Acetate Kinase: An enzyme that catalyzes reversibly the phosphorylation of acetate in the presence of a divalent cation and ATP with the formation of acetylphosphate and ADP. It is important in the glycolysis process. EC 2.7.2.1.Phosphate Acetyltransferase: An enzyme that catalyzes the synthesis of acetylphosphate from acetyl-CoA and inorganic phosphate. Acetylphosphate serves as a high-energy phosphate compound. EC 2.3.1.8.Acetates: Derivatives of ACETIC ACID. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain the carboxymethane structure.Methanosarcina: A genus of anaerobic, irregular spheroid-shaped METHANOSARCINALES whose organisms are nonmotile. Endospores are not formed. These archaea derive energy via formation of methane from acetate, methanol, mono-, di-, and trimethylamine, and possibly, carbon monoxide. Organisms are isolated from freshwater and marine environments.Antibodies: Immunoglobulin molecules having a specific amino acid sequence by virtue of which they interact only with the ANTIGEN (or a very similar shape) that induced their synthesis in cells of the lymphoid series (especially PLASMA CELLS).Organophosphates: Carbon-containing phosphoric acid derivatives. Included under this heading are compounds that have CARBON atoms bound to one or more OXYGEN atoms of the P(=O)(O)3 structure. Note that several specific classes of endogenous phosphorus-containing compounds such as NUCLEOTIDES; PHOSPHOLIPIDS; and PHOSPHOPROTEINS are listed elsewhere.Antibody Specificity: The property of antibodies which enables them to react with some ANTIGENIC DETERMINANTS and not with others. Specificity is dependent on chemical composition, physical forces, and molecular structure at the binding site.Enzyme-Linked Immunosorbent Assay: An immunoassay utilizing an antibody labeled with an enzyme marker such as horseradish peroxidase. While either the enzyme or the antibody is bound to an immunosorbent substrate, they both retain their biologic activity; the change in enzyme activity as a result of the enzyme-antibody-antigen reaction is proportional to the concentration of the antigen and can be measured spectrophotometrically or with the naked eye. Many variations of the method have been developed.Antibodies, Viral: Immunoglobulins produced in response to VIRAL ANTIGENS.Recombinant Proteins: Proteins prepared by recombinant DNA technology.Phosphotransferases (Carboxyl Group Acceptor): A class of enzymes that transfers phosphate groups and has a carboxyl group as an acceptor. EC 2.7.2.Fatigue: The state of weariness following a period of exertion, mental or physical, characterized by a decreased capacity for work and reduced efficiency to respond to stimuli.Propionates: Derivatives of propionic acid. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain the carboxyethane structure.Databases, Protein: Databases containing information about PROTEINS such as AMINO ACID SEQUENCE; PROTEIN CONFORMATION; and other properties.Sequence Analysis, Protein: A process that includes the determination of AMINO ACID SEQUENCE of a protein (or peptide, oligopeptide or peptide fragment) and the information analysis of the sequence.Systems Integration: The procedures involved in combining separately developed modules, components, or subsystems so that they work together as a complete system. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)Internet: A loose confederation of computer communication networks around the world. The networks that make up the Internet are connected through several backbone networks. The Internet grew out of the US Government ARPAnet project and was designed to facilitate information exchange.Acetates: Derivatives of ACETIC ACID. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain the carboxymethane structure.Proteins: Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein.Proteome: The protein complement of an organism coded for by its genome.Acetate Kinase: An enzyme that catalyzes reversibly the phosphorylation of acetate in the presence of a divalent cation and ATP with the formation of acetylphosphate and ADP. It is important in the glycolysis process. EC 2.7.2.1.Phosphate Acetyltransferase: An enzyme that catalyzes the synthesis of acetylphosphate from acetyl-CoA and inorganic phosphate. Acetylphosphate serves as a high-energy phosphate compound. EC 2.3.1.8.Clostridium thermocellum: A species of gram-positive, thermophilic, cellulolytic bacteria in the family Clostridaceae. It degrades and ferments CELLOBIOSE and CELLULOSE to ETHANOL in the CELLULOSOME.Methanosarcina: A genus of anaerobic, irregular spheroid-shaped METHANOSARCINALES whose organisms are nonmotile. Endospores are not formed. These archaea derive energy via formation of methane from acetate, methanol, mono-, di-, and trimethylamine, and possibly, carbon monoxide. Organisms are isolated from freshwater and marine environments.Acetates: Derivatives of ACETIC ACID. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain the carboxymethane structure.Acetate-CoA Ligase: An enzyme that catalyzes the formation of CoA derivatives from ATP, acetate, and CoA to form AMP, pyrophosphate, and acetyl CoA. It acts also on propionates and acrylates. EC 6.2.1.1.Genetic Complementation Test: A test used to determine whether or not complementation (compensation in the form of dominance) will occur in a cell with a given mutant phenotype when another mutant genome, encoding the same mutant phenotype, is introduced into that cell.Cloning, Molecular: The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.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: The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.Aplysia: An opisthobranch mollusk of the order Anaspidea. It is used frequently in studies of nervous system development because of its large identifiable neurons. Aplysiatoxin and its derivatives are not biosynthesized by Aplysia, but acquired by ingestion of Lyngbya (seaweed) species.Migraine Disorders: A class of disabling primary headache disorders, characterized by recurrent unilateral pulsatile headaches. The two major subtypes are common migraine (without aura) and classic migraine (with aura or neurological symptoms). (International Classification of Headache Disorders, 2nd ed. Cephalalgia 2004: suppl 1)Motor Neurons: Neurons which activate MUSCLE CELLS.Phenotype: The outward appearance of the individual. It is the product of interactions between genes, and between the GENOTYPE and the environment.Alginates: Salts of alginic acid that are extracted from marine kelp and used to make dental impressions and as absorbent material for surgical dressings.Headache Disorders: Various conditions with the symptom of HEADACHE. Headache disorders are classified into major groups, such as PRIMARY HEADACHE DISORDERS (based on characteristics of their headache symptoms) and SECONDARY HEADACHE DISORDERS (based on their etiologies). (International Classification of Headache Disorders, 2nd ed. Cephalalgia 2004: suppl 1)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.HIV-1: The type species of LENTIVIRUS and the etiologic agent of AIDS. It is characterized by its cytopathic effect and affinity for the T4-lymphocyte.Cloning, Molecular: The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.Glutathione: A tripeptide with many roles in cells. It conjugates to drugs to make them more soluble for excretion, is a cofactor for some enzymes, is involved in protein disulfide bond rearrangement and reduces peroxides.Enoyl-CoA Hydratase: An enzyme that catalyzes reversibly the hydration of unsaturated fatty acyl-CoA to yield beta-hydroxyacyl-CoA. It plays a role in the oxidation of fatty acids and in mitochondrial fatty acid synthesis, has broad specificity, and is most active with crotonyl-CoA. EC 4.2.1.17.Dihydrolipoamide Dehydrogenase: A flavoprotein containing oxidoreductase that catalyzes the reduction of lipoamide by NADH to yield dihydrolipoamide and NAD+. The enzyme is a component of several MULTIENZYME COMPLEXES.Acyl-CoA Dehydrogenase: A flavoprotein oxidoreductase that has specificity for medium-chain fatty acids. It forms a complex with ELECTRON TRANSFERRING FLAVOPROTEINS and conveys reducing equivalents to UBIQUINONE.Acyl-CoA Dehydrogenases: Enzymes that catalyze the first step in the beta-oxidation of FATTY ACIDS.Transaminases: A subclass of enzymes of the transferase class that catalyze the transfer of an amino group from a donor (generally an amino acid) to an acceptor (generally a 2-keto acid). Most of these enzymes are pyridoxyl phosphate proteins. (Dorland, 28th ed) EC 2.6.1.3-Hydroxyacyl CoA Dehydrogenases: Enzymes that reversibly catalyze the oxidation of a 3-hydroxyacyl CoA to 3-ketoacyl CoA in the presence of NAD. They are key enzymes in the oxidation of fatty acids and in mitochondrial fatty acid synthesis.Dodecenoyl-CoA Isomerase: A carbon-carbon double bond isomerase that catalyzes the movement double bond from C3 to C2 of an unsaturated acyl-CoA. The enzyme plays a key role in allowing acyl-CoA substrates to re-enter the beta-oxidation pathway.Hydro-Lyases: Enzymes that catalyze the breakage of a carbon-oxygen bond leading to unsaturated products via the removal of water. EC 4.2.1.Alcohol Oxidoreductases: A subclass of enzymes which includes all dehydrogenases acting on primary and secondary alcohols as well as hemiacetals. They are further classified according to the acceptor which can be NAD+ or NADP+ (subclass 1.1.1), cytochrome (1.1.2), oxygen (1.1.3), quinone (1.1.5), or another acceptor (1.1.99).Amino Acids, Branched-Chain: Amino acids which have a branched carbon chain.Pyruvate Dehydrogenase (Lipoamide): The E1 component of the multienzyme PYRUVATE DEHYDROGENASE COMPLEX. It is composed of 2 alpha subunits (pyruvate dehydrogenase E1 alpha subunit) and 2 beta subunits (pyruvate dehydrogenase E1 beta subunit).Dihydrolipoamide Dehydrogenase: A flavoprotein containing oxidoreductase that catalyzes the reduction of lipoamide by NADH to yield dihydrolipoamide and NAD+. The enzyme is a component of several MULTIENZYME COMPLEXES.Pyruvate Dehydrogenase Complex: A multienzyme complex responsible for the formation of ACETYL COENZYME A from pyruvate. The enzyme components are PYRUVATE DEHYDROGENASE (LIPOAMIDE); dihydrolipoamide acetyltransferase; and LIPOAMIDE DEHYDROGENASE. Pyruvate dehydrogenase complex is subject to three types of control: inhibited by acetyl-CoA and NADH; influenced by the energy state of the cell; and inhibited when a specific serine residue in the pyruvate decarboxylase is phosphorylated by ATP. PYRUVATE DEHYDROGENASE (LIPOAMIDE)-PHOSPHATASE catalyzes reactivation of the complex. (From Concise Encyclopedia Biochemistry and Molecular Biology, 3rd ed)Pyruvate Dehydrogenase Complex Deficiency Disease: An inherited metabolic disorder caused by deficient enzyme activity in the PYRUVATE DEHYDROGENASE COMPLEX, resulting in deficiency of acetyl CoA and reduced synthesis of acetylcholine. Two clinical forms are recognized: neonatal and juvenile. The neonatal form is a relatively common cause of lactic acidosis in the first weeks of life and may also feature an erythematous rash. The juvenile form presents with lactic acidosis, alopecia, intermittent ATAXIA; SEIZURES; and an erythematous rash. (From J Inherit Metab Dis 1996;19(4):452-62) Autosomal recessive and X-linked forms are caused by mutations in the genes for the three different enzyme components of this multisubunit pyruvate dehydrogenase complex. One of the mutations at Xp22.2-p22.1 in the gene for the E1 alpha component of the complex leads to LEIGH DISEASE.Acetyl-CoA Carboxylase: A carboxylating enzyme that catalyzes the conversion of ATP, acetyl-CoA, and HCO3- to ADP, orthophosphate, and malonyl-CoA. It is a biotinyl-protein that also catalyzes transcarboxylation. The plant enzyme also carboxylates propanoyl-CoA and butanoyl-CoA (From Enzyme Nomenclature, 1992) EC 6.4.1.2.Acetate-CoA Ligase: An enzyme that catalyzes the formation of CoA derivatives from ATP, acetate, and CoA to form AMP, pyrophosphate, and acetyl CoA. It acts also on propionates and acrylates. EC 6.2.1.1.Carbon-Nitrogen Ligases: Enzymes that catalyze the joining of two molecules by the formation of a carbon-nitrogen bond. EC 6.3.Dihydrolipoyllysine-Residue Acetyltransferase: An enzyme that catalyzes the acetyltransferase reaction using ACETYL CoA as an acetyl donor and dihydrolipoamide as acceptor to produce COENZYME A (CoA) and S-acetyldihydrolipoamide. It forms the (E2) subunit of the PYRUVATE DEHYDROGENASE COMPLEX.Acinetobacter baumannii: A species of gram-negative, aerobic bacteria, commonly found in the clinical laboratory, and frequently resistant to common antibiotics.Fatty Acid Synthase, Type II: The form of fatty acid synthase complex found in BACTERIA; FUNGI; and PLANTS. Catalytic steps are like the animal form but the protein structure is different with dissociated enzymes encoded by separate genes. It is a target of some ANTI-INFECTIVE AGENTS which result in disruption of the CELL MEMBRANE and CELL WALL.
(1/86) Purification and characterization of two extremely thermostable enzymes, phosphate acetyltransferase and acetate kinase, from the hyperthermophilic eubacterium Thermotoga maritima.

Phosphate acetyltransferase (PTA) and acetate kinase (AK) of the hyperthermophilic eubacterium Thermotoga maritima have been purified 1,500- and 250-fold, respectively, to apparent homogeneity. PTA had an apparent molecular mass of 170 kDa and was composed of one subunit with a molecular mass of 34 kDa, suggesting a homotetramer (alpha4) structure. The N-terminal amino acid sequence showed significant identity to that of phosphate butyryltransferases from Clostridium acetobutylicum rather than to those of known phosphate acetyltransferases. The kinetic constants of the reversible enzyme reaction (acetyl-CoA + Pi -->/<-- acetyl phosphate + CoA) were determined at the pH optimum of pH 6.5. The apparent Km values for acetyl-CoA, Pi, acetyl phosphate, and coenzyme A (CoA) were 23, 110, 24, and 30 microM, respectively; the apparent Vmax values (at 55 degrees C) were 260 U/mg (acetyl phosphate formation) and 570 U/mg (acetyl-CoA formation). In addition to acetyl-CoA (100%), the enzyme accepted propionyl-CoA (60%) and butyryl-CoA (30%). The enzyme had a temperature optimum at 90 degrees C and was not inactivated by heat upon incubation at 80 degrees C for more than 2 h. AK had an apparent molecular mass of 90 kDa and consisted of one 44-kDa subunit, indicating a homodimer (alpha2) structure. The N-terminal amino acid sequence showed significant similarity to those of all known acetate kinases from eubacteria as well that of the archaeon Methanosarcina thermophila. The kinetic constants of the reversible enzyme reaction (acetyl phosphate + ADP -->/<-- acetate + ATP) were determined at the pH optimum of pH 7.0. The apparent Km values for acetyl phosphate, ADP, acetate, and ATP were 0.44, 3, 40, and 0.7 mM, respectively; the apparent Vmax values (at 50 degrees C) were 2,600 U/mg (acetate formation) and 1,800 U/mg (acetyl phosphate formation). AK phosphorylated propionate (54%) in addition to acetate (100%) and used GTP (100%), ITP (163%), UTP (56%), and CTP (21%) as phosphoryl donors in addition to ATP (100%). Divalent cations were required for activity, with Mn2+ and Mg2+ being most effective. The enzyme had a temperature optimum at 90 degrees C and was stabilized against heat inactivation by salts. In the presence of (NH4)2SO4 (1 M), which was most effective, the enzyme did not lose activity upon incubation at 100 degrees C for 3 h. The temperature optimum at 90 degrees C and the high thermostability of both PTA and AK are in accordance with their physiological function under hyperthermophilic conditions.  (+info)

(2/86) Cloning, sequence analysis, expression and inactivation of the Corynebacterium glutamicum pta-ack operon encoding phosphotransacetylase and acetate kinase.

The Corynebacterium glutamicum ack and pta genes encoding the acetate-activating enzymes acetate kinase and phosphotransacetylase were isolated, subcloned on a plasmid and re-introduced into Corynebacterium glutamicum. Relative to the wild-type, the recombinant strains showed about tenfold higher specific activities of both enzymes. Sequence analysis of a 3657 bp DNA fragment revealed that the ack and pta genes are contiguous in the corynebacterial chromosome, with pta upstream and the last nucleotide of the pta stop codon (TAA) overlapping the first of the ack start codon (ATG). The predicted gene product of pta consists of 329 amino acids (Mr 35242), that of ack consists of 397 amino acids (Mr 43098) and the amino acid sequences of the two polypeptides show up to 60 % (phosphotransacetylase) and 53% (acetate kinase) identity in comparison with respective enzymes from other organisms. Northern (RNA) blot hybridizations using pta- and ack-specific probes and transcriptional cat fusion experiments revealed that the two genes are transcribed as a 2.5 kb bicistronic mRNA and that the expression of this operon is induced when Corynebacterium glutamicum grows on acetate instead of glucose as a carbon source. Directed inactivation of the chromosomal pta and ack genes led to the absence of detectable phosphotransacetylase and acetate kinase activity in the respective mutants and to their inability to grow on acetate. These data indicate that no isoenzymes of acetate kinase and phosphotransacetylase are present in Corynebacterium glutamicum and that a functional acetate kinase/phosphotransacetylase pathway is essential for growth of this organism on acetate.  (+info)

(3/86) Genes coding for phosphotransacetylase and acetate kinase in Sinorhizobium meliloti are in an operon that is inducible by phosphate stress and controlled by phoB.

Recent work in this laboratory has shown that the gene coding for acetate kinase (ackA) in Sinorhizobium meliloti is up-regulated in response to phosphate limitation. Characterization of the region surrounding ackA revealed that it is adjacent to pta, which codes for phosphotransacetylase, and that these two genes are part of an operon composed of at least two additional genes in the following order: an open reading frame (orfA), pta, ackA, and the partial sequence of a gene with an inferred peptide that has a high degree of homology to enoyl-ACP reductase (fabI). Experiments combining enzyme assays, a chromosomal lacZ::ackA transcriptional fusion, complementation analysis with cosmid subclones, and the creation of mutations in pta and ackA all indicated that the orfA-pta-ackA-fabI genes are cotranscribed in response to phosphate starvation. Primer extension was used to map the position of the phosphate starvation-inducible transcriptional start sites upstream of orfA. The start sites were found to be preceded by a sequence having similarity to PHO boxes from other phosphate-regulated genes in S. meliloti and to the consensus PHO box in Escherichia coli. Introduction of a phoB mutation in the wild-type strain eliminated elevated levels of acetate kinase and phosphotransacetylase activities in response to phosphate limitation and also eliminated the phosphate stress-induced up-regulation of the ackA::lacZ fusion. Mutations in either ackA alone or both pta and ackA did not affect the nodulation or nitrogen fixation phenotype of S. meliloti.  (+info)

(4/86) Homofermentative production of D- or L-lactate in metabolically engineered Escherichia coli RR1.

We investigated metabolic engineering of fermentation pathways in Escherichia coli for production of optically pure D- or L-lactate. Several pta mutant strains were examined, and a pta mutant of E. coli RR1 which was deficient in the phosphotransacetylase of the Pta-AckA pathway was found to metabolize glucose to D-lactate and to produce a small amount of succinate by-product under anaerobic conditions. An additional mutation in ppc made the mutant produce D-lactate like a homofermentative lactic acid bacterium. When the pta ppc double mutant was grown to higher biomass concentrations under aerobic conditions before it shifted to the anaerobic phase of D-lactate production, more than 62.2 g of D-lactate per liter was produced in 60 h, and the volumetric productivity was 1.04 g/liter/h. To examine whether the blocked acetate flux could be reoriented to a nonindigenous L-lactate pathway, an L-lactate dehydrogenase gene from Lactobacillus casei was introduced into a pta ldhA strain which lacked phosphotransacetylase and D-lactate dehydrogenase. This recombinant strain was able to metabolize glucose to L-lactate as the major fermentation product, and up to 45 g of L-lactate per liter was produced in 67 h. These results demonstrate that the central fermentation metabolism of E. coli can be reoriented to the production of D-lactate, an indigenous fermentation product, or to the production of L-lactate, a nonindigenous fermentation product.  (+info)

(5/86) Characterization of a group of anaerobically induced, fnr-dependent genes of Salmonella typhimurium.

We have previously reported the isolation of a group of anaerobically regulated, fnr-dependent lac fusions in Salmonella typhimurium and have grouped these oxd genes into classes based on map position. In order to identify these genes, we have replaced the original Mud-lac fusion in a member of each oxd class with the much smaller Mud-cam element, cloned the fusion, and determined DNA sequence sufficient to define the oxd gene. Several of the fusions correspond to previously known genes from S. typhimurium or Escherichia coli: oxd-4 = cbiA and oxd-11 = cbiK, oxd-5 = hybB, oxd-7 = dcuB, oxd-8 = moaB, oxd-12 = dmsA, and oxd-14 = napB (aeg-46. 5). Two other fusions correspond to previously unknown loci: oxd-2 encodes an acetate/propionate kinase, and oxd-6 encodes a putative ABC transporter present in S. typhimurium but not in E. coli.  (+info)

(6/86) Catabolite regulation of the pta gene as part of carbon flow pathways in Bacillus subtilis.

In Bacillus subtilis, the products of the pta and ackA genes, phosphotransacetylase and acetate kinase, play a crucial role in the production of acetate, one of the most abundant by-products of carbon metabolism in this gram-positive bacterium. Although these two enzymes are part of the same pathway, only mutants with inactivated ackA did not grow in the presence of glucose. Inactivation of pta had only a weak inhibitory effect on growth. In contrast to pta and ackA in Escherichia coli, the corresponding B. subtilis genes are not cotranscribed. Expression of the pta gene was increased in the presence of glucose, as has been reported for ackA. The effects of the predicted cis-acting catabolite response element (CRE) located upstream from the promoter and of the trans-acting proteins CcpA, HPr, Crh, and HPr kinase on the catabolite regulation of pta were investigated. As for ackA, glucose activation was abolished in ccpA and hprK mutants and in the ptsH1 crh double mutant. Footprinting experiments demonstrated an interaction between CcpA and the pta CRE sequence, which is almost identical to the proposed CRE consensus sequence. This interaction occurs only in the presence of Ser-46-phosphorylated HPr (HPrSer-P) or Ser-46-phosphorylated Crh (CrhSer-P) and fructose-1,6-bisphosphate (FBP). In addition to CcpA, carbon catabolite activation of the pta gene therefore requires at least two other cofactors, FBP and either HPr or Crh, phosphorylated at Ser-46 by the ATP-dependent Hpr kinase.  (+info)

(7/86) The role of histidines in the acetate kinase from Methanosarcina thermophila.

The role of histidine in the catalytic mechanism of acetate kinase from Methanosarcina thermophila was investigated by diethylpyrocarbonate inactivation and site-directed mutagenesis. Inactivation was accompanied by an increase in absorbance at 240 nm with no change in absorbance at 280 nm, and treatment of the inactivated enzyme with hydroxylamine restored 95% activity, results that indicated diethylpyrocarbonate inactivates the enzyme by the specific modification of histidine. The substrates ATP, ADP, acetate, and acetyl phosphate protected against inactivation suggesting at least one active site where histidine is modified. Correlation of residual activity with the number of histidines modified, as determined by absorbance at 240 nm, indicated that a maximum of three histidines are modified per subunit, two of which are essential for full inactivation. Comparison of the M. thermophila acetate kinase sequence with 56 putative acetate kinase sequences revealed eight highly conserved histidines, three of which (His-123, His-180, and His-208) are perfectly conserved. Diethylpyrocarbonate inactivation of the eight histidine --> alanine variants indicated that His-180 and His-123 are in the active site and that the modification of both is necessary for full inactivation. Kinetic analyses of the eight variants showed that no other histidines are important for activity. Analysis of additional His-180 variants indicated that phosphorylation of His-180 is not essential for catalysis. Possible functions of His-180 are discussed.  (+info)

(8/86) Urkinase: structure of acetate kinase, a member of the ASKHA superfamily of phosphotransferases.

Acetate kinase, an enzyme widely distributed in the Bacteria and Archaea domains, catalyzes the phosphorylation of acetate. We have determined the three-dimensional structure of Methanosarcina thermophila acetate kinase bound to ADP through crystallography. As we previously predicted, acetate kinase contains a core fold that is topologically identical to that of the ADP-binding domains of glycerol kinase, hexokinase, the 70-kDa heat shock cognate (Hsc70), and actin. Numerous charged active-site residues are conserved within acetate kinases, but few are conserved within the phosphotransferase superfamily. The identity of the points of insertion of polypeptide segments into the core fold of the superfamily members indicates that the insertions existed in the common ancestor of the phosphotransferases. Another remarkable shared feature is the unusual, epsilon conformation of the residue that directly precedes a conserved glycine residue (Gly-331 in acetate kinase) that binds the alpha-phosphate of ADP. Structural, biochemical, and geochemical considerations indicate that an acetate kinase may be the ancestral enzyme of the ASKHA (acetate and sugar kinases/Hsc70/actin) superfamily of phosphotransferases.  (+info)

*  Acetate kinase
In molecular biology, acetate kinase (EC 2.7.2.1), which is predominantly found in micro-organisms, facilitates the production ... The growth of a bacterial mutant lacking acetate kinase has been shown to be inhibited by glucose, suggesting that the enzyme ... Grundy FJ, Waters DA, Allen SH, Henkin TM (November 1993). "Regulation of the Bacillus subtilis acetate kinase gene by CcpA". J ... Salmonella typhimurium propionate kinase (StTdcD) catalyzes reversible transfer of the γ-phosphate of ATP to propionate during ...
*  Acetate kinase (diphosphate)
Reeves RE, Guthrie JD (1975). "Acetate kinase (pyrophosphate). A fourth pyrophosphate-dependent kinase from Entamoeba ... an acetate kinase (diphosphate) (EC 2.7.2.12) is an enzyme that catalyzes the chemical reaction diphosphate + acetate ⇌ {\ ... The systematic name of this enzyme class is diphosphate:acetate phosphotransferase. This enzyme is also called pyrophosphate- ... the two substrates of this enzyme are diphosphate and acetate, whereas its two products are phosphate and acetyl phosphate. ...
*  Butyrate kinase
Ballongue, Jean; Amine, Jamel; Gay, Peptitdemange; Gay, Robert (July 1986). "Regulation of acetate kinase and butyrate kinase ... Butyrate kinase is active within the human colon. To form butyrate, two molecules of acetyl-CoA are combined and reduced to ... One study has previously found that butyrate kinase is not regulated by its end-products or other acids such as acetic acid, ... Butyryl-phosphate is then converted into butyrate by using butyrate kinase and in the process, releases ATP. Butyrate plays an ...
*  Propionate kinase
... (EC 2.7.2.15, PduW, TdcD, propionate/acetate kinase) is an enzyme with systematic name ATP:propanoate ... "Characterization of the acetate binding pocket in the Methanosarcina thermophila acetate kinase". J. Bacteriol. 187: 2386-2394 ... comparison with members of acetate and sugar kinase/heat shock cognate 70/actin superfamily". J. Mol. Biol. 352: 876-892. doi: ... Propionate kinase at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular Biology portal ...
*  Methanosarcina
... the team concluded that the microbe likely acquired the ability to efficiently consume acetate using acetate kinase and ... Scientists hypothesize acetate kinase could be the urkinase in a major protein superfamily that includes actin. Evidence ... Recently researchers have proposed an evolution hypothesis for acetate kinase and phosphoacetyl transferase with genomic ... structure of acetate kinase, a member of the ASKHA superfamily of phosphotransferases". Journal of Bacteriology. 183 (2): 680- ...
*  Mixed acid fermentation
Acetate formation requires two enzymes: phosphate acetyltransferase and acetate kinase. acetyl-CoA + phosphate → acetyl- ... The E. coli strain W3110 was genetically engineered to generate 2 moles of acetate for every 1 mole of glucose that undergoes ... For instance, strains for the increased production of ethanol, lactate, succinate and acetate have been developed due to the ... The mixture of end products produced by mixed acid fermentation includes lactate, acetate, succinate, formate, ethanol and the ...
*  Branched-chain-fatty-acid kinase
Harwood CS, Canale-Parola E (1982). "Properties of acetate kinase isozymes and a branched-chain fatty acid kinase from a ... In enzymology, a branched-chain-fatty-acid kinase (EC 2.7.2.14) is an enzyme that catalyzes the chemical reaction ATP + 2- ... This enzyme is also called isobutyrate kinase. ...
*  Dimethyl dicarbonate
242), and acts by inhibiting the enzymes acetate kinase and L-glutamic acid decarboxylase. It has also been proposed that DMDC ...
*  Corynebacterium
... decaprenyl-phosphate phosphoribosyltransferase and a three-amino-acid insertion in acetate kinase, both of which are found only ...
*  SLC1A1
González MI, Bannerman PG, Robinson MB (2003). "Phorbol myristate acetate-dependent interaction of protein kinase Calpha and ...
*  HABP4
... interacts with RACK1 and is a substrate for the phosphorylation by phorbol 12-myristate 13-acetate-activated protein kinase C ... The protein kinase Ki-1/57 occurs in the nucleus". Am. J. Pathol. 140 (2): 473-82. PMC 1886443 . PMID 1310832. Strausberg RL, ...
*  Exopolyphosphatase
... acetate and sugar kinases, Hsp70, actin). In A. aeolicus, the active site of the enzyme exists in a cleft between the two ... This can be accomplished via inhibition of polyphosphate kinase, enhancement of exopolyphosphatase activity, or both. ... which includes polyphosphate kinase [PPK] and PPX) and develop a wide variety of assays and techniques for quantification of ... by the lab of Nobel laureate Arthur Kornberg in 1993 and is part of the polyphosphate operon along with polyphosphate kinase, ...
*  Sphingosine kinase 1
Extracellular release of sphingosine-1-phosphate induced by phorbol 12-myristate 13-acetate (PMA)". The Journal of Biological ... Sphingosine kinase 1 is an enzyme that in humans is encoded by the SPHK1 gene. Sphingosine kinase 1 phosphorylates sphingosine ... "Entrez Gene: SPHK1 sphingosine kinase 1". Xia P, Wang L, Moretti PA, Albanese N, Chai F, Pitson SM, D'Andrea RJ, Gamble JR, ... Xia P, Wang L, Moretti PA, Albanese N, Chai F, Pitson SM, D'Andrea RJ, Gamble JR, Vadas MA (Mar 2002). "Sphingosine kinase ...
*  PTK2B
... of the related adhesion focal tyrosine kinase in megakaryocytes upon stem cell factor and phorbol myristate acetate stimulation ... "Protein tyrosine kinase PYK2 involved in Ca(2+)-induced regulation of ion channel and MAP kinase functions". Nature. 376 (6543 ... Protein tyrosine kinase 2 beta is an enzyme that in humans is encoded by the PTK2B gene. This gene encodes a cytoplasmic ... "Entrez Gene: PTK2B PTK2B protein tyrosine kinase 2 beta". Soni D, Regmi SC, Wang DM, DebRoy A, Zhao YY, Vogel SM, Malik AB, ...
*  Paxillin
... of the related adhesion focal tyrosine kinase in megakaryocytes upon stem cell factor and phorbol myristate acetate stimulation ... The proteins that bind to paxillin are diverse and include protein tyrosine kinases, such as Src and focal adhesion kinase (FAK ... "Activation of pyk2/related focal adhesion tyrosine kinase and focal adhesion kinase in cardiac remodeling". The Journal of ... We also know that the binding of paxillin to focal adhesion kinase (FAK) is critical for directing paxillin function. The ...
*  Phorbol 12,13-dibutyrate
As an activator of protein kinase C, it is a weak tumor promoter compared to 12-O-tetradecanoylphorbol-13-acetate. PDBu is ...
*  List of EC numbers (EC 2)
UDP-N-acetylglucosamine kinase EC 2.7.1.177: L-threonine kinase EC 2.7.2.1: acetate kinase EC 2.7.2.2: carbamate kinase EC 2.7. ... subunit kinase EC 2.7.11.24: mitogen-activated protein kinase EC 2.7.11.25: mitogen-activated protein kinase kinase kinase EC ... EC 2.7.1.71: shikimate kinase EC 2.7.1.72: streptomycin 6-kinase EC 2.7.1.73: inosine kinase EC 2.7.1.74: deoxycytidine kinase ... glutamate 5-kinase EC 2.7.2.12: acetate kinase (diphosphate) EC 2.7.2.13: glutamate 1-kinase EC 2.7.2.14: branched-chain-fatty- ...
*  List of MeSH codes (D08)
... acetate kinase MeSH D08.811.913.696.630.050 --- aspartate kinase MeSH D08.811.913.696.630.050.050 --- aspartokinase homoserine ... map kinase kinase kinases MeSH D08.811.913.696.620.682.700.559.100 --- map kinase kinase kinase 1 MeSH D08.811.913.696.620.682. ... map kinase kinase kinase 2 MeSH D08.811.913.696.620.682.700.559.300 --- map kinase kinase kinase 3 MeSH D08.811.913.696.620.682 ... map kinase kinase kinase 4 MeSH D08.811.913.696.620.682.700.559.500 --- map kinase kinase kinase 5 MeSH D08.811.913.696.620.682 ...
*  Small molecule
An example is the teratogen and carcinogen phorbol 12-myristate 13-acetate, which is a plant terpene that activates protein ... kinase C, which promotes cancer, making it a useful investigative tool. There is also interest in creating small molecule ...
*  Ulocladium botrytis
doi:10.1007/s00374-007-0217-7. Höller, Ulrich; König, Gabriele M.; Wright, Anthony D. (November 1999). "A New Tyrosine Kinase ... was found in ethyl acetate extract from U. botrytis. Ulocladium botrytis also synthesizes extracellular keratinases and can ... Additionally, a new tyrosine kinase (p56tck) inhibitor called ulocladol, with the molecular formula C16H14O7, ...
*  Torreyanic acid
... was found to be 5-10 times more potent in cell lines sensitive to protein kinase C (PKC) agonists, 12-o- ... tetradecanoyl phorbol-13-acetate (TPA), and was shown to cause cell death via apoptosis. Torreyanic acid also promoted G1 ...
*  Tumor promotion
Mitogen-activated protein kinase kinase, VEGF, or Akt. Tumor progression Phorbol myristate acetate Seth Rakoff-Nahoum (Dec 2006 ...
*  Hydrogenosome
... acetate, carbon dioxide and ATP by the combined actions of pyruvate:ferredoxin oxido-reductase, hydrogenase, acetate:succinate ... Superoxide dismutase, malate dehydrogenase (decarboxylating), ferredoxin, adenylate kinase and NADH:ferredoxin oxido-reductase ...
*  Rubottom oxidation
The Rubottom group found that lead(IV) acetate in DCM or benzene gave good yields of acyclic and cyclic α-hydroxy esters after ... synthesized various derivatives of phosphatidyl-D-myo-inositol to aid in the study of the various phosphatidylinositol 3-kinase ... In order to synthesize α-hydroxy esters, different oxidants are needed such as NaOCl (see above), lead(IV) acetate, or a ... acetate or hypofluorous acid-acetonitrile (HOF-ACN). However, these α-hydroxylations do not proceed via silyl enol ether ...
*  Creatinine
Creatine conversion to phosphocreatine is catalyzed by creatine kinase; spontaneous formation of creatinine occurs during the ... guanidino acetate, synthesized in the kidney from the amino acids arginine and glycine) by S-adenosyl methionine. It is then ...
*  Susan K. Gilmour
"Ornithine decarboxylase expression leads to translocation and activation of protein kinase CK2 in vivo". J Biol Chem. 272 (19 ... "Heterogeneity of ornithine decarboxylase expression in 12-O-tetradecanoylphorbol-13-acetate-treated mouse skin and in epidermal ... "Ornithine decarboxylase over-expression stimulates mitogen-activated protein kinase and anchorage-independent growth of human ... "Induction of ornithine decarboxylase by 12-O-tetradecanoylphorbol 13-acetate in hamster fibroblasts. Relationship between ...
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Cloning of Clostridium thermocellum acetate kinase (ack) and/or phosphotransacetylase (pta) genes in Escherichia coli by functional complementation of ack and/or pta mutants was complicated by an alternative acetate assimilation pathway involving acetyl-CoA synthetase (ACS). In addition to the problems encountered with the complementation approach, cloning of these genes was not readily achieved using heterologous probing with corresponding genes from Escherichia coli and Methanosarcina thermophila due to the lack of sufficient homology. The use of a PCR-based approach, on the other hand, yielded a specific C. Thermocellum gene fragment which showed significant sequence identity to the ack gene for which primers were designed. The subcloned ack fragment was then successfully used as a probe for the isolation of the corresponding gene and restriction analysis of that region.
Mukhopadhyay, S., Hasson, M.S., and Sanders, D.A. (2008) A continuous assay of acetate kinase activity: Measurement of inorganic phosphate release generated by hydroxylaminolysis of acetyl phosphate. Bioorg Chem 36, 65-69.. Brindley, M. A., L. Hughes, A. Ruiz, P. B. McCray, Jr., A. Sanchez, D. A. Sanders, and W. Maury (2007) Ebola virus glycoprotein 1: Identification of residues important for binding and postbinding events. J Virol 81, 7702-7709.. Alvarado, J., Ghosh, A., Janovitz, T., Jauregui, A., Hasson, M.S., and Sanders, D.A. (2006). Origin of Exopolyphosphatase Processivity: Fusion of an ASKHA Phosphotransferase and a Cyclic Nucleotide Phosphodiesterase Homolog. Structure. 14, 1263-1272.. Strang B. L., Takeuchi Y., Relander T., Richter J., Bailey R., Sanders D.A., Collins M.K., and Ikeda Y. (2005). Human immunodeficiency virus type 1 vectors with alphavirus envelope glycoproteins produced from stable packaging cells. J Virol. 79:1765-1771.. Sanders, D.A. and B. L. Wanner (2005). ...
Members of the class Asteroidea exhibit both asexual (regeneration and clonal) and sexual (gonochoric) means of reproduction. Life cycle: Embryos hatch into planktonic larvae and later metamorphose into pentamorous juveniles which develop into young sea stars with stubby arms (Ref. 833). ...
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Products derived from the central aerobic metabolic pathway in Escherichia coli often compete with the acetate-producing pathways poxB and ackA-pta for glucose. The production of isoamyl acetate from acetyl-CoA by ATF2, a yeast alcohol acetyltransferase, was a model system to demonstrate the beneficial effects of reducing aerobic acetate production. Ester production was 80% higher in the poxB, ackA-pta strain (0.18 mM) than found in the single ackA-pta mutant, when both overexpressed the PDH complex, panK, and ATF2. Anaerobically, succinate was produced alongside isoamyl acetate to maintain the proper redox balance between NADH and NAD+. The two compounds could be easily separated in an industrial setting because of the difference in their volatilities. An ldhA, adhE double mutant strain served as the control strain to test the effect of an additional ackA-pta mutation. The triple mutant produced 36% more ester (9.4 mM) and 7 times more succinate (45.5 mM) than the control ...
Figure 1. Metabolism of pyruvate to acetate in Clostridia. The phosphoroclastic conversion of pyruvate to acetate is mediated by several iron-containing proteins. Pyruvate-ferridoxin oxidoreductase oxidizes pyruvate, using ferridoxin (Fd) as the electron acceptor. Reduced ferridoxin is then re-oxidized by a third iron-containing protein, hydrogenase. Protons serve as the electron acceptor, and hydrogen gas is formed. Phospho-transacetylase and acetate kinase catalyze the final two steps, with acetate and one mole of ATP formed as end products. Importantly, both pyruvate-ferridoxin oxidoreductase and ferridoxin are able to form complexes with nitric oxide. This would effectively block this pathway, depriving cells of ATP, as well as increasing the concentration of pyruvate to potentially toxic levels. Adapted from White, 2000.. ...
Drugs and other reagents. Ganciclovir from Roche Laboratories was prepared (20 mmol/L) in PBS. Azidothymidine from Sigma and ganciclovir triphosphate (GCVTP) from TriLink Biotechnologies were prepared (10 mmol/L) in PBS and stored at −20°C. Azidothymidine triphosphate (AZTTP) from Calbiochem was prepared (10 mmol/L) in PBS and stored at −70°C. Venom phosphodiesterase was obtained from Worthington Biochemical Corp. Acetate kinase was obtained from Roche Applied Sciences.. Synthesis of ganciclovir monophosphate, ganciclovir diphosphate, azidothymidine monophosphate, and azidothymidine diphosphate. Venom phosphodiesterase was used to synthesize ganciclovir monophosphate (GCVMP) from GCVTP ( 26). The reaction mixture consisted of 0.01 mol/L Tris-HCl, 0.01 mol/L MgCl2 (pH 9.0), 1 unit venom phosphodiesterase, and 250 μmol/L GCVTP. The reaction proceeded for 6 h at 37°C and was inactivated by heating for 2 min at 95°C. Generation of GCVMP was confirmed by liquid chromatography/mass ...
PubMed comprises more than 30 million citations for biomedical literature from MEDLINE, life science journals, and online books. Citations may include links to full-text content from PubMed Central and publisher web sites.
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Accepted name: phosphate acetyltransferase. Reaction: acetyl-CoA + phosphate = CoA + acetyl phosphate. Other name(s): phosphotransacetylase; phosphoacylase; PTA. Systematic name: acetyl-CoA:phosphate acetyltransferase. Comments: Also acts with other short-chain acyl-CoAs.. Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9029-91-8. References: 1. Bergmeyer, H.U., Holz, G., Klotzsch, H. and Lang, G. Phosphotransacetylase aus Clostridium kluyveri. Züchtung des Bacteriums, Isolierung, Krystallisation und Eigenschaften des Enzyms. Biochem. Z. 338 (1963) 114-121.. 2. Stadtman, E.R. The purification and properties of phosphotransacetylase. J. Biol. Chem. 196 (1952) 527-534.. 3. Stadtman, E.R. Phosphotransacetylase from Clostridium kluyveri. Methods Enzymol. 1 (1955) 596-599.. ...
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Bouche, S. , Klauck, E. , Fischer, D. , Lucassen, M. , Jung, K. and Hengge-Aronis, R. (1998): Regulation of RssB-dependent proteolysis in Escherichia coli: a role for acetyl phosphate in a response regulator-controlled process , Molecular microbiology ...
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Geobacillus thermoglucosidasius is a Gram-positive, thermophilic bacterium capable of ethanologenic fermentation of both C5 and C6 sugars and may have possible use for commercial bioethanol production [Tang et al., 2009; Taylor et al. (2009) Trends Biotechnol 27(7): 398-405]. Little is known about the physiological changes that accompany a switch from aerobic (high redox) to microaerobic/fermentative (low redox) conditions in thermophilic organisms. The changes in the central metabolic pathways in response to a switch in redox potential were analyzed using quantitative real-time PCR and proteomics. During low redox (fermentative) states, results indicated that glycolysis was uniformly up-regulated, the Krebs (tricarboxylic acid or TCA) cycle non-uniformly down-regulated and that there was little to no change in the pentose phosphate pathway. Acetate accumulation was accounted for by strong down-regulation of the acetate CoA ligase gene (acs) in addition to up-regulation of the pta and ackA genes ...
Johnjeff Alvarado, Anita Ghosh, Tyler Janovitz, Andrew Jauregui, Miriam S. Hasson, and David Avram Sanders. The Escherichia coli Ppx protein is an exopolyphosphatase that degrades long-chain polyphosphates in a highly processive reaction. It also hydrolyzes the terminal 5 phosphate of the modified nucleotide guanosine 5 triphoshpate 3 diphosphate (pppGpp). The structure of Ppx has been determined to 1.9 angstrom resolution by X-ray crystallography. The exopolyphospatase is an ASKHA (Acetate and Sugar Kinases, Hsp70, Actin) phosphotransferase with an active site found in a clet between the two amino-terminal domains. Analysis of the active site indicates that among ASKHA phosphotranferases of known structure Ppx is the closest to the ecto-nucleoside triphosphate diphosphohydrolases. A third domain forms a six-helix claw that is similar to the catalytic core of the eukaryotic cyclic nucleotide phosphodiesterases. Most of the twenty-nine sulfate ions bound to the Ppx dimmer occupy sites where ...
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I cut an 8 1/2 x 11 to 4.25 x 11. Scored at 5.5, 7.25 and 9. The second and third score lines are were you are going to cut out your center panel. Save your bottom piece when you cut , you will reattach to the acetate panel. For the acetate panel I cut a 2.5" x 4.25". attach to inside of card bring in 1/2" to adhere to card. Take your bottom panel and reattach bringing in 1/2" to attache. Whala, you now have an acetate panel card ...
ethyl [(2E)-3-(4-cyanophenyl)-2-triazenyl]acetate - chemical structural formula, chemical names, chemical properties, synthesis references
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Syntrophus aciditrophicusis a model syntrophic bacterium that degrades key intermediates in anaerobic decomposition, such as benzoate, cyclohexane-1-carboxylate, and certain fatty acids, to acetate when grown with hydrogen-/formate-consuming microorganisms. ATP formation coupled to acetate production is the main source for energy conservation byS. aciditrophicus. However, the absence of homologs for phosphate acetyltransferase and acetate kinase in the genome ofS. aciditrophicusleaves it unclear as to how ATP is formed, as most fermentative bacteria rely on these two enzymes to synthesize ATP from acetyl coenzyme A (CoA) and phosphate. Here, we combine transcriptomic, proteomic, metabolite, and enzymatic approaches to show thatS. aciditrophicususes AMP-forming, acetyl-CoA synthetase (Acs1) for ATP synthesis from acetyl-CoA.acs1mRNA and Acs1 were abundant in transcriptomes and proteomes, respectively, ofS. aciditrophicusgrown in pure culture and coculture. Cell extracts ofS. aciditrophicushad low ...
... in a solution of 2 mM acetate, 2 mM phosphate and 3 nM acetyl phosphate. The standard state free energy of hydolysis of acetyl phosphate is /\G = -42.3 kJ/mol. ...
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1997-2006 Healthboard.com. Healthboard.com is a purely informational website, and should not be used as a substitute for professional legal, medical or technical advice. ...
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Metabolic Engineering of Thermophilic Bacillus licheniformis for Chiral Pure D-2,3-Butanediol Production Another BDO, 2,3-Butanediol, is also a potential fuel and a platform chemical. Organisms that natively produce the chemical are pathogenic and can only form the product with fermentations at 37°C. To transform the Bacillus licheniformis they had to use a protoplast fusion method. They were able to utilize xylose as a feedstock at 50°C to create 2,3-Butanediol. This will be helpful to utilize lignocellulose substrates as higher temperatures are helpful because of higher rates of degradation and fewer enzymes are need to be added [13]. Metabolic engineering of a thermophilic bacterium to produce ethanol at high yield In this paper the authors used Thermoanaerobacterium saccharolyticum and made knockouts in the genes for acetate kinase, phosphate acetyltransferase, and L-lactate dehydrogenase. Their strain was able to produce high yields of ethanol as the only measurable fermentation ...
A closer look at the active site of gamma-class carbonic anhydrases: high-resolution crystallographic studies of the carbonic anhydrase from Methanosarcina thermophila ...
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This is NOT an acetate, its just a bootleg that was pressed in 1975/76 i remeber seeing it around the record fairs of the time.you only have to look at the pictures to realise that,look at the outfits & the stage..the sleeve if i remeber right was just a photo copied sheet of coloured paper stuck to a card album cover.sorry to burst any bubbles ...
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... ; 3-Oxoadipate enol-lactone; 4,5-Dihydro-5-oxofuran-2-acetate; 5-Oxo-4,5-dihydrofuran-2-acetate; C03586 ...
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Microorganisms comprising modifications for producing pyruvate, ethanol, and other compounds. The microorganisms comprise modifications that reduce or ablate activity of one or more of pyruvate dehydrogenase, 2-oxoglutarate dehydrogenase, phosphate acetyltransferase, acetate kinase, pyruvate oxidase, lactate dehydrogenase, cytochrome terminal oxidase, succinate dehydrogenase, 6-phosphogluconate dehydrogenase, glutamate dehydrogenase, pyruvate formate lyase, pyruvate formate lyase activating enzyme, and isocitrate lyase. The microorganisms optionally comprise modifications that enhance expression or activity of pyruvate decarboxylase and alcohol dehydrogenase. The microorganisms are optionally evolved in defined media to enhance specific production of one or more compounds. Methods of producing compounds with the microorganisms are provided.
Looking for online definition of acetyl coenzyme A in the Medical Dictionary? acetyl coenzyme A explanation free. What is acetyl coenzyme A? Meaning of acetyl coenzyme A medical term. What does acetyl coenzyme A mean?
RN [1] RM 96134964 RT Characterization of the cdhD and cdhE genes encoding subunits of the corrinoid/iron-sulfur enzyme of the CO dehydrogenase complex from Methanosarcina thermophila. RA Maupin-Furlow J, Ferry JG RL J Bacteriol 1996 Jan;178(2):340-6 RN [2] RT Cloning and expression of the gene cluster encoding key proteins involved in acetyl-CoA synthesis in Clostridium thermoaceticum: CO dehydrogenase, the corrinoid/Fe-S protein, and methyltransferase. RA Roberts DL, James-Hagstrom JE, Garvin DK, Gorst CM, Runquist JA, Baur JR, Haase FC, Ragsdale SW RL Proc Natl Acad Sci U S A 1989 Jan;86(1):32-6 SE TIGR GA hmmls AL clustalw, belvu DR HAMAP; MF_01135; 9 of ...
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Probable acetate kinase elisa and antibody  Probable acetate kinase elisa and antibody
Recombinant Protein and Probable acetate kinase Antibody at MyBioSource. Custom ELISA Kit, Recombinant Protein and Antibody are ... Probable acetate kinase. Probable acetate kinase ELISA Kit. Probable acetate kinase Recombinant. Probable acetate kinase ... CATALYTIC ACTIVITY: ATP + acetate = ADP + acetyl phosphate. .. Below are the list of possible Probable acetate kinase products ... Serine-threonine-protein kinase ppk22 (ppk22), partial Recombinant Protein. • DNA-directed RNA polymerase III subunit RPC1 ( ...
more infohttps://www.mybiosource.com/protein_family.php?root=probable-acetate-kinase
Superiority of the PCR-based Approach for Cloning the Acetate Kinase G by G. Ozcengiz, J-H Kim et al.  "Superiority of the PCR-based Approach for Cloning the Acetate Kinase G" by G. Ozcengiz, J-H Kim et al.
... genes in Escherichia coli by functional complementation of ack and/or pta mutants was complicated by an alternative acetate ... Cloning of Clostridium thermocellum acetate kinase (ack) and/or phosphotransacetylase (pta) ... "Superiority of the PCR-based Approach for Cloning the Acetate Kinase Gene of Clostridium Thermocellum," Industrial Microbiology ... Cloning of Clostridium thermocellum acetate kinase (ack) and/or phosphotransacetylase (pta) genes in Escherichia coli by ...
more infohttp://scholarsmine.mst.edu/biosci_facwork/10/
Acetate kinase antibody | acris-antibodies.com  Acetate kinase antibody | acris-antibodies.com
ackA catalyzes the formation of acetyl phosphate from acetate and ATP. This protein can also catalyze the reverse reaction. ... Background of Acetate kinase antibody. ackA catalyzes the formation of acetyl phosphate from acetate and ATP. This protein can ...
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Acetate kinase - Wikipedia  Acetate kinase - Wikipedia
In molecular biology, acetate kinase (EC 2.7.2.1), which is predominantly found in micro-organisms, facilitates the production ... The growth of a bacterial mutant lacking acetate kinase has been shown to be inhibited by glucose, suggesting that the enzyme ... Grundy FJ, Waters DA, Allen SH, Henkin TM (November 1993). "Regulation of the Bacillus subtilis acetate kinase gene by CcpA". J ... Salmonella typhimurium propionate kinase (StTdcD) catalyzes reversible transfer of the γ-phosphate of ATP to propionate during ...
more infohttps://en.wikipedia.org/wiki/Acetate_kinase
Acetate kinase (diphosphate) - Wikipedia  Acetate kinase (diphosphate) - Wikipedia
Reeves RE, Guthrie JD (1975). "Acetate kinase (pyrophosphate). A fourth pyrophosphate-dependent kinase from Entamoeba ... an acetate kinase (diphosphate) (EC 2.7.2.12) is an enzyme that catalyzes the chemical reaction diphosphate + acetate ⇌ {\ ... The systematic name of this enzyme class is diphosphate:acetate phosphotransferase. This enzyme is also called pyrophosphate- ... the two substrates of this enzyme are diphosphate and acetate, whereas its two products are phosphate and acetyl phosphate. ...
more infohttps://en.wikipedia.org/wiki/Acetate_kinase_(diphosphate)
Urkinase: Structure of Acetate Kinase, a Member of the ASKHA Superfamily of Phosphotransferases | Journal of Bacteriology  Urkinase: Structure of Acetate Kinase, a Member of the ASKHA Superfamily of Phosphotransferases | Journal of Bacteriology
Structure of acetate kinase. The structure of the acetate kinase dimer (A) and a view with a 90° rotation around a horizontal ... Architecture of acetate kinase.The structure of M. thermophila acetate kinase was solved through the combination of two ... In acetate kinase, following aspartate-148, there is a helical insert (domain IC) which is unique to acetate kinase and which ... from the acetate kinases and have eliminated certain peripheral secondary-structure elements. Acetate kinase also has an ...
more infohttps://jb.asm.org/content/183/2/680
Isolation and Characterization of acetate kinase and phosphotransacetylase mutants of Escherichia coli and Salmonella...  Isolation and Characterization of acetate kinase and phosphotransacetylase mutants of Escherichia coli and Salmonella...
Mutations in the ack (acetate kinase) and pta (phosphotransacetylase) genes in Salmonella typhimurium were characterized and ... Isolation and Characterization of acetate kinase and phosphotransacetylase mutants of Escherichia coli and Salmonella ... Isolation and Characterization of acetate kinase and phosphotransacetylase mutants of Escherichia coli and Salmonella ... Isolation and Characterization of acetate kinase and phosphotransacetylase mutants of Escherichia coli and Salmonella ...
more infohttps://jb.asm.org/content/143/2/1081?ijkey=e3f83f9133903b318f1f86e6616da447f3f9e9c1&keytype2=tf_ipsecsha
Identification of essential arginines in the acetate kinase from Methanosarcina thermophila. - Semantic Scholar  Identification of essential arginines in the acetate kinase from Methanosarcina thermophila. - Semantic Scholar
The role of arginines in this acetate kinase was investigated. Five arginines (R91, R175, R241, R285, and R340) in the M. ... this approach has only recently become available for acetate kinase. The enzyme from Methanosarcina thermophila has been cloned ... thermophila enzyme were selected for individual replacement based on their high conservation among sequences of acetate kinase ... The K(m) value for acetate of the R91K variant increased greater than 10-fold relative to recombinant wild-type, suggesting an ...
more infohttps://www.semanticscholar.org/paper/Identification-of-essential-arginines-in-the-kinase-Singh-Wissmann-Miles/ee06bdd8bf0bf4e313bf8e177e32fb24611db563
Acetate/propionate kinase (IPR004372) | InterPro | EMBL-EBI  Acetate/propionate kinase (IPR004372) | InterPro | EMBL-EBI
Acetate/propionate kinase (IPR004372). Short name: Ac/propionate_kinase Family relationships *Aliphatic acid kinase, short- ... For example, Acetate kinase, which catalyses the reaction ATP + acetate = ADP + acetyl phosphate [PMID: 9484901]. ... GO:0016301 kinase activity GO:0016774 phosphotransferase activity, carboxyl group as acceptor ... Novel keto acid formate-lyase and propionate kinase enzymes are components of an anaerobic pathway in Escherichia coli that ...
more infohttp://www.ebi.ac.uk/interpro/entry/IPR004372?q=kinase
Acetic Acid Assay Kit Acetate Kinase Analyser Format - Megazyme  Acetic Acid Assay Kit Acetate Kinase Analyser Format - Megazyme
... test kit for specific measurement analysis of acetic acid acetate in beverages and food products. ... acetate kinase). (1) Acetic acid + ATP → acetyl-phosphate + ADP. (pyruvate kinase). (2) ADP + PEP → ATP + pyruvate. (D-lactate ... Current densities were 6.3 and 8.9 A m-2 on average at −0.4 and +0.1 V/SCE respectively, with acetate 10 mM. The catalytic ... Microbial bioanodes formed from a salt marsh inoculum under constant acetate feeding generated up to 85 A•m-2 in media ...
more infohttps://secure.megazyme.com/Acetic-Acid-Assay-Kit-Acetate-Kinase-Analyser-Format
Native Bacillus stearothermophilus Acetate Kinase(EC 2.7.2.1) - Creative Enzymes  Native Bacillus stearothermophilus Acetate Kinase(EC 2.7.2.1) - Creative Enzymes
... facilitates the production of acetyl-CoA by phosphorylating acetate in ... acetate kinase (EC 2.7.2.1), which is predominantly found in micro-organisms, ... Acetate kinase is used to phosphorylate acetate to acetyl phosphate. Acetate Kinase from Bacillus stearothermophilus has been ... Acetate kinase (phosphorylating); Acetic kinase; Acetokinase; EC 2.7.2.1; 9027-42-3; Acetate kinase ...
more infohttps://www.creative-enzymes.com/product/Native-Bacillus-Stearothermophilus-Acetate-Kinase_1034.html
Acetate and Sugar Kinases/Hepatic Stellate Cells 70/Actin - How is Acetate and Sugar Kinases/Hepatic Stellate Cells 70/Actin...  Acetate and Sugar Kinases/Hepatic Stellate Cells 70/Actin - How is Acetate and Sugar Kinases/Hepatic Stellate Cells 70/Actin...
Looking for abbreviations of ASKHA? It is Acetate and Sugar Kinases/Hepatic Stellate Cells 70/Actin. Acetate and Sugar Kinases/ ... Acetate and Sugar Kinases/Hepatic Stellate Cells 70/Actin. ... acetate. *Acetate and Sugar Kinases/Hepatic Stellate Cells 70/ ... Acetate and Sugar Kinases/Hepatic Stellate Cells 70/Actin - How is Acetate and Sugar Kinases/Hepatic Stellate Cells 70/Actin ... redirected from Acetate and Sugar Kinases/Hepatic Stellate Cells 70/Actin) Acronym. Definition. ...
more infohttps://acronyms.thefreedictionary.com/Acetate+and+Sugar+Kinases%2FHepatic+Stellate+Cells+70%2FActin
STAble: a novel approach to de novo assembly of RNA-seq data and its application in a metabolic model network based...  STAble: a novel approach to de novo assembly of RNA-seq data and its application in a metabolic model network based...
acetate kinase. ACS. Pyruvate Metabolism. acetyl-CoA synthetase. SERt2rpp. Transport. L-serine reversible transport via proton ...
more infohttps://link.springer.com/article/10.1186%2Fs12859-018-2174-6
Standardized assay medium to measure Lactococcus lactis enzyme activities while mimicking intracellular conditions.  - PubMed -...  Standardized assay medium to measure Lactococcus lactis enzyme activities while mimicking intracellular conditions. - PubMed -...
ACK, acetate kinase; G6PDH, glucose-6-phosphate dehydrogenase.. Standardized Assay Medium To Measure Lactococcus lactis Enzyme ...
more infohttps://www.ncbi.nlm.nih.gov/pubmed/22020503
A glycyl radical enzyme enables hydrogen sulfide production by the human intestinal bacterium Bilophila wadsworthia | PNAS  A glycyl radical enzyme enables hydrogen sulfide production by the human intestinal bacterium Bilophila wadsworthia | PNAS
... acetate kinase; Pta, phosphotransacetylase. (C) The gene clusters identified in this study. In B. wadsworthia, two separate ...
more infohttps://www.pnas.org/content/116/8/3171/tab-figures-data
A novel acyl-CoA beta-transaminase characterized from a metagenome.  - PubMed - NCBI  A novel acyl-CoA beta-transaminase characterized from a metagenome. - PubMed - NCBI
... acetate kinase (10); butyryl-CoA dehydrogenase (11); butyrate-acetoacetate CoA transferase (12). ... The latter compound is converted to acetate via acetyl-CoA and acetyl phosphate by acetoacetyl-CoA thiolase (8), phosphate ...
more infohttps://www.ncbi.nlm.nih.gov/pubmed/21826218?dopt=Abstract
Optimization of ʟ-ornithine production in recombinant Corynebacterium glutamicum S9114 by cg3035 overexpression and...  Optimization of ʟ-ornithine production in recombinant Corynebacterium glutamicum S9114 by cg3035 overexpression and...
... encodes pyruvate kinase; pta, encodes phosphotransacetylase; ackA, encodes acetate kinase; cat, encodes succinyl-CoA:acetate ... encodes gamma-glutamate kinase; cg3035, encodes N-acetylglutamate synthase; argB, encodes N-acetylglutamate kinase; argC, ... Blocking acetate biosynthesis by inserting a terminator into the upstream region of pta and cat, and its effect on ʟ-ornithine ... Despite altered acetate biosynthesis, the engineered strains SO5 and SO6 grow robustly in the fermentation medium, maintaining ...
more infohttps://link.springer.com/article/10.1186/s12934-018-0940-9
Stearothermophilus at Thomas Scientific  Stearothermophilus at Thomas Scientific
SIGMA Acetate Kinase from Bacillus stearothermophilus lyophilized powder, 400-1… MilliporeSigma. Synonym(s): ATP:Acetate ... Acetate Kinase Bacillus stearothermophilus MDL Number: MFCD00130330 Storage: 2-8°C ... SIGMA Pyruvate Kinase from Bacillus stearothermophilus Type VIII, lyophilized… MilliporeSigma. Synonym(s): ATP:pyruvate 2-O- ... SIGMA Fructose-6-phosphate Kinase from Bacillus stearothermophilus Type VII,… MilliporeSigma. Synonym(s): 6-Phosphofructokinase ...
more infohttps://www.thomassci.com/scientific-supplies/Stearothermophilus
Enzyme Explorer Assay Library | Sigma-Aldrich  Enzyme Explorer Assay Library | Sigma-Aldrich
Acetate Kinase Bacillus stearothermophilus 2.7.2.1. α-Acetolactate Decarboxylase 4.1.1.5. S-Acetyl Coenzyme A Synthetase 6.2. ...
more infohttps://www.sigmaaldrich.com/life-science/metabolomics/enzyme-explorer/learning-center/assay-library.html
pyruvate kinase Protocols and Video...  'pyruvate kinase' Protocols and Video...
Direct Detection of the Acetate-forming Activity of the Enzyme Acetate Kinase, Isolation of Translating Ribosomes Containing ... pyruvate kinase include Reconstitution of Basic Mitotic Spindles in Spherical Emulsion Droplets, Detergent-free Ultrafast ... An Integrated System to Remotely Trigger Intracellular Signal Transduction by Upconversion Nanoparticle-mediated Kinase ... Direct Detection of the Acetate-forming Activity of the Enzyme Acetate Kinase. Matthew L. Fowler1, Cheryl J. Ingram-Smith1, ...
more infohttps://www.jove.com/keyword/pyruvate+kinase
  • As we previously predicted, acetate kinase contains a core fold that is topologically identical to that of the ADP-binding domains of glycerol kinase, hexokinase, the 70-kDa heat shock cognate (Hsc70), and actin. (asm.org)
  • View all proteins of this organism that are known to be involved in the subpathway that synthesizes acetyl-CoA from acetate , the pathway acetyl-CoA biosynthesis and in Metabolic intermediate biosynthesis . (uniprot.org)
  • Acetate kinase is widespread in both anaerobic and aerobic microbes of the Bacteria and Archaea domains and a central player in a major link in the global carbon cycle, the anaerobic decomposition of organic matter to methane, in which it performs a dual role ( 14 ). (asm.org)
  • Subsequent steps involve the oxidation of such alcohols and fatty acids with carbon chain longer than C2 to acetate by syntrophic bacteria and their activity depends on the removal of hydrogen either by CO 2 or sulfate reduction. (frontiersin.org)
  • Bacterial responses to changes in environmental conditions are most commonly evoked through two-component regulatory systems consisting of a sensor kinase that autophosphorylates on a histidine residue and a response regulator ( 39 ). (asm.org)