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  • reaction
  • In biochemistry, a lyase is an enzyme that catalyzes the breaking (an "elimination" reaction) of various chemical bonds by means other than hydrolysis (a "substitution" reaction) and oxidation, often forming a new double bond or a new ring structure. (wikipedia.org)
  • A combination of both an elimination and a Michael addition is seen in O-succinylhomoserine (thiol)-lyase (MetY or MetZ) which catalyses first the γ-elimination of O-succinylhomoserine (with succinate as a leaving group) and then the addition of sulfide to the vinyl intermediate, this reaction was first classified as a lyase (EC 4.2.99.9), but was then reclassified as a transferase (EC 2.5.1.48). (wikipedia.org)
  • Adenylosuccinate lyase deficiency, also called adenylosuccinase deficiency, is a rare autosomal recessive metabolic disorder characterized by the appearance of succinylaminoimidazolecarboxamide riboside (SAICA riboside) and succinyladenosine (S-Ado) in cerebrospinal fluid, urine.These two succinylpurines are the dephosphorylated derivatives of SAICA ribotide (SAICAR) and adenylosuccinate (S-AMP), the two substrates of adenylosuccinate lyase (ADSL), which catalyzes an important reaction in the de novo pathway of purine biosynthesis. (wikipedia.org)
  • His68 and His141 seem to serve as the general acid and base catalysts, and are critical to the catalyzing reaction of the substrate. (wikipedia.org)
  • mechanism
  • The precise molecular mechanism by which selenols, generated by β-lyase, provide protection against cisplatin-induced cytotoxicity, however, remains to be established. (aspetjournals.org)
  • Structure and mechanism of PhnP, a phosphodiesterase of the carbon-phosphorus lyase pathway. (nih.gov)
  • As shown in the mechanism below, cystathionine beta-lyase facilitates the S-C bond cleavage in cystathionine with the use of a PLP cofactor bounded to a catalytic lysine residue. (wikipedia.org)
  • Class I AP endonucleases (EC 4.2.99.18) cleave 3' to AP sites by a β-lyase mechanism, leaving an unsaturated aldehyde, termed a 3'-(4-hydroxy-5-phospho-2-pentenal) residue, and a 5'-phosphate. (wikipedia.org)
  • amino
  • Crystal structures of Citrobacter freundii methionine γ-lyase complexes with the substrates of γ- (L-1-amino-3-methylthiopropylphosphinic acid) and β- (S-ethyl-L-cysteine) elimination reactions and the competitive inhibitor L-norleucine have been determined at 1.45, 1.8, and 1.63 Å resolution, respectively. (sigmaaldrich.com)
  • Plant and bacterial cystathionine beta-lyases are inhibited by the antimicrobial amino acid, L-aminoethoxybinylglycine (AVG), and the antibacterial amino acid, rhizobitoxine. (wikipedia.org)
  • The enzyme is required for ketogenesis in the liver, and is also responsible for processing the amino acid leucine inside the mitochondrion Mutations in the HMGCL gene cause 3-hydroxy-3-methylglutaryl-CoA lyase deficiency (HMGCLD), a rare autosomal recessive inborn error of metabolism characterized by disruption of ketogenesis and L-leucine catabolism. (wikipedia.org)
  • Cysteine
  • Selenocysteine Se -conjugates have previously been proposed as kidney-selective prodrugs of pharmacologically active selenols because of their active uptake and bioactivation by cysteine conjugate β-lyases in the kidney. (aspetjournals.org)
  • To elucidate whether chemoprotection is β-lyase-dependent wild-type LLC-PK 1 cells, possessing a very low β-lyase activity, and LLC-PK 1 cells stably transfected with full-length cDNA coding for rat kidney cysteine conjugate β-lyase/glutamine transaminase K (R1J) were used. (aspetjournals.org)
  • The protective activity against cisplatin-induced cytotoxicity and ROS generation was blocked by aminooxyacetic acid, a selective inhibitor of pyridoxal 5′-phosphate-dependent cysteine conjugate β-lyases, further supporting the role of β-lyase in the observed chemoprotection. (aspetjournals.org)
  • structurally
  • The cystathionine beta-lyase monomer consists of three functionally and structurally distinct domains: Composed of three α-helices and one beta-strand that contribute to the formation of the quaternary structure. (wikipedia.org)
  • methionine
  • Three-dimensional structures of noncovalent complexes of Citrobacter freundii methionine γ-lyase with substrates. (sigmaaldrich.com)
  • Other members include cystathionine gamma-synthase, cystathionine gamma-lyase, and methionine gamma lyase. (wikipedia.org)
  • Treatment of adenylosuccinate lyase deficiency can be done via epilepsy management with anticonvulsive drugs.Additionally the following options include: D-ribose and uridine administration Ketogenic diet S-adenosyl-l-methionine The prognosis of this condition in childhood usually has a stable outcome, whereas in neonatal is almost always fatal, according to Jurecka, et al. (wikipedia.org)
  • bacterial
  • Herein, we demonstrate that a bacterial PAL from Anabaena variabilis (AvPAL) displays significantly higher activity towards a series of non-natural substrates than previously described eukaryotic PALs. (manchester.ac.uk)
  • Utilization of glyphosate as phosphate source: biochemistry and genetics of bacterial carbon-phosphorus lyase. (nih.gov)
  • Hevea
  • Commonly studied (S)-selective hydroxynitrile lyases include MeHNL from Manihot esculenta and HbHNL from Hevea brasiliensis. (wikipedia.org)
  • structures
  • The binary complex of the truncated enzyme with cyanocobalamin and the ternary complex with cyanocobalamin or adeninylpentylcobalamin and substrates were crystallized, and their x-ray structures were analyzed. (pubmedcentralcanada.ca)
  • cleavage
  • This subclass contains the decarboxylases ( EC 4.1.1 ), the aldehyde-lyases catalysing the reversal of an aldol condensation ( EC 4.1.2 ), and the oxo-acid-lyases, catalysing the cleavage of a 3-hydroxy acid ( EC 4.1.3 ), or the reverse reactions. (qmul.ac.uk)
  • Molecule
  • When acting on the single substrate, a molecule is eliminated and this generates either a new double bond or a new ring. (qmul.ac.uk)
  • deficiency
  • In addition, the lysine 48 residue which is mutated in patients with 3-hydroxy-3-methylglutaryl-CoA lyase deficiency is also found to be necessary for substrate binding. (wikipedia.org)
  • Among the signs and symptoms of adenylosuccinate lyase deficiency are the following: Aggressive behavior Microcephaly Autism Brachycephaly Mild Cerebellar hypoplasia Seizures Adenylosuccinate lyase deficiency is responsible for a range of symptoms that involve psychomotor retardation, often accompanied by epileptic seizures, and autistic features. (wikipedia.org)
  • molecular
  • To rationalize the observed structure-affinity relationships of aliginate lyase alyVI with its (GGG) substrate, molecular docking, MD imulations and binding free energy calculations followed by site-directed mutagenesis and alyVI activity assays were carried out. (sigmaaldrich.com)
  • hydro-lyase
  • The systematic name of this enzyme class is (R,R)-tartrate hydro-lyase (oxaloacetate-forming). (wikipedia.org)
  • Other names in common use include tartrate dehydratase, tartaric acid dehydrase, L-tartrate dehydratase, L-(+)-tartaric acid dehydratase, and (R,R)-tartrate hydro-lyase. (wikipedia.org)
  • The systematic name of this enzyme class is (6R)-6-(L-erythro-1,2-dihydroxypropyl)-5,6,7,8-tetrahydro-4a-hydroxy pterin hydro-lyase [(6R)-6-(L-erythro-1,2-dihydroxypropyl)-7,8-dihydro-6H-pterin-formin g]. (wikipedia.org)
  • Other names in common use include 4alpha-hydroxy-tetrahydropterin dehydratase, pterin-4alpha-carbinolamine dehydratase, and 4a-hydroxytetrahydrobiopterin hydro-lyase. (wikipedia.org)
  • The systematic name of this enzyme class is 16alpha-hydroxyprogesterone hydro-lyase (16,17-didehydroprogesterone-forming). (wikipedia.org)
  • Other names in common use include hydroxyprogesterone dehydroxylase, 16alpha-hydroxyprogesterone dehydroxylase, 16alpha-dehydroxylase, and 16alpha-hydroxyprogesterone hydro-lyase. (wikipedia.org)
  • decarboxylase
  • In enzymology, an oxalyl-CoA decarboxylase (OXC) (EC 4.1.1.8) is an enzyme primarily produced by the gastrointestinal bacterium Oxalobacter formigenes that catalyzes the chemical reaction oxalyl-CoA ⇌ {\displaystyle \rightleftharpoons } formyl-CoA + CO2 OXC belongs to the family of lyases, specifically the carboxy-lyases (decarboxylases), which cleave carbon-carbon bonds. (wikipedia.org)
  • No FAD binding is observed in oxalyl-CoA decarboxylase, but an excess of coenzyme A in the crystal structure has led to the hypothesis that the binding site was co-opted during OXC evolution to bind the CoA moiety of its substrate. (wikipedia.org)
  • Malonyl-CoA decarboxylase (which can also be called MCD and malonyl-CoA carboxyl-lyase) is found from bacteria to humans, has important roles in regulating fatty acid metabolism and food intake, and it is an attractive target for drug discovery. (wikipedia.org)
  • transfer
  • tRNA-intron lyase (EC 4.6.1.16, tRNA intron endonuclease, transfer ribonucleate intron endoribonuclease, tRNA splicing endonuclease, splicing endonuclease, tRNATRPintron endonuclease, transfer splicing endonuclease) is an enzyme. (wikipedia.org)