Benzamidines
Lyases
Heterocyclic Compounds
Chondroitin Lyases
Enzymes which catalyze the elimination of delta-4,5-D-glucuronate residues from polysaccharides containing 1,4-beta-hexosaminyl and 1,3-beta-D-glucuronosyl or 1,3-alpha-L-iduronosyl linkages thereby bringing about depolymerization. EC 4.2.2.4 acts on chondroitin sulfate A and C as well as on dermatan sulfate and slowly on hyaluronate. EC 4.2.2.5 acts on chondroitin sulfate A and C.
Furans
Structure-Activity Relationship
Molecular Structure
Pectobacterium chrysanthemi
Crystallography, X-Ray
Chondroitinases and Chondroitin Lyases
Models, Molecular
Pectins
High molecular weight polysaccharides present in the cell walls of all plants. Pectins cement cell walls together. They are used as emulsifiers and stabilizers in the food industry. They have been tried for a variety of therapeutic uses including as antidiarrheals, where they are now generally considered ineffective, and in the treatment of hypercholesterolemia.
Chicory
Aldehyde-Lyases
DNA
A deoxyribonucleotide polymer that is the primary genetic material of all cells. Eukaryotic and prokaryotic organisms normally contain DNA in a double-stranded state, yet several important biological processes transiently involve single-stranded regions. DNA, which consists of a polysugar-phosphate backbone possessing projections of purines (adenine and guanine) and pyrimidines (thymine and cytosine), forms a double helix that is held together by hydrogen bonds between these purines and pyrimidines (adenine to thymine and guanine to cytosine).
Carbon-Oxygen Lyases
Erwinia
Heparin Lyase
An enzyme of the isomerase class that catalyzes the eliminative cleavage of polysaccharides containing 1,4-linked D-glucuronate or L-iduronate residues and 1,4-alpha-linked 2-sulfoamino-2-deoxy-6-sulfo-D-glucose residues to give oligosaccharides with terminal 4-deoxy-alpha-D-gluc-4-enuronosyl groups at their non-reducing ends. (From Enzyme Nomenclature, 1992) EC 4.2.2.7.
Oxo-Acid-Lyases
Polygalacturonase
Alginates
Hexuronic Acids
Isocitrate Lyase
Rhodophyta
Plants of the division Rhodophyta, commonly known as red algae, in which the red pigment (PHYCOERYTHRIN) predominates. However, if this pigment is destroyed, the algae can appear purple, brown, green, or yellow. Two important substances found in the cell walls of red algae are AGAR and CARRAGEENAN. Some rhodophyta are notable SEAWEED (macroalgae).
Substrate Specificity
Phycobilins
Chondroitin ABC Lyase
Sphingomonas
Molecular Sequence Data
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
Amino Acid Sequence
Cytochromes c1
Bacteroides
Flavobacterium
Adenylosuccinate Lyase
Streptococcus anginosus
Glucuronic Acid
Hevea
Cloning, Molecular
Glycosaminoglycans
Proteus vulgaris
Sequence Homology, Amino Acid
Uronic Acids
Chondroitin Sulfates
Derivatives of chondroitin which have a sulfate moiety esterified to the galactosamine moiety of chondroitin. Chondroitin sulfate A, or chondroitin 4-sulfate, and chondroitin sulfate C, or chondroitin 6-sulfate, have the sulfate esterified in the 4- and 6-positions, respectively. Chondroitin sulfate B (beta heparin; DERMATAN SULFATE) is a misnomer and this compound is not a true chondroitin sulfate.
Sulfonium Compounds
Dermatan Sulfate
Carbohydrate Sequence
Carbon-Nitrogen Lyases
Carbon-Carbon Lyases
DNA-(Apurinic or Apyrimidinic Site) Lyase
A DNA repair enzyme that catalyses the excision of ribose residues at apurinic and apyrimidinic DNA sites that can result from the action of DNA GLYCOSYLASES. The enzyme catalyzes a beta-elimination reaction in which the C-O-P bond 3' to the apurinic or apyrimidinic site in DNA is broken, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate. This enzyme was previously listed under EC 3.1.25.2.
Pseudomonas
N-Glycosyl Hydrolases
Sequence Alignment
The arrangement of two or more amino acid or base sequences from an organism or organisms in such a way as to align areas of the sequences sharing common properties. The degree of relatedness or homology between the sequences is predicted computationally or statistically based on weights assigned to the elements aligned between the sequences. This in turn can serve as a potential indicator of the genetic relatedness between the organisms.
Hydrogen-Ion Concentration
Kinetic and inhibition studies on substrate channelling in the bifunctional enzyme catalysing C-terminal amidation. (1/31)
A series of experiments has been conducted to investigate the possibility that substrate channelling might occur in the bifunctional forms of enzymes carrying out C-terminal amidation, a post-translational modification essential to the biological activity of many neuropeptides. C-terminal amidation entails sequential action by peptidylglycine mono-oxygenase (PAM, EC 1.14.17.3) and peptidylamidoglycolate lyase (PGL, EC 4.3.2.5), with the mono-oxygenase catalysing conversion of a glycine-extended pro-peptide into the corresponding alpha-hydroxyglycine derivative, which is then converted by the lyase into amidated peptide plus glyoxylate. Since the mono-oxygenase and lyase reactions exhibit tandem reaction stereospecificities, channelling of the alpha-hydroxy intermediate might occur, as is the case for some other multifunctional enzymes. Selective inhibition of the mono-oxygenase domain by competitive ester inhibitors, as well as mechanism-based mono-oxygenase inactivation by the novel olefinic inhibitor 5-acetamido-4-oxo-6-phenylhex-2-enoate (N-acetylphenylalanyl acrylate), has little to no effect on the kinetic parameters of the lyase domain of the AE from Xenopus laevis. Similarly, inhibition of the lyase domain by the potent dioxo inhibitor 2,4-dioxo-5-acetamido-6-phenylhexanoate has little effect on the activity of the monooxygenase domain in the bifunctional enzyme. A series of experiments on intermediate accumulation and conversion were also carried out, along with kinetic investigations of the reactivities of the monofunctional and bifunctional forms of PAM and PGL towards substrates and inhibitors. Taken together, the results demonstrate the kinetic independence of the mono-oxygenase and lyase domains, and provide no evidence for substrate channelling between these domains in the bifunctional amidating enzyme. (+info)Kinetic and stereochemical studies on novel inactivators of C-terminal amidation. (2/31)
C-terminal amidation, a required post-translational modification for the bioactivation of many neuropeptides, entails sequential enzymic action by peptidylglycine alpha-mono-oxygenase (PAM, EC 1.14.17.3) and peptidylamidoglycolate lyase (PGL, EC 4.3.2.5). Here we introduce novel compounds in which an olefinic functionality is incorporated into peptide analogues as the most potent turnover-dependent inactivators of PAM. Kinetic parameters for PAM inactivation by 4-oxo-5-acetamido-6-phenyl-hex-2-enoic acid and 4-oxo-5-acetamido-6-(2-thienyl)-hex-2-enoic acid were obtained by using both the conventional dilution assay method and the more complex progress curve method. The results obtained from the progress curve method establish that these compounds exhibit the kinetic characteristics of pure competitive inactivators (i.e. no ESI complex forms during inactivation). On the basis of k(inact)/K(i) values, 4-oxo-5-acetamido-6-(2-thienyl)-hex-2-enoic acid is almost two orders of magnitude more potent than benzoylacrylate, a chemically analogous olefinic inactivator that lacks the peptide moiety. Stereochemical studies established that PAM inactivation by 4-oxo-5-acetamido-6-(2-thienyl)-hex-2-enoic acid is stereospecific with respect to the moiety at the P(2) position, which is consistent with previous results with substrates and reversible inhibitors. In contrast, 2, 4-dioxo-5-acetamido-6-phenylhexanoic acid, which is a competitive inhibitor with respect to ascorbate, exhibits a low degree of stereospecificity in binding to the ascorbate sites of both PAM and dopamine-beta-hydroxylase. (+info)Urea is a product of ureidoglycolate degradation in chickpea. Purification and characterization of the ureidoglycolate urea-lyase. (3/31)
A ureidoglycolate-degrading activity was analyzed in different organs of chickpea (Cicer arietinum). Activity was detected in all the tissues analyzed, but highest levels of specific activity were found in pods, from which it has been purified and characterized. This is the first ureidoglycolate-degrading activity that has been purified to homogeneity from any photosynthetic organism. Only one ureidoglycolate-degrading activity was found during the purification. The enzyme was purified 1,500-fold, and specific activity for the pure enzyme was 8.6 units mg(-1), which corresponds with a turnover number of 1,600 min(-1). The native enzyme has a molecular mass of 180 kD and consists of six identical or similar-sized subunits of 31 kD each. The enzyme exhibited hyperbolic, Michaelian kinetics for (-) ureidoglycolate with K(m) values of 6 and 10 microM in the presence or absence of Mn(2+), respectively. Optimum pH was between 7 and 8 and maximum activity was found at temperatures above 70 degrees C, the enzyme being extremely stable and resistant to heat denaturation. The activity was inhibited by EDTA and enhanced by several bivalent cations, thus suggesting that the enzyme is a metalloprotein. This enzyme has been characterized as a ureidoglycolate urea-lyase (EC 4.3.2.3), which catalyzes the degradation of (-) ureidoglycolate to glyoxylate and urea. This is the first time that such an activity is detected in plant tissues. A possible function for this activity and its implications in the context of nitrogen mobilization in legume plants is also discussed. (+info)Pathways for urea production during early life of an air-breathing teleost, the African catfish Clarias gariepinus Burchell. (4/31)
Embryos and larvae of the African catfish Clarias gariepinus excrete significant quantities of urea. The present study focused on the potential urea-generating pathways during early development of this teleost; uricolysis, argininolysis and the ornithine-urea cycle (OUC). Uricase, allantoinase, allantoicase and ureidoglycollate lyase of the uricolytic pathway were expressed in all early life stages and in adult liver of C. gariepinus. Uricase activity increased in starved larvae compared with yolk-sac larvae. The key regulatory enzyme of the teleost OUC, carbamoyl phosphate synthetase III (CPSase III), was expressed predominantly in muscle of developing C. gariepinus larvae and showed negligible activity in the absence of its allosteric effector N-acetyl-L-glutamate. CPSase III and ornithine carbamoyl transferase activities increased in fed larvae compared with starved larvae. In contrast to the early developmental stages, adult C. gariepinus expressed only low and variable levels of CPSase III, suggesting that, under the experimental conditions employed, OUC expression is influenced by developmental stage in this species. The data indicate that early C. gariepinus life stages express the enzymes necessary for urea production by uricolysis, argininolysis and the OUC, and this may explain why urea tissue levels and urea excretion rates are substantial during the early development of this air-breathing teleost. (+info)Catalysis, stereochemistry, and inhibition of ureidoglycolate lyase. (5/31)
Ureidoglycolate lyase (UGL, EC 4.3.2.3) catalyzes the breakdown of ureidoglycolate to glyoxylate and urea, which is the final step in the catabolic pathway leading from purines to urea. Although the sequence of enzymatic steps was worked out nearly 40 years ago, the stereochemistry of the uric acid degradation pathway and the catalytic properties of UGL have remained very poorly described. We now report the first direct investigation of the absolute stereochemistry of UGL catalysis. Using chiral chromatographic analyses with substrate enantiomers, we demonstrate that UGL catalysis is stereospecific for substrates with the (S)-hydroxyglycine configuration. The first potent competitive inhibitors for UGL are reported here. These inhibitors are compounds which contain a 2,4-dioxocarboxylate moiety, designed to mimic transient species produced during lyase catalysis. The most potent inhibitor, 2,4-dioxo-4-phenylbutanoic acid, exhibits a KI value of 2.2 nM and is therefore among the most potent competitive inhibitors ever reported for a lyase enzyme. New synthetic alternate substrates for UGL, which are acyl-alpha-hydroxyglycine compounds, are described. Based on these alternate substrates, we introduce the first assay method for monitoring UGL activity directly. Finally, we report the first putative primary nucleotide and derived peptide sequence for UGL. This sequence exhibits a high level of similarity to the fumarylacetoacetate hydrolase family of proteins. Close mechanistic similarities can be visualized between the chemistries of ureidoglycolate lyase and fumarylacetoacetate hydrolase catalysis. (+info)Differentially regulated malate synthase genes participate in carbon and nitrogen metabolism of S. cerevisiae. (6/31)
We have isolated a second gene (MLS1), which in addition to DAL7, encodes malate synthase from S. cerevisiae. Expression of the two genes is specific for their physiological roles in carbon and nitrogen metabolism. Expression of MLS1, which participates in the utilization of non-fermentable carbon sources, is sensitive to carbon catabolite repression, but nearly insensitive to nitrogen catabolite repression. DAL7, which participates in catabolism of the nitrogenous compound allantoin, is insensitive to carbon catabolite repression, but highly sensitive to nitrogen catabolite repression. Results obtained with null mutations in these genes suggest that S. cerevisiae contains at least one and perhaps two additional malate synthase genes. (+info)The source of the oxygen atom in the alpha-hydroxyglycine intermediate of the peptidylglycine alpha-amidating reaction. (7/31)
Peptidylglycine alpha-amidating activity catalyses the oxidation of a C-terminally glycine-extended peptide to a desglycine alpha-amidated peptide at the expense of ascorbate and O2 in the presence of Cu2+. The reaction involves oxidative N-dealkylation within the terminal glycine residue, with retention of the glycine N atom and release of the remainder as glyoxylate. Recent studies by us and others have revealed that the reaction consists of two steps via a carbinolamide as an intermediate (peptidyl alpha-hydroxyglycine), and also that two separate enzymes derived from a common precursor protein catalyse these steps, formation of the carbinolamide and its conversion into alpha-amide and glyoxylate. As for the mechanism of carbinolamide formation, two distinct pathways can be considered: direct mono-oxygenation at the glycine alpha-C atom and dehydrogenation leading to an imine followed by hydration. To draw a distinction between them, we carried out the reaction with D-Tyr-Val-Gly as the substrate either in the H2(18)O-enriched medium or under an atmosphere of 18O2, and isolated the alpha-hydroxylglycine intermediate. The fast-atom-bombardment mass-spectral analysis demonstrated that the hydroxy O atom comes from O2, but not from H2O, indicating that the alpha-hydroxylation should be a monooxygenase reaction. (+info)Intermittent hypoxia activates peptidylglycine alpha-amidating monooxygenase in rat brain stem via reactive oxygen species-mediated proteolytic processing. (8/31)
(+info)
DAL3 - Ureidoglycolate lyase - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Bakers yeast) - DAL3 gene & protein
allA - Ureidoglycolate lyase - Shigella flexneri - allA gene & protein
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peptidylglycine monooxygenase
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Purine imidazole-ring cyclase
This enzyme belongs to the family of lyases, specifically amidine lyases. The systematic name of this enzyme class is DNA-4,6- ... 9-N-lyase (cyclizing), DNA-4,6-diamino-5-formamidopyrimidine 8-C,9-N-lyase (cyclizing, and DNA-adenine-forming). Chetsanga CJ, ... diamino-5-formamidopyrimidine C8-N9-lyase (cyclizing DNA-adenine-forming). Other names in common use include DNA-4,6-diamino-5- ...
Proteaasid - Vikipeedia, vaba entsüklopeedia
Amidine-lyases Kasutatud 23.10.2016 (inglise) *↑ 11,0 11,1 Craik, C. S. et al., (2011). Proteases as therapeutics. Biochem J., ... 2,00 2,01 2,02 2,03 2,04 2,05 2,06 2,07 2,08 2,09 2,10 2,11 Rawlings, N. D., et al., (2011) Asparagine Peptide Lyases: A ...
List of MeSH codes (D08)
... tyrosine phenol-lyase MeSH D08.811.520.232.300 - amidine-lyases MeSH D08.811.520.232.300.200 - adenylosuccinate lyase MeSH ... chondroitin lyases MeSH D08.811.520.241.700.350.500.500 - chondroitin abc lyase MeSH D08.811.520.241.700.512 - heparin lyase ... ammonia-lyases MeSH D08.811.520.232.400.200 - aspartate ammonia-lyase MeSH D08.811.520.232.400.350 - ethanolamine ammonia-lyase ... lyase MeSH D08.811.520.241.300 - hydro-lyases MeSH D08.811.520.241.300.050 - aconitate hydratase MeSH D08.811.520.241.300.050. ...
Peptidylamidoglycolate lyase
This enzyme belongs to the family of lyases, specifically amidine lyases. The systematic name of this enzyme class is ... peptidyl-alpha-hydroxyglycine alpha-amidating lyase, HGAD, PGL, PAL, and peptidylamidoglycolate peptidylamide-lyase. Katopodis ... In enzymology, a peptidylamidoglycolate lyase (EC 4.3.2.5) is an enzyme that catalyzes the chemical reaction ... peptidylamidoglycolate peptidyl-amide-lyase (glyoxylate-forming). Other names in common use include alpha-hydroxyglycine ...
Ureidoglycolate lyase
This enzyme belongs to the family of lyases, specifically amidine lyases. The systematic name of this enzyme class is (S)- ... In enzymology, an ureidoglycolate lyase (EC 4.3.2.3) is an enzyme that catalyzes the chemical reaction (S)-ureidoglycolate ⇌ {\ ... ureidoglycolate urea-lyase. This enzyme participates in purine metabolism. Trijbels F, Vogels GD (1967). "Allantoate and ... ureidoglycolate urea-lyase (glyoxylate-forming). Other names in common use include ureidoglycolatase, ureidoglycolase, ...
List of enzymes
EC 4.3.1 Phenylalanine ammonia-lyase (EC 4.3.1.24) Category:EC 4.4.1 Cystathionine gamma-lyase Cystathionine beta-lyase ... In linear amidines) Arginase (EC 3.5.3.1) Category:EC 3.5.4 (In cyclic amidines) Adenosine deaminase (EC 3.5.4.4) GTP ... lyase) ligase EC 6.2.1.23: Dicarboxylate-CoA ligase EC 6.2.1.24: Phytanate-CoA ligase EC 6.2.1.25: Benzoate-CoA ligase EC 6.2. ...
GTP cyclohydrolase II
... specifically in cyclic amidines. The systematic name of this enzyme class is GTP 7,8-8,9-dihydrolase (diphosphate-forming). ...
Succinyl-diaminopimelate desuccinylase
3.5.4: Cyclic amidines/. Aminohydrolases. *Guanine deaminase. *Adenosine deaminase. *AMP deaminase. *Inosine monophosphate ... EC4 Lyases (list). *EC5 Isomerases (list). *EC6 Ligases (list). *EC7 Translocases (list) ...
Phosphoribosylaminoimidazolecarboxamide formyltransferase
EC4 Lyases (list). *EC5 Isomerases (list). *EC6 Ligases (list). *EC7 Translocases (list) ...
DNA methyltransferase
m6A and m4C methyltransferases are found primarily in prokaryotes (although recent evidence has suggested that m6A is abundant in eukaryotes[1]). m5C methyltransfereases are found in some lower eukaryotes, in most higher plants, and in animals beginning with the echinoderms. The m6A methyltransferases (N-6 adenine-specific DNA methylase) (A-Mtase) are enzymes that specifically methylate the amino group at the C-6 position of adenines in DNA. They are found in the three existing types of bacterial restriction-modification systems (in type I system the A-Mtase is the product of the hsdM gene, and in type III it is the product of the mod gene). These enzymes are responsible for the methylation of specific DNA sequences in order to prevent the host from digesting its own genome via its restriction enzymes. These methylases have the same sequence specificity as their corresponding restriction enzymes. These enzymes contain a conserved motif Asp/Asn-Pro-Pro-Tyr/Phe in their N-terminal section, this ...
Thiopurine methyltransferase
EC4 Lyases (list). *EC5 Isomerases (list). *EC6 Ligases (list). *EC7 Translocases (list) ...
List of enzymes
Category:Lyases (EC 4) (Lyase)Edit. Category:EC 4.1 (carbon-carbon lyases)Edit. *Category:EC 4.1.1 *Ornithine decarboxylase (EC ... Category:EC 3.5.4 (In cyclic amidines) *Adenosine deaminase (EC 3.5.4.4) ... 4 Category:Lyases (EC 4) (Lyase) *4.1 Category:EC 4.1 (carbon-carbon lyases) ... Category:EC 4.3 (carbon-nitrogen lyases)Edit. *Category:EC 4.3.1 *Phenylalanine ammonia-lyase (EC 4.3.1.24) ...
Contents EC 4
EC 4.3.2 Amidine-Lyases. EC 4.3.2.1 argininosuccinate lyase. EC 4.3.2.2 adenylosuccinate lyase EC 4.3.2.3 ureidoglycolate lyase ... EC 4.2.2.7 heparin lyase. EC 4.2.2.8 heparin-sulfate lyase. EC 4.2.2.9 pectate disaccharide-lyase. EC 4.2.2.10 pectin lyase. EC ... EC 4 Lyases. EC 4.1 Carbon-Carbon Lyases. EC 4.1.1 Carboxy-Lyases. EC 4.1.1.1 pyruvate decarboxylase. EC 4.1.1.2 oxalate ... EC 4.1.2.61 feruloyl-CoA hydratase/lyase EC 4.1.3 Oxo-Acid-Lyases. EC 4.1.3.1 isocitrate lyase. EC 4.1.3.2 now EC 2.3.3.9. EC ...
Proteaasid - Vikipeedia, vaba entsüklopeedia
Peptidylamidoglycolate lyase - Wikipedia
This enzyme belongs to the family of lyases, specifically amidine lyases. The systematic name of this enzyme class is ... peptidyl-alpha-hydroxyglycine alpha-amidating lyase, HGAD, PGL, PAL, and peptidylamidoglycolate peptidylamide-lyase. Katopodis ... In enzymology, a peptidylamidoglycolate lyase (EC 4.3.2.5) is an enzyme that catalyzes the chemical reaction ... peptidylamidoglycolate peptidyl-amide-lyase (glyoxylate-forming). Other names in common use include alpha-hydroxyglycine ...
Ureidoglycolate lyase - Wikipedia
This enzyme belongs to the family of lyases, specifically amidine lyases. The systematic name of this enzyme class is (S)- ... In enzymology, an ureidoglycolate lyase (EC 4.3.2.3) is an enzyme that catalyzes the chemical reaction (S)-ureidoglycolate ⇌ {\ ... ureidoglycolate urea-lyase. This enzyme participates in purine metabolism. Trijbels F, Vogels GD (1967). "Allantoate and ... ureidoglycolate urea-lyase (glyoxylate-forming). Other names in common use include ureidoglycolatase, ureidoglycolase, ...
YRC Public Data Repository - Protein Structure Prediction - Protein Overview
amidine-lyase activity. 3.84281419858187. bayes_pls_golite062009. argininosuccinate lyase activity. 3.58328346705456. bayes_pls ... ASL - argininosuccinate lyase. 0.0. [1..462]. [1..459]. ARLY_CANAX - Argininosuccinate lyase OS=Candida albicans GN=ARG4 PE=3 ... lyase activity. 2.31268471569846. bayes_pls_golite062009. carbon-nitrogen lyase activity. 2.2046475419807. bayes_pls_ ... ARLY_SACDO - Argininosuccinate lyase OS=Saccharomyces douglasii GN=ARG4 PE=3 SV=1. ARLY_SACPA - Argininosuccinate lyase OS= ...
CA2426774A1 - Method for generating a library of oligonucleotides comprising a controlled distribution of mutations
-...
102000009575 Amidine-Lyases Human genes 0 description 1 * 108010034488 Amidine-Lyases Proteins 0 description 1 ... 108090000489 Carboxy-Lyases Proteins 0 description 1 * 102000007132 Carboxyl and Carbamoyl Transferases Human genes 0 ... 108090000673 Ammonia-Lyases Proteins 0 description 1 * AVKUERGKIZMTKX-NJBDSQKTSA-N Ampicillin Chemical compound data:image/svg+ ... 108090000453 Intramolecular Lyases Proteins 0 description 1 * 108010084764 Intramolecular Oxidoreductases Proteins 0 ...
BRENDA - EC Explorer
The sub-subclasses of EC 4.3 are the ammonia-lyases (EC 4.3.1), lyases acting on amides, amidines, etc. (amidine-lyases; EC 4.3 ... 4.2 Carbon-oxygen lyases (2350 organisms) CH-CH(-NH-R)- → >C=CH- + NH2-R. Others, however, catalyse elimination of another ... 4.4 Carbon-sulfur lyases (596 organisms) EC subclass 4.5", WIDTH, 550, FGCOLOR, "#ffffff", TEXTSIZE, "10px", CAPTIONSIZE, "12px ... 4.5 Carbon-halide lyases (42 organisms) EC subclass 4.6", WIDTH, 550, FGCOLOR, "#ffffff", TEXTSIZE, "10px", CAPTIONSIZE, "12px ...
US Patent # 4,299,916. Preferential signal production on a surface in immunoassays - Patents.com
... lyases 4.3 Carbon-nitrogen lyases 4.3.1 Ammonia-lyases 4.3.2 Amidine-lyases 4.4 Carbon-sulfur lyases 4.5 Carbon-halide lyases ... Lyases 4.1 Carbon-carbon lyases 4.1.1 Carboxy-lyases 4.1.2 Aldehyde-lyases 4.1.3 Ketoacid-lyases 4.2 Carbon-oxygen lyases 4.2.1 ... Lyases 4.1 Carbon-carbon lyases 4.1.2 Aldehyde lyases 13. aldolyase 4.2.1 Hydro-lyases 1. carbonic anhydrase 5. Isomerase 5.4 ... bonds other than peptide bonds 3.5.1 In linear amides 3.5.2 In cyclic amides 3.5.3 In linear amidines 3.5.4 In cyclic amidines ...
Serine dehydratase - wikidoc
Serine dehydratase or L-serine ammonia lyase (SDH) is in the β-family of pyridoxal phosphate-dependent (PLP) enzymes. SDH is ... L-serine hydro-lyase. Enzyme structure. HoloEnzyme: The holoenzyme SDH contains 319 residues, 1 PLP cofactor molecule, and 131 ... The β enzymes are all lyases and catalyze reactions where Cα and Cβ participate. Overall, in the PLP-dependent enzymes, the PLP ...
DeCS
Argininosuccinate lyase (P04076) - Yeast Metabolome Database
Argininosuccinate | definition of argininosuccinate by Medical dictionary
M2 PHARMA-September 21, 2017-FDA Grants Orphan Drug Designation to PhaseRx for PRX-ASL for Treatment of Argininosuccinate Lyase ... Additional galU genes were found adjacent to the gene argH encoding argininosuccinate lyase in the sequenced genomes from ... M2 EQUITYBITES-September 21, 2017-PhaseRx wins US FDAs orphan drug designation for PRX-ASL for argininosuccinate lyase ... FDA Grants Orphan Drug Designation to PhaseRx for PRX-ASL for Treatment of Argininosuccinate Lyase Deficiency ...
EC 4.3
... 2 Lyases Acting on Amides, Amidines, etc.. EC 4.3.3 Amine-Lyases. EC 4.3.99 Other Carbon-Nitrogen Lyases. EC 4.3.1 ... EC 4.3.2 Lyases Acting on Amides, Amidines, etc.. Contents. EC 4.3.2.1 argininosuccinate lyase. EC 4.3.2.2 adenylosuccinate ... EC 4.3.1.16 threo-3-hydroxy-L-aspartate ammonia-lyase EC 4.3.1.17 L-serine ammonia-lyase. EC 4.3.1.18 D-serine ammonia-lyase. ... Other name(s): adenylosuccinase; succino AMP-lyase; N6-(1,2-dicarboxyethyl)AMP AMP-lyase; 6-N-(1,2-dicarboxyethyl)AMP AMP-lyase ...
E367 | definition of E367 by Medical dictionary
KEGG BRITE: Enzymes - Equus caballus (horse)
EC 4 Introduction
... lyases acting on amides, amidines, etc. (EC 4.3.2), the amine-lyases (EC 4.3.3), and other carbon-nitrogen lyases (EC 4.3.99). ... EC 4. Lyases. Lyases are enzymes cleaving C-C, C-O, C-N and other bonds by other means than by hydrolysis or oxidation. They ... EC 4.2 Carbon-Oxygen Lyases. These enzymes catalyse the breakage of a carbon-oxygen bond. In the case of hydro-lyases (EC 4.2.1 ... EC 4.1 Carbon-Carbon Lyases. This subclass contains the decarboxylases (EC 4.1.1), the aldehyde-lyases catalysing the reversal ...
ENZYME search by enzyme class
4. 3. 1.- Ammonia-lyases. 4. 3. 2.- Lyases acting on amides, amidines, etc. 4. 3. 3.- Amine-lyases. 4. 3.99.- Other carbon- ... 4. -. -.- Lyases. 4. 1. -.- Carbon-carbon lyases. 4. 1. 1.- Carboxy-lyases. 4. 1. 2.- Aldehyde-lyases. 4. 1. 3.- Oxo-acid- ... 4. 7. -.- Carbon-phosphorus lyases. 4. 7. 1.- Carbon-phosphorus lyases. 4.99. -.- Other lyases. 4.99. 1.- Other lyases. 5 ... 4. 4. -.- Carbon-sulfur lyases. 4. 4. 1.- Carbon-sulfur lyases. 4. 5. -.- Carbon-halide lyases. 4. 5. 1.- Carbon-halide lyases ...
Type 2 diabetes risk alleles in PAM impact insulin release from human pancreatic β-cells. - Radcliffe Department of Medicine
AMIDEAST - What does AMIDEAST stand for? The Free Dictionary
AMIDE - What does AMIDE stand for? The Free Dictionary
Amide anesthetic | Article about amide anesthetic by The Free Dictionary
Succinyl-diaminopimelate desuccinylase - Wikipedia
Synthesis of unprecedented steroidal spiro heterocycles as potential antiproliferative drugs, European Journal of Medicinal...
Novel steroidal inhibitors of human cytochrome P45017α, (l7α-hydroxylase-Cl7,20-lyase): potential agents for the treatment of ... Unprecedented spiro-annelated sugar isoureas, guanidines and amidines as new families of glycosidase inhibitors ... 17α-Hydroxylase/17,20 lyase inhibitor VN/124-1 inhibits growth of androgen-independent prostate cancer cells via induction of ... Steroselective synthesis of some steroidal oxazolines, as novel potential inhibitors of 17α-hydroxylase-C17,20-lyase ...
DeCS
Subclasses are the AMMONIA-LYASES, the AMIDINE-LYASES, the amine-lyases, and other carbon-nitrogen lyases. EC 4.3. ... Subclasses are the AMMONIA-LYASES, the AMIDINE-LYASES, the amine-lyases, and other carbon-nitrogen lyases. EC 4.3.. ... Carbon-Nitrogen Lyases - Preferred Concept UI. M0029321. Scope note. Enzymes that catalyze the cleavage of a carbon-nitrogen ...
Coexpression cluster:C896 - resource browser
Sphingosine kinase inhibitors: A patent review
Amidine based SphK inhibitors. Amidine-based SphK inhibitors are also structural analogues of sphingosine that prevent from the ... The only exit pathway of sphingolipid pathways is metabolism of S1P mediated by S1P lyase (3) (Fig. 1). These interconnected ... The amidine-based SphK inhibitors showed high selective activity to SphK1 with in vitro potency in the nanomolar range. ... Biological evaluation of amidine based SphK inhibitors reveals substantial differences in inhibitory quality of molecules ...
Plasma levels of sphingosine 1-phosphate are strongly correlated with haematocrit, but variably restored by red blood cell...
RBC S1P lyase activity was evident when the formation of hexadecenal, detected as its semicarbazone derivative, was measured ... Discovery, biological evaluation, and structure-activity relationship of amidine based sphingosine kinase inhibitors ... S1P lyase activity was determined by measuring the formation of hexadecenal detected as its semicarbazone derivative as ... S1P lyase and phosphatase activities were determined using Triton X-100-solubilized substrates and assay conditions determined ...
New Delhi metallo-beta-lactamase 1
Pfam:
Family: PCMT (PF01135)
Ammonia-lyase2
- Serine dehydratase or L -serine ammonia lyase (SDH) is in the β-family of pyridoxal phosphate-dependent (PLP) enzymes. (wikidoc.org)
- This enzyme is a member of the aromatic amino acid lyase family, other members of which are EC 4.3.1.23 (tyrosine ammonia-lyase), EC 4.3.1.24 (phenylalanine ammonia-lyase) and EC 4.3.1.25 (phenylalanine/tyrosine ammonia-lyase). (qmul.ac.uk)
Carbon-nitrogen3
- EC 4.3.2 ), the amine-lyases ( EC 4.3.3 ), and other carbon-nitrogen lyases ( EC 4.3.99 ). (qmul.ac.uk)
- Subclasses are the AMMONIA-LYASES, the AMIDINE-LYASES, the amine-lyases, and other carbon-nitrogen lyases. (bvsalud.org)
- This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amidines. (creative-enzymes.com)
Subclass contains1
- 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)
Enzymes4
- These enzymes catalyze the elimination of ammonia from amidines with the formation of a double bond. (bvsalud.org)
- These enzymes are carbamoyl phosphate synthetase 1 (CPS1), ornithine transcarbamylase (OTC), argininosuccinate synthetase (ASS), argininosuccinate lyase (ASL), arginase and N-acetylglutamate synthetase. (thefreedictionary.com)
- Lyases are enzymes cleaving C-C, C-O, C-N and other bonds by other means than by hydrolysis or oxidation. (qmul.ac.uk)
- CYP17A1 mutations are associated with steroid-17 alpha-hydroxylase deficiency, 17-alpha-hydroxylase/17,20-lyase deficiency, pseudohermaphroditism, and adrenal hyperplasia type V (AH-V). P450 enzymes catalyze reactions involved in drug metabolism and synthesis of cholesterol, steroids and other lipids. (healthmatics.info)
Systematic name2
- The systematic name of this enzyme class is peptidylamidoglycolate peptidyl-amide-lyase (glyoxylate-forming). (wikipedia.org)
- The systematic name of this enzyme class is DNA-4,6-diamino-5-formamidopyrimidine C8-N9-lyase (cyclizing DNA-adenine-forming). (wikipedia.org)
Catalyzes2
- In enzymology, a peptidylamidoglycolate lyase (EC 4.3.2.5) is an enzyme that catalyzes the chemical reaction peptidylamidoglycolate ⇌ {\displaystyle \rightleftharpoons } peptidyl amide + glyoxylate Hence, this enzyme has one substrate, peptidylamidoglycolate, and two products, peptidyl amide and glyoxylate. (wikipedia.org)
- Abiraterone acetate [17-(3-pyridyl)-5,16-androstadien-33-acetate] is a steroid compound which inhibits selectively and efficiently the enzyme 17-ohydroxylase-C17- 20-lyase, which catalyzes the conversion of dehydroepiandrosterone and androstenedione to testosterone. (google.com)
Arginine1
- Design, synthesis, and biological evaluation of tetrazole analogs of Cl-amidine as protein arginine deiminase inhibitors. (umassmed.edu)
Activity1
- Encoded by human CYP17A1 Gene (Cytochrome P450 Family), 508-aa 57-kDa Cytochrome P450 XVIIA1 is a cAMP-regulated endoplasmic reticulum P450 heme-thiolate monooxygenase with 17alpha-hydroxylase and 17,20-lyase activity and a key enzyme in the steroidogenic pathway that produces progestins, mineralocorticoids, glucocorticoids, androgens, and estrogens. (healthmatics.info)
Family1
- This enzyme belongs to the family of lyases, specifically amidine lyases. (wikipedia.org)
Common2
- Other names in common use include alpha-hydroxyglycine amidating dealkylase, peptidyl-alpha-hydroxyglycine alpha-amidating lyase, HGAD, PGL, PAL, and peptidylamidoglycolate peptidylamide-lyase. (wikipedia.org)
- Other names in common use include DNA-4,6-diamino-5-formamidopyrimidine 8-C,9-N-lyase (cyclizing), DNA-4,6-diamino-5-formamidopyrimidine 8-C,9-N-lyase (cyclizing, and DNA-adenine-forming). (wikipedia.org)
Mediated by S1P lyase1
- The only exit pathway of sphingolipid pathways is metabolism of S1P mediated by S1P lyase ( 3 ) ( Fig. 1 ). (spandidos-publications.com)