Dph5) to diphthine amidation. (nih.gov)
  • E) diphthine-modified peptide in the dph6Δ strain with loss of the trimethylamino group before analysis in the mass spectrometer indicated by the parent ion m/z. (nih.gov)
  • In enzymology, a diphthine-ammonia ligase (EC 6.3.1.14, diphthamide synthase, diphthamide synthetase) is an enzyme that catalyzes the chemical reaction ATP + diphthine + NH3 ⇌ {\displaystyle \rightleftharpoons } ADP + phosphate + diphthamide The 3 substrates of this enzyme are ATP, diphthine, and NH3, whereas its 3 products are ADP, phosphate, and diphthamide. (wikipedia.org)
  • cytochromes
  • Hemes are most commonly recognized as components of hemoglobin, the red pigment in blood, but are also found in a number of other biologically important hemoproteins such as myoglobin, cytochromes, catalases, heme peroxidase, and endothelial nitric oxide synthase. (wikipedia.org)
  • Type
  • Unmodified peptide was also found in eEF2 prepared from dph5, dph6 and dph7 deletion strains as well as from wild-type cells (Figures S1 and S2). (nih.gov)