• aroG , encoding the monofunctional chorismate mutase (TtCM) of the thermophilic gram-negative bacterium Thermus thermophilus , was cloned and its gene product characterized. (springer.com)
  • Comparison of the enzyme's structure with that of its mesophilic counterpart from Bacillus revealed an increase in hydrophilicity on the protein's surface, greater hydrophobicity in cavities within the protein, and greater restriction of conformational freedom, features that contribute to the thermal stability of this chorismate mutase. (springer.com)
  • Chook YM, Gray JV, Ke H, Lipscomb WN (1994) The monofunctional chorismate mutase from Bacillus subtilis . (springer.com)
  • Structure determination of chorismate mutase and its complexes with a transition state analog and prephenate, and implications for the mechanism of the enzymatic reaction. (springer.com)
  • Escherichia coli aspartate transcarbamoylase versus yeast chorismate mutase. (springer.com)
  • MacBeath G, Kast P, Hilvert D (1998) A small, thermostable, and monofunctional chorismate mutase from the archaeon Methanococcus jannaschii . (springer.com)
  • Such cases exist: for example, a mutase such as phosphoglucomutase catalyses the transfer of a phospho group from one position to another, and isomerase is a more general term for an enzyme that catalyses any one-substrate one-product reaction, such as triosephosphate isomerase . (wikipedia.org)
  • Chorismate mutase catalyzes the Claisen rearrangement of chorismate to prephenate and provides a simple test for modeling an enzyme-catalyzed reaction. (openmopac.net)
  • Mechanisms of catalysis and allosteric regulation of yeast chorismate mutase from crystal structures. (openmopac.net)
  • Lorence, J.H. and Nester, E.W. Multiple molecular forms of chorismate mutase in Bacillus subtillis . (enzyme-database.org)
  • Woodin, T.S. and Nishioka, L. Evidence for three isozymes of chorismate mutase in alfalfa. (enzyme-database.org)
  • In the enteric bacteria, this enzyme also possesses chorismate mutase activity, thereby catalyzing the first two steps in the biosynthesis of tyrosine. (nih.gov)
  • For this research, they studied the chorismate mutase family of metabolic enzymes, a type of protein that is important for life in many bacteria, fungi, and plants. (swisscognitive.ch)
  • Echvi_0120 is a fusion with chorismate mutase. (lbl.gov)
  • Another significant variation between chorismate mutase is definitely activated in complex with DAH7PS suggests a key part of DAH7PS in the regulatory network of aromatic rate of metabolism of (26). (cyberdakwah.net)
  • Allosteric regulation of catalytic activity: Escherichia coli aspartate transcarbamoylase versus yeast chorismate mutase. (jove.com)
  • The enzyme chorismate lyase (EC 4.1.3.40) catalyzes the first step in ubiquinone biosynthesis, the removal of pyruvate from chorismate, to yield 4-hydroxybenzoate in Escherichia coli and other Gram-negative bacteria. (wikipedia.org)
  • This enzyme has an optimum pH at 7.5 Inhibited by: Vanillate 4-hydroxybenzaldehyde 3-carboxylmethylaminmethyl-4-hydroxybenzoic acid 4HB - ubiC is inhibited by the product of the reaction, which scientists believe serves as a control mechanism for the pathway The pathway used is called the ubiquinone biosynthesis pathway, it catalyzes the first step in the biosynthesis of ubiquinone in E. coli. (wikipedia.org)
  • This enzyme participates in ubiquinone biosynthesis. (np-mrd.org)
  • This enzyme catalyses the first step in ubiquinone biosynthesis in Escherichia coli and other Gram-negative bacteria. (np-mrd.org)
  • ATCase is part of the CAD multi-enzyme complex, part of the pyrimidine biosynthesis pathway, along with carbamoyl phosphate synthetase II and dihydroorotase. (jove.com)
  • In plants, the pathway produces chorismate, a precursor for the biosynthesis of a variety of central metabolites including, anthocyanins, flavonoids and isoflavonoids which are potential antioxidants with important nutritional benefits to humans. (utoronto.ca)
  • The systematic name of this enzyme class is chorismate pyruvate-lyase (4-hydroxybenzoate-forming). (wikipedia.org)
  • This enzyme catalyses the chemical reaction: chorismate ⇌ {\displaystyle \rightleftharpoons } 4-hydroxybenzoate + pyruvate Its activity does not require metal cofactors. (wikipedia.org)
  • It is also called chorismate pyruvate lyase (4-hydroxybenzoate-forming) and it is also abbreviated several different ways: CPL, CL, and ubiC. (wikipedia.org)
  • Chorismate lyase is an enzyme that transforms chorismate into 4-hydroxybenzoate and pyruvate. (np-mrd.org)
  • In the first step of this pathway, chorismate lyase transforms chorismate into 4-hydroxybenzoate and pyruvate (PMID 1644758). (foodcomex.org)
  • protein_coding" "Cz10g28290.t1","No alias","Chromochloris zofingiensis","Chorismate pyruvate-lyase Rv2949c-like [Interproscan]. (ntu.edu.sg)
  • In some organisms this enzyme is part of a multifunctional protein that also includes one or more of the enzymes EC 2.4.2.18 (anthranilate phosphoribosyltransferase), EC 4.1.1.48 (indole-3-glycerol-phosphate synthase), EC 4.1.3.27 (anthranilate synthase) and EC 5.3.1.24 (phosphoribosylanthranilate isomerase). (enzyme-database.org)
  • Woehl, E. and Dunn, M.F. Mechanisms of monovalent cation action in enzyme catalysis: the tryptophan synthase α-, β-, and αβ-reactions. (enzyme-database.org)
  • SA pre-treatment increased the expression of the chorismate synthase and isochorismate synthase genes in the epicotyl. (rosehybridizers.org)
  • Within the framework of a DFG research group (For 1296), we investigated the use of the enzyme MenD (SEPHCHC synthase) as a novel biocatalyst for 1,2- and 1,4-additions in cooperation with the group of Jürgen Pleiss (ITB, Univ. (uni-stuttgart.de)
  • An example of enzymes that bind a single substrate and release multiple products are proteases , which cleave one protein substrate into two polypeptide products. (wikipedia.org)
  • in such cases, it is helpful to determine the enzyme structure with and without bound substrate analogues that do not undergo the enzymatic reaction. (wikipedia.org)
  • Beyond this limit the enzyme is saturated with substrate and the reaction rate ceases to increase. (wikipedia.org)
  • For example, aspartate transcarbamoylase, also known as ATCase, is a large enzyme containing six catalytic subunits, each with a substrate binding site. (jove.com)
  • For the first time, the enzyme:substrate complex of the Schiff base type was elucidated for aldolases. (uni-stuttgart.de)
  • The pathway used by Chlamydiae for pABA synthesis differs from the canonical multi-enzyme pathway used by most bacteria that relies on chorismate as a metabolic precursor. (ncsu.edu)
  • UTP and CTP, the end products of the pyrimidine synthesis pathway, inhibit the activity of ATCase, the enzyme that catalyzes the first essential step of this pathway. (jove.com)
  • The Christendat lab studies the functional diversification of shikimate pathway enzymes in plants, microbes, and apicomplexan parasites. (utoronto.ca)
  • The DB consists of a collection of frames , where each frame encodes information about a single object, such as an enzyme, a gene, or a biochemical pathway. (ecocyc.org)
  • In enzyme kinetics, the reaction rate is measured and the effects of varying the conditions of the reaction are investigated. (wikipedia.org)
  • This rate-determining step may be a chemical reaction or a conformational change of the enzyme or substrates, such as those involved in the release of product(s) from the enzyme. (wikipedia.org)
  • The reaction catalysed by an enzyme uses exactly the same reactants and produces exactly the same products as the uncatalysed reaction. (wikipedia.org)
  • that is located in the appropriate position to assault the face of P-enolpyruvate during the course of the reaction, permitting the catalytic mechanism for this enzyme to be clearly defined. (cyberdakwah.net)
  • Both type I and type II DAH7PS enzymes share the common triosephosphate isomerase (TIM barrel) fold, and mechanistic studies have suggested that the key details of the reaction chemistry are related for enzymes of both DAH7PS types (25). (cyberdakwah.net)
  • The class Enzymatic-Reactions describes information specific to the pairing of an enzyme with a reaction that the enzyme catalyzes, such as its activators, inhibitors, and cofactors. (ecocyc.org)
  • An enzyme that catalyzes the conversion of prephenate to p-hydroxyphenylpyruvate in the presence of NAD . (nih.gov)
  • An enzyme that catalyzes the formation of anthranilate (o-aminobenzoate) and pyruvic acid from chorismate and glutamine. (nih.gov)
  • The enzyme catalyzes an essential step in pyrimidine synthesis, the condensation of aspartate and carbamoyl phosphate to produce carbamoyl aspartate. (jove.com)
  • Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to N-carbamoyl-L-aspartate. (jove.com)
  • The enzyme belongs to the rare group of AroH-type chorismate mutases which are mainly found in gram-positive bacteria of the Bacillus / Clostridia group and have recently also been described for gram-negative organisms. (springer.com)
  • Chorismic acid, more commonly known as its anionic form chorismate, is an important biochemical intermediate in plants and microorganisms. (ecmdb.ca)
  • The enzyme acts on L-tryptophan, 5-hydroxy-L-tryptophan and dihydroxy-L-phenylalanine. (shroomery.org)
  • COMMENT: In some organisms, this enzyme is part of a multifunctional protein together with one or more other components of the for biosymthesis of tryptophan (EC 2.4.2.18, 4.1.1.48, 4.2.1.20, 5.3.1.24). (shroomery.org)
  • Together these enzymes catalyze formation of tryptophan from chorismate. (thesciencenotes.com)
  • Likewise, other chorismate-derived substances such as violacein (via the intermediate L-tryptophan) could be obtained. (uni-stuttgart.de)
  • Taxonomic lineage: bacteria → proteobacteria → gammaproteobacteria → enterobacteriales → enterobacteriaceae → escherichia → Escherichia coli This enzyme is a monomer. (wikipedia.org)
  • Studying an enzyme's kinetics in this way can reveal the catalytic mechanism of this enzyme, its role in metabolism , how its activity is controlled, and how a drug or a modifier ( inhibitor or activator ) might affect the rate. (wikipedia.org)
  • Various thiamine diphosphate (ThDP)-dependent enzymes can - apart from their functions in metabolism - also be used as biocatalysts for C-C bond linkages. (uni-stuttgart.de)
  • HPLC-based assays were used to determine the enzyme activities and subsequently the inhibitory potentials of varying concentrations of a P. sidoides extract against the produced enzymes. (biomedcentral.com)
  • 4-Hydroxybenzoate is an intermediate in many enzyme-mediated reactions in microbes. (np-mrd.org)
  • Candidates for each step are identified by using ublast (a fast alternative to protein BLAST) against a database of manually-curated proteins (most of which are experimentally characterized) or by using HMMer with enzyme models (usually from TIGRFam ). (lbl.gov)
  • For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor. (jove.com)
  • HinfPDH is a dimeric enzyme, with each monomer consisting of an N-terminal α/β dinucleotide-binding domain and a C-terminal α-helical dimerization domain. (rcsb.org)
  • This enzyme participates in toluene and xylene degradation in bacteria such as Pseudomonas mendocina. (np-mrd.org)
  • This enzyme participates in 2,4-dichlorobenzoate degradation and is found in Candida parapsilosis. (np-mrd.org)
  • This enzyme participates in benzoate degradation via hydroxylation and 2,4-dichlorobenzoate degradation and is found in Pseudomonas putida and Pseudomonas fluorescens. (np-mrd.org)
  • This enzyme is involved in the degradation of N -acetylneuraminate. (qmul.ac.uk)
  • Furthermore, the transcriptional responses of B5 at different temperature by using rice straw as sole carbon sources were also analyzed, based on which the mechanism of lignocellulose degradation at high temperature was revealed that B5 could resist the heat by up-regulating the heat shock proteins (HSP) and then secrete various Carbohydrate-Active enzymes (CAZymes) to realize energy balance. (researchsquare.com)
  • Cornish-Bowden A (1976) Principles of enzyme kinetics. (springer.com)
  • Enzyme kinetics is the study of the rates of enzyme-catalysed chemical reactions . (wikipedia.org)
  • When enzymes bind multiple substrates, such as dihydrofolate reductase (shown right), enzyme kinetics can also show the sequence in which these substrates bind and the sequence in which products are released. (wikipedia.org)
  • Results A lignocellulose degrading strain isolated from thermophilic compost was identified as Geobacillus stearothermophilus B5, which could secrete considerable enzymes at the optimal temperature (60°C) and pH (7.5). (researchsquare.com)
  • GapMind searches the predicted proteins for candidates by using ublast (a fast alternative to protein BLAST) to find similarities to characterized proteins or by using HMMer to find similarities to enzyme models (usually from TIGRFams ). (lbl.gov)
  • Proteins that contain linked binding sites are called allosteric proteins and can be of various types, such as enzymes, receptors, structural proteins, and motor proteins. (jove.com)
  • The structure determination process was an unusual one, involving 12 monomers of the enzyme in the asymmetric unit. (wikigenes.org)
  • The structure of the decameric enzyme FSA was also solved. (uni-stuttgart.de)
  • The main difference between ribozymes and enzymes is that RNA catalysts are composed of nucleotides, whereas enzymes are composed of amino acids. (wikipedia.org)
  • Moreover, an intermediate-enzyme adduct with a NOS-covalent linkage was observed in the later site, where it acts as a two-scissile-bond linkage facilitating nucleophilic addition and cofactor-free decarboxylation. (hokudai.ac.jp)
  • We are investigating enzymes that can make or cleave C-C bonds, as these are suitable biocatalysts in chemo-enzymatic syntheses, e.g. to produce novel hydroxylated compounds. (uni-stuttgart.de)
  • 4-hydroxybenzoate and chloride are produced when the enzyme 4-chlorobenzoate dehalogenase acts on the halide bond of 4-chlorobenzoate with H2O (PMID: 6497878). (foodcomex.org)
  • The native molecular mass is consistent with a pseudo-α/β barrel enzyme that is organized as a trimer. (springer.com)
  • For instance, the enzyme 4-hydroxybenzaldehyde dehydrogenase uses 4-hydroxybenzaldehyde, NAD+ and H2O to produce 4-hydroxybenzoate, NADH and H+. (np-mrd.org)
  • The aim of this study was to develop a platform of Mycobacterium tuberculosis (Mtb) kinase enzymes that may be used for the identification of therapeutically relevant ethnobotanical extracts that will allow drug target identification, as well as the subsequent isolation of the active compounds. (biomedcentral.com)
  • These enzyme targets were further assessed for compound identification from the P. sidoides literature. (biomedcentral.com)
  • The native enzyme in the complex uses either or, less efficiently, NH3. (shroomery.org)
  • The enzyme separated from the complex uses NH3 only. (shroomery.org)
  • That enzyme cannot combine with the α unit of EC 4.2.1.20 to form a complex. (enzyme-database.org)
  • The enzyme activity assays indicated that these enzymes were active at low ATP concentrations. (biomedcentral.com)