Corynebacterium: A genus of asporogenous bacteria that is widely distributed in nature. Its organisms appear as straight to slightly curved rods and are known to be human and animal parasites and pathogens.Parabens: Methyl, propyl, butyl, and ethyl esters of p-hydroxybenzoic acid. They have been approved by the FDA as antimicrobial agents for foods and pharmaceuticals. (From Hawley's Condensed Chemical Dictionary, 11th ed, p872)NADP: Nicotinamide adenine dinucleotide phosphate. A coenzyme composed of ribosylnicotinamide 5'-phosphate (NMN) coupled by pyrophosphate linkage to the 5'-phosphate adenosine 2',5'-bisphosphate. It serves as an electron carrier in a number of reactions, being alternately oxidized (NADP+) and reduced (NADPH). (Dorland, 27th ed)FlavoproteinsCorynebacterium Infections: Infections with bacteria of the genus CORYNEBACTERIUM.Hydroxybenzoates: Benzoate derivatives substituted by one or more hydroxy groups in any position on the benzene ring.Corynebacterium glutamicum: A species of gram-positive, asporogenous, non-pathogenic, soil bacteria that produces GLUTAMIC ACID.Kinetics: The rate dynamics in chemical or physical systems.Gentisates: Salts and esters of gentisic acid.Corynebacterium diphtheriae: A species of gram-positive, asporogenous bacteria in which three cultural types are recognized. These types (gravis, intermedius, and mitis) were originally given in accordance with the clinical severity of the cases from which the different strains were most frequently isolated. This species is the causative agent of DIPHTHERIA.Attentional Blink: Temporary visual deficit or impaired visual processing occurring in a rapid serial visual presentation task. After a person identifies the first of two visual targets, the ability to detect the second target is impaired for the next few hundred milliseconds. This phenomenon is called attentional blink.Williams Syndrome: A disorder caused by hemizygous microdeletion of about 28 genes on chromosome 7q11.23, including the ELASTIN gene. Clinical manifestations include SUPRAVALVULAR AORTIC STENOSIS; MENTAL RETARDATION; elfin facies; impaired visuospatial constructive abilities; and transient HYPERCALCEMIA in infancy. The condition affects both sexes, with onset at birth or in early infancy.Cholestasis, Intrahepatic: Impairment of bile flow due to injury to the HEPATOCYTES; BILE CANALICULI; or the intrahepatic bile ducts (BILE DUCTS, INTRAHEPATIC).MississippiDrugs, Chinese Herbal: Chinese herbal or plant extracts which are used as drugs to treat diseases or promote general well-being. The concept does not include synthesized compounds manufactured in China.Receptor-Interacting Protein Serine-Threonine Kinase 2: A RIP serine-theonine kinase that contains a C-terminal caspase activation and recruitment domain. It can signal by associating with other CARD-signaling adaptor proteins and INITIATOR CASPASES that contain CARD domains within their N-terminal pro-domain region.Retroelements: Elements that are transcribed into RNA, reverse-transcribed into DNA and then inserted into a new site in the genome. Long terminal repeats (LTRs) similar to those from retroviruses are contained in retrotransposons and retrovirus-like elements. Retroposons, such as LONG INTERSPERSED NUCLEOTIDE ELEMENTS and SHORT INTERSPERSED NUCLEOTIDE ELEMENTS do not contain LTRs.Nobel PrizeGenetic Drift: The fluctuation of the ALLELE FREQUENCY from one generation to the next.History, 19th Century: Time period from 1801 through 1900 of the common era.Benzoic Acid: A fungistatic compound that is widely used as a food preservative. It is conjugated to GLYCINE in the liver and excreted as hippuric acid.Transition Temperature: The temperature at which a substance changes from one state or conformation of matter to another.Benzoates: Derivatives of BENZOIC ACID. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain the carboxybenzene structure.Nitrobenzoates: Benzoic acid or benzoic acid esters substituted with one or more nitro groups.Hippurates: Salts and esters of hippuric acid.Fermentation: Anaerobic degradation of GLUCOSE or other organic nutrients to gain energy in the form of ATP. End products vary depending on organisms, substrates, and enzymatic pathways. Common fermentation products include ETHANOL and LACTIC ACID.Molecular Weight: The sum of the weight of all the atoms in a molecule.Physicochemical Phenomena: The physical phenomena describing the structure and properties of atoms and molecules, and their reaction and interaction processes.Metalloporphyrins: Porphyrins which are combined with a metal ion. The metal is bound equally to all four nitrogen atoms of the pyrrole rings. They possess characteristic absorption spectra which can be utilized for identification or quantitative estimation of porphyrins and porphyrin-bound compounds.Chemistry: A basic science concerned with the composition, structure, and properties of matter; and the reactions that occur between substances and the associated energy exchange.4-Hydroxybenzoate-3-Monooxygenase: A flavoprotein that catalyzes the synthesis of protocatechuic acid from 4-hydroxybenzoate in the presence of molecular oxygen. EC 1.14.13.2.Pseudomonas fluorescens: A species of nonpathogenic fluorescent bacteria found in feces, sewage, soil, and water, and which liquefy gelatin.Mixed Function Oxygenases: Widely distributed enzymes that carry out oxidation-reduction reactions in which one atom of the oxygen molecule is incorporated into the organic substrate; the other oxygen atom is reduced and combined with hydrogen ions to form water. They are also known as monooxygenases or hydroxylases. These reactions require two substrates as reductants for each of the two oxygen atoms. There are different classes of monooxygenases depending on the type of hydrogen-providing cosubstrate (COENZYMES) required in the mixed-function oxidation.Flavin-Adenine Dinucleotide: A condensation product of riboflavin and adenosine diphosphate. The coenzyme of various aerobic dehydrogenases, e.g., D-amino acid oxidase and L-amino acid oxidase. (Lehninger, Principles of Biochemistry, 1982, p972)Flavins: Derivatives of the dimethylisoalloxazine (7,8-dimethylbenzo[g]pteridine-2,4(3H,10H)-dione) skeleton. Flavin derivatives serve an electron transfer function as ENZYME COFACTORS in FLAVOPROTEINS.Aminobenzoates: Derivatives of BENZOIC ACID that contain one or more amino groups attached to the benzene ring structure. Included under this heading are a broad variety of acid forms, salts, esters, and amides that include the aminobenzoate structure.ortho-Aminobenzoates: Benzoic acids, salts, or esters that contain an amino group attached to carbon number 2 or 6 of the benzene ring structure.4-Aminobenzoic Acid: An aminobenzoic acid isomer that combines with pteridine and GLUTAMIC ACID to form FOLIC ACID. The fact that 4-aminobenzoic acid absorbs light throughout the UVB range has also resulted in its use as an ingredient in SUNSCREENS.Rhodopseudomonas: A genus of gram-negative, rod-shaped, phototrophic bacteria found in aquatic environments. Internal photosynthetic membranes are present as lamellae underlying the cytoplasmic membrane.Biodegradation, Environmental: Elimination of ENVIRONMENTAL POLLUTANTS; PESTICIDES and other waste using living organisms, usually involving intervention of environmental or sanitation engineers.Anaerobiosis: The complete absence, or (loosely) the paucity, of gaseous or dissolved elemental oxygen in a given place or environment. (From Singleton & Sainsbury, Dictionary of Microbiology and Molecular Biology, 2d ed)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).Purchasing, Hospital: Hospital department responsible for the purchasing of supplies and equipment.Catechols: A group of 1,2-benzenediols that contain the general formula R-C6H5O2.Leasing, Property: Contractual arrangement between the lessor (owner) and the lessee in which the use of equipment or facilities is granted to the lessee for a period of time and at a specified rate.Economic Competition: The effort of two or more parties to secure the business of a third party by offering, usually under fair or equitable rules of business practice, the most favorable terms.Methanosarcina barkeri: A species of halophilic archaea whose organisms are nonmotile. Habitats include freshwater and marine mud, animal-waste lagoons, and the rumens of ungulates.Search Engine: Software used to locate data or information stored in machine-readable form locally or at a distance such as an INTERNET site.Orthomyxoviridae: A family of RNA viruses causing INFLUENZA and other diseases. There are five recognized genera: INFLUENZAVIRUS A; INFLUENZAVIRUS B; INFLUENZAVIRUS C; ISAVIRUS; and THOGOTOVIRUS.Information Storage and Retrieval: Organized activities related to the storage, location, search, and retrieval of information.Semiconductors: Materials that have a limited and usually variable electrical conductivity. They are particularly useful for the production of solid-state electronic devices.Aspergillus oryzae: An imperfect fungus present on most agricultural seeds and often responsible for the spoilage of seeds in bulk storage. It is also used in the production of fermented food or drink, especially in Japan.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.Software: Sequential operating programs and data which instruct the functioning of a digital computer.PubMed: A bibliographic database that includes MEDLINE as its primary subset. It is produced by the National Center for Biotechnology Information (NCBI), part of the NATIONAL LIBRARY OF MEDICINE. PubMed, which is searchable through NLM's Web site, also includes access to additional citations to selected life sciences journals not in MEDLINE, and links to other resources such as the full-text of articles at participating publishers' Web sites, NCBI's molecular biology databases, and PubMed Central.User-Computer Interface: The portion of an interactive computer program that issues messages to and receives commands from a user.
(1/76) Phe161 and Arg166 variants of p-hydroxybenzoate hydroxylase. Implications for NADPH recognition and structural stability.

Phe161 and Arg166 of p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens belong to a newly discovered sequence motif in flavoprotein hydroxylases with a putative dual function in FAD and NADPH binding [1]. To study their role in more detail, Phe161 and Arg166 were selectively changed by site-directed mutagenesis. F161A and F161G are catalytically competent enzymes having a rather poor affinity for NADPH. The catalytic properties of R166K are similar to those of the native enzyme. R166S and R166E show impaired NADPH binding and R166E has lost the ability to bind FAD. The crystal structure of substrate complexed F161A at 2.2 A is indistinguishable from the native enzyme, except for small changes at the site of mutation. The crystal structure of substrate complexed R166S at 2.0 A revealed that Arg166 is important for providing an intimate contact between the FAD binding domain and a long excursion of the substrate binding domain. It is proposed that this interaction is essential for structural stability and for the recognition of the pyrophosphate moiety of NADPH.  (+info)

(2/76) Modelling flavin and substrate substituent effects on the activation barrier and rate of oxygen transfer by p-hydroxybenzoate hydroxylase.

The simulation of enzymatic reactions, using computer models, is becoming a powerful tool in the most fundamental challenge in biochemistry: to relate the catalytic activity of enzymes to their structure. In the present study, various computed parameters were correlated with the natural logarithm of experimental rate constants for the hydroxylation of various substrate derivatives catalysed by wild-type para-hydroxybenzoate hydroxylase (PHBH) as well as for the hydroxylation of the native substrate (p-hydroxybenzoate) by PHBH reconstituted with a series of 8-substituted flavins. The following relative parameters have been calculated and tested: (a) energy barriers from combined quantum mechanical/molecular mechanical (QM/MM) (AM1/CHARMM) reaction pathway calculations, (b) gas-phase reaction enthalpies (AM1) and (c) differences between the HOMO and LUMO energies of the isolated substrate and cofactor molecules (AM1 and B3LYP/6-31+G(d)). The gas-phase approaches yielded good correlations, as long as similarly charged species are involved. The QM/MM approach resulted in a good correlation, even including differently charged species. This indicates that the QM/MM model accounts quite well for the solvation effects of the active site surroundings, which vary for differently charged species. The correlations obtained demonstrate quantitative structure activity relationships for an enzyme-catalysed reaction including, for the first time, substitutions on both substrate and cofactor.  (+info)

(3/76) Antioxidative galloyl esters as enzyme inhibitors of p-hydroxybenzoate hydroxylase.

Gallic acid and its esters were evaluated as enzyme inhibitors of recombinant p-hydroxybenzoate hydroxylase (PHBH), a NADPH-dependent flavin monooxygenase from Pseudomonas aeruginosa. n-Dodecyl gallate (DG) (IC(50)=16 microM) and (-)-epigallocatechin-3-O-gallate (EGCG) (IC(50)=16 microM), a major component of green tea polyphenols, showed the most potent inhibition, while product-like gallic acid did not inhibit the enzyme significantly (IC(50)>250 microM). Inhibition kinetics revealed that both DG and EGCG inhibited PHBH in a non-competitive manner (K(I)=18.1 and 14.0 microM, respectively). The enzyme inhibition was caused by specific binding of the antioxidative gallate to the enzyme, and by scavenging reactive oxygen species required for the monooxygenase reaction. Molecular modeling predicted that EGCG binds to the enzyme in the proximity of the FAD binding site via formation of three hydrogen bonds.  (+info)

(4/76) Comparing protein-ligand interactions in solution and single crystals by Raman spectroscopy.

By using a Raman microscope, we show that it is possible to probe the conformational states in protein crystals and crystal fragments under growth conditions (in hanging drops). The flavin cofactor in the enzyme para-hydroxybenzoate hydroxylase can assume two conformations: buried in the protein matrix ("in") or essentially solvent-exposed ("out"). By using Raman difference spectroscopy, we previously have identified characteristic flavin marker bands for the in and out conformers in the solution phase. Now we show that the flavin Raman bands can be used to probe these conformational states in crystals, permitting a comparison between solution and crystal environments. The in or out marker bands are similar for the respective conformers in the crystal and in solution; however, significant differences do exist, showing that the environments for the flavin's isoalloxazine ring are not identical in the two phases. Moreover, the Raman-band widths of the flavin modes are narrower for both in and out conformers in the crystals, indicating that the flavin exists in a more limited range of closely related conformational states in the crystal than in solution. In general, the ability to compare detailed Raman data for complexes in crystals and solution provides a means of bridging crystallographic and solution studies.  (+info)

(5/76) Regulation of the p-hydroxybenzoic acid hydroxylase gene (pobA) in plant-growth-promoting Pseudomonas putida WCS358.

The regulation of the p-hydroxybenzoate hydroxylase gene (pobA) of Pseudomonas putida WCS358 involved in the catabolism of p-hydroxybenzoic acid (PHB) to the central intermediate protocatechuate was studied. Protocatechuic acid (PCA) is then degraded via the beta-ketoadipate pathway to form tricarboxylic acid intermediates. In several Gram-negative bacteria pobA has been found genetically linked to a regulator called pobR which activates pobA expression in response to PHB. In this study the identification and characterization of the pobC-pobA locus of P. putida WCS358 is presented. The p-hydroxybenzoate hydroxylase (PobA) is highly identical to other identified PobA proteins, whereas the regulatory protein PobC did not display very high identity to other PobR proteins studied and belonged to the AraC family of regulatory proteins, hence it has been designated POBC: Using the pobA promoter transcriptionally fused to a promoterless lacZ gene it was observed that induction via PobC occurred very efficiently when PHB was present and to a lesser but still significant level also in the presence of PCA. This PobC-PCA response was genetically demonstrated by making use of pobC::Tn5 and pcaH::Tn5 mutants of strain WCS358 constructed in this study. In pobC mutants both the p-hydroxybenzoic and PCA response were not observed, whereas in the pcaH mutant, which lacks a functional protocatechuate 3,4-dioxygenase, the protocatechuic-acid-dependent pobA activation was still observed. Finally, the activation of pobA by PHB varied according to the concentration and it was observed that in the pcaR::Tn5 regulatory mutant of strain WCS358 the pobA promoter activity was reduced. PcaR is a regulator involved in the regulation of several loci of the beta-ketoadipate pathway, one of which is pcaK. It was postulated that the reduction of pobA activation in pcaR::Tn5 mutants was because there was no expression of the pcaK gene encoding the PHB transport protein resulting in lower levels of PHB present inside the cell.  (+info)

(6/76) A study of p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens. Improved purification, relative molecular mass, and amino acid composition.

The purification procedure for p-hydroxybenzoate hydroxylase has been modified by replacement of the DEAE-cellulose (DE-32) column in the original procedure by a Sephadex--Cibacron-blue affinity column. In this way the yield of enzyme could be improved from 16% to about 40--50%. Preparative gel chromatography indicated that the enzyme does not exist as a monomeric species as earlier believed but mainly as a dimer. Sodium dodecyl sulfate gel electrophoresis of purified enzyme revealed a minimum relative molecular mass (Mr) of 43000--45000. Analytical gel chromatography, sedimentation equilibrium and sedimentation velocity experiments showed that the enzyme exists in solution mainly as a dimer but also in higher-order quaternary structures (presumably tetramer and hexamer). Temperature dependence of the distribution of the oligomers suggests that the association is of hydrophobic nature. The amino acid composition of the enzyme is also presented. The enzyme contains no disulfide but five sulfhydryl groups. In the native state of the enzyme only one sulfhydryl group is accessible to N-ethylmaleimide or 5,5'-dithiobis(2-nitrobenzoic acid). The iso-electric point of the enzyme was found to be 5.8.  (+info)

(7/76) Protein and ligand dynamics in 4-hydroxybenzoate hydroxylase.

para-Hydroxybenzoate hydroxylase catalyzes a two-step reaction that demands precise control of solvent access to the catalytic site. The first step of the reaction, reduction of flavin by NADPH, requires access to solvent. The second step, oxygenation of reduced flavin to a flavin C4a-hydroperoxide that transfers the hydroxyl group to the substrate, requires that solvent be excluded to prevent breakdown of the hydroperoxide to oxidized flavin and hydrogen peroxide. These conflicting requirements are met by the coordination of multiple movements involving the protein, the two cofactors, and the substrate. Here, using the R220Q mutant form of para-hydroxybenzoate hydroxylase, we show that in the absence of substrate, the large beta alpha beta domain (residues 1-180) and the smaller sheet domain (residues 180-270) separate slightly, and the flavin swings out to a more exposed position to open an aqueous channel from the solvent to the protein interior. Substrate entry occurs by first binding at a surface site and then sliding into the protein interior. In our study of this mutant, the structure of the complex with pyridine nucleotide was obtained. This cofactor binds in an extended conformation at the enzyme surface in a groove that crosses the binding site of FAD. We postulate that for stereospecific reduction, the flavin swings to an out position and NADPH assumes a folded conformation that brings its nicotinamide moiety into close contact with the isoalloxazine moiety of the flavin. This work clearly shows how complex dynamics can play a central role in catalysis by enzymes.  (+info)

(8/76) Reaction of reduced flavins and flavoproteins with diphenyliodonium chloride.

The reaction of diphenyliodonium chloride with free reduced flavins has been studied by stopped flow spectrophotometry under anaerobic conditions, and second order rate constants were determined as a function of pH. The reactive flavin species was identified as the reduced anion, based on an observed reaction pK of 6.7. The product mixture was independent of the initial concentration of reactant and contained approximately 20% oxidized flavin. The results can be modeled quantitatively on a modification of the mechanism proposed by Tew (Tew, D. G. (1993) Biochemistry 32, 10209-10215). The composition of the complex reaction mixture has been analyzed, and four flavin-phenyl adducts with distinctive absorbance and fluorescence characteristics have been identified, involving substitution at the flavin C4a, N5, and C8 positions. Inactivation of flavoprotein enzymes by diphenyliodonium has also been studied, and several examples were found where inactivation occurs readily, despite noninvolvement of radical intermediates in their reaction mechanisms. It can be concluded that inactivation by phenyliodonium species is not a valid indicator of catalytic mechanism involving radical intermediates. One of the several factors determining inactivation is maintenance of the enzyme flavin in the reduced form in the steady state of catalysis, the other factors being redox potential and accessibility of the inhibitor to the flavin active site.  (+info)

*  4-hydroxybenzoate 3-monooxygenase
Howell LG, Spector T, Massey V (July 1972). "Purification and properties of p-hydroxybenzoate hydroxylase from Pseudomonas ... Spector T, Massey V (July 1972). "Studies on the effector specificity of p-hydroxybenzoate hydroxylase from Pseudomonas ... Hosokawa K, Stanier RY (May 1966). "Crystallization and properties of p-hydroxybenzoate hydroxylase from Pseudomonas putida". ... Spector T, Massey V (September 1972). "p-Hydroxybenzoate hydroxylase from Pseudomonas fluorescens. Evidence for an oxygenated ...
*  4-hydroxybenzoate 3-monooxygenase (NAD(P)H)
Fujii T, Kaneda T (1985). "Purification and properties of NADH/NADPH-dependent p-hydroxybenzoate hydroxylase from ... In enzymology, a 4-hydroxybenzoate 3-monooxygenase [NAD(P)H] (EC 1.14.13.33) is an enzyme that catalyzes the chemical reaction ... The systematic name of this enzyme class is 4-hydroxybenzoate,NAD(P)H:oxygen oxidoreductase (3-hydroxylating). Other names in ... Seibold B, Matthes M, Eppink MH, Lingens F, Van Berkel WJ, Muller R (1996). "4-Hydroxybenzoate hydroxylase from Pseudomonas sp ...
*  3-hydroxybenzoate 4-monooxygenase
55 (3): 888-96. doi:10.1016/0006-291X(73)91227-8. PMID 4148586. Premkumar R, Rao PV, Sreeleela NS, Vaidyanathan CS (1969). "m- ... In enzymology, a 3-hydroxybenzoate 4-monooxygenase (EC 1.14.13.23) is an enzyme that catalyzes the chemical reaction 3- ... hydroxybenzoate + NADPH + H+ + O2 ⇌ {\displaystyle \rightleftharpoons } 3,4-dihydroxybenzoate + NADP+ + H2O The 4 substrates of ... The systematic name of this enzyme class is 3-hydroxybenzoate,NADPH:oxygen oxidoreductase (4-hydroxylating). This enzyme is ...
*  Protocatechuic acid
The enzyme protocatechuate 3,4-dioxygenase uses 3,4-dihydroxybenzoate and O2 to produce 3-carboxy-cis,cis-muconate. Ethyl ... 43 (3): 474-477. doi:10.1042/bj0430474. PMC 1274717 . PMID 16748434. Pacheco-Palencia LA, Mertens-Talcott S, Talcott ST (Jun ... 2011 Mar;14(3):276-83 Antibacterial phenolics from Boswellia dalzielii. Alemika Taiwo E, Onawunmi Grace O and Olugbade, ... Lin HH, Chen JH, Huang CC, Wang CJ (June 2007). "Apoptotic effect of 3,4-dihydroxybenzoic acid on human gastric carcinoma cells ...
*  List of MeSH codes (D08)
... camphor 5-monooxygenase MeSH D08.811.682.690.708.170.500 --- alkane 1-monooxygenase MeSH D08.811.682.690.708.170.915 --- ... monophenol monooxygenase MeSH D08.811.682.690.708.170 --- cytochrome p-450 enzyme system MeSH D08.811.682.690.708.170.040 --- ... monooxygenase MeSH D08.811.682.690.708.392.468 --- Linoleoyl-CoA desaturase MeSH D08.811.682.690.708.392.625 --- stearoyl-coa ... camphor 5-monooxygenase MeSH D08.244.453.915 --- steroid hydroxylases MeSH D08.244.453.915.050 --- aldosterone synthase MeSH ...
*  3-hydroxybenzoate 6-monooxygenase
... m-hydroxybenzoate 6-hydroxylase, and 3-hydroxybenzoic acid-6-hydroxylase. This enzyme participates in benzoate degradation via ... In enzymology, a 3-hydroxybenzoate 6-monooxygenase (EC 1.14.13.24) is an enzyme that catalyzes the chemical reaction 3- ... hydroxybenzoate + NADH + H+ + O2 ⇌ {\displaystyle \rightleftharpoons } 2,5-dihydroxybenzoate + NAD+ + H2O The 4 substrates of ... 55 (3): 897-903. doi:10.1016/0006-291X(73)91228-X. PMID 4357436. Molecular and Cellular Biology portal. ...
*  Benzoate 4-monooxygenase
... and p-hydroxybenzoate hydroxylase. This enzyme participates in benzoate degradation via hydroxylation and benzoate degradation ... In enzymology, a benzoate 4-monooxygenase (EC 1.14.13.12) is an enzyme that catalyzes the chemical reaction benzoate + NADPH + ... The systematic name of this enzyme class is benzoate,NADPH:oxygen oxidoreductase (4-hydroxylating). Other names in common use ... It has 3 cofactors: iron, Tetrahydrobiopterin, and Tetrahydropteridine. Reddy CC, Vaidyanathan CS (1975). "Purification, ...
*  4-methoxybenzoate monooxygenase (O-demethylating)
In enzymology, a 4-methoxybenzoate monooxygenase (O-demethylating) (EC 1.14.99.15) is an enzyme that catalyzes the chemical ... 119 (3): 595-602. doi:10.1111/j.1432-1033.1981.tb05649.x. PMID 6273164. Molecular and Cellular Biology portal. ... Twilfer H, Bernhardt FH, Gersonde K (1981). "An electron-spin-resonance study on the redox-active centers of the 4- ... methoxybenzoate monooxygenase from Pseudomonas putida". Eur. J. Biochem. ...
*  4-Hydroxybenzoic acid
... is a popular antioxidant in part because of its low toxicity. The LD50 is 2200 mg/kg in mice (oral). 4- ... 4-Hydroxybenzoic acid is primarily known as the basis for the preparation of its esters, known as parabens, which are used as ... 4-Hydroxybenzoic acid has about one tenth the acidity of benzoic acid, having an acid dissociation constant Ka = 3.3 x 10−5 M ... 4-Hydroxybenzoic acid can be found naturally in Cocos nucifera. It is one of the main catechins metabolites found in humans ...
*  List of EC numbers (EC 1)
... alpha-pinene monooxygenase EC 1.14.13.156: 1,8-cineole 2-endo-monooxygenase EC 1.14.13.157: 1,8-cineole 2-exo-monooxygenase EC ... camphor 5-monooxygenase EC 1.14.15.2: camphor 1,2-monooxygenase EC 1.14.15.3: alkane 1-monooxygenase EC 1.14.15.4: steroid 11b- ... arginine 2-monooxygenase EC 1.13.12.2: lysine 2-monooxygenase EC 1.13.12.3: tryptophan 2-monooxygenase EC 1.13.12.4: lactate 2- ... steroid 17a-monooxygenase EC 1.14.99.10: steroid 21-monooxygenase EC 1.14.99.11: estradiol 6b-monooxygenase EC 1.14.99.12: 4- ...
*  4-hydroxybenzaldehyde dehydrogenase
Sircar, D.; Mitra, A. (2008). "Evidence for p-hydroxybenzoate formation involving enzymatic phenylpropanoid side-chain cleavage ... In enzymology, a 4-hydroxybenzaldehyde dehydrogenase (EC 1.2.1.64) is an enzyme that catalyzes the chemical reaction 4- ... 165 (4): 407-414. doi:10.1016/j.jplph.2007.05.005. PMID 17658659. Molecular and Cellular Biology portal. ... The systematic name of this enzyme class is 3-hydroxybenzaldehyde:NAD+ oxidoreductase. This enzyme is also called p- ...
*  Flavin adenine dinucleotide
p-Hydroxybenzoate hydroxylase (PHBH) catalyzes the oxygenation of p-hydroxybenzoate (pOHB) to 3,4-dihyroxybenzoate (3,4-diOHB ... Riboflavin FADH2 FMN FMO, flavin-containing monooxygenase NAD Teufel, Robin; Agarwal, Vinayak; Moore, Bradley S. (2016-04-01 ... 5 (3): 533-44. doi:10.1093/mp/sss020. PMID 22431563. Sivabalan S, Vedeswari CP, Jayachandran S, Koteeswaran D, Pravda C, Aruna ... Mechanisms 3 and 4 radical formation and hydride loss. Radical species contain unpaired electron atoms and are very chemically ...
*  Cytochrome P450 omega hydroxylase
... cytochrome P450 monooxygenases, and fatty acid monooxygenases, are a set of cytochrome P450-containing enzymes that catalyze ... Schreuder HA, van Berkel WJ, Eppink MH, Bunthol C (1999). "Phe161 and Arg166 variants of p-hydroxybenzoate hydroxylase. ... The CYP450 omega hydroxylases are accordingly better viewed as a subset of monooxygenases that have the ability to hydroxylate ... the monooxygenases are CYP450 enzymes that add a hydroxyl group to a wide range of xenobiotic (e.g. drugs, industrial toxins) ...
*  List of EC numbers (EC 2)
... tetraacyldisaccharide 4'-kinase EC 2.7.1.131: now EC 2.7.11.29 EC 2.7.1.132: now EC 2.7.11.28 EC 2.7.1.133: now with EC 2.7. ... UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase EC 2.3.1.203: UDP-4-amino-4,6-dideoxy-N-acetyl-alpha-D- ... precorrin-4 C11-methyltransferase EC 2.1.1.134: now with EC 2.1.1.129 EC 2.1.1.135: now EC 1.16.1.8 EC 2.1.1.136: chlorophenol ... hygromycin B 4-O-kinase EC 2.7.1.164: O-phosphoseryl-tRNASec kinase EC 2.7.1.165: glycerate 2-kinase EC 2.7.1.166: 3-deoxy-D- ...
4-hydroxybenzoate 3-monooxygenase - Wikipedia  4-hydroxybenzoate 3-monooxygenase - Wikipedia
Howell LG, Spector T, Massey V (July 1972). "Purification and properties of p-hydroxybenzoate hydroxylase from Pseudomonas ... Spector T, Massey V (July 1972). "Studies on the effector specificity of p-hydroxybenzoate hydroxylase from Pseudomonas ... Hosokawa K, Stanier RY (May 1966). "Crystallization and properties of p-hydroxybenzoate hydroxylase from Pseudomonas putida". ... Spector T, Massey V (September 1972). "p-Hydroxybenzoate hydroxylase from Pseudomonas fluorescens. Evidence for an oxygenated ...
more infohttps://en.wikipedia.org/wiki/4-hydroxybenzoate_3-monooxygenase
4-hydroxybenzoate 3-monooxygenase (NAD(P)H) - Wikipedia  4-hydroxybenzoate 3-monooxygenase (NAD(P)H) - Wikipedia
Fujii T, Kaneda T (1985). "Purification and properties of NADH/NADPH-dependent p-hydroxybenzoate hydroxylase from ... In enzymology, a 4-hydroxybenzoate 3-monooxygenase [NAD(P)H] (EC 1.14.13.33) is an enzyme that catalyzes the chemical reaction ... The systematic name of this enzyme class is 4-hydroxybenzoate,NAD(P)H:oxygen oxidoreductase (3-hydroxylating). Other names in ... Seibold B, Matthes M, Eppink MH, Lingens F, Van Berkel WJ, Muller R (1996). "4-Hydroxybenzoate hydroxylase from Pseudomonas sp ...
more infohttps://en.wikipedia.org/wiki/4-hydroxybenzoate_3-monooxygenase_(NAD(P)H)
Evolutionary divergence of pobA, the structural gene encoding p-hydroxybenzoate hydroxylase in an Acinetobacter calcoaceticus...  Evolutionary divergence of pobA, the structural gene encoding p-hydroxybenzoate hydroxylase in an Acinetobacter calcoaceticus...
... we have assembled a consensus sequence for nicotinamide-flavoprotein monooxygenases which differs from that of the ... The pobA gene encoding p-hydroxybenzoate hydroxylase (PobA) from Acinetobacter calcoaceticus has been developed as a genetic ... Evolutionary divergence of pobA, the structural gene encoding p-hydroxybenzoate hydroxylase in an Acinetobacter calcoaceticus ...
more infohttps://www.ncbi.nlm.nih.gov/pubmed/8449410?dopt=Abstract
KEGG ENZYME: 1.14.13.33  KEGG ENZYME: 1.14.13.33
Purification and properties of NADH/NADPH-dependent p-hydroxybenzoate hydroxylase from Corynebacterium cyclohexanicum. ... 4-hydroxybenzoate [CPD:C00156];. NADH [CPD:C00004];. NADPH [CPD:C00005];. H+ [CPD:C00080];. O2 [CPD:C00007]. ... Pathway (6) KEGG PATHWAY (6) Chemical substance (9) KEGG COMPOUND (9) Chemical reaction (3) KEGG REACTION (2) KEGG RCLASS (1) ... 3,4-dihydroxybenzoate [CPD:C00230];. NAD+ [CPD:C00003];. NADP+ [CPD:C00006];. H2O [CPD:C00001]. ...
more infohttp://www.genome.jp/dbget-bin/www_bget?ec:1.14.13.33
Construction and Optimization of a Heterologous Pathway for Protocatechuate Catabolism in Escherichia coli Enables...  Construction and Optimization of a Heterologous Pathway for Protocatechuate Catabolism in Escherichia coli Enables...
B) The monooxygenase gene, praI, is integrated in both JME7 (black) and JME50 (orange). The difference between JME7 and JME50 ... FIG 3 A mutation in the RBS of pcaH is sufficient for reproduction of the increase in the PCA-specific growth rate. (A) The ... A) The 3,4-cleavage pathway of PCA was transferred from P. putida KT2440 to E. coli, allowing growth with PCA as the sole ... F− Δ(araD-araB)567 lacZ4787(del)::rrnB-3 λ− rph-1 Δ(rhaD-rhaB)568 hsdR514. 33. ...
more infohttps://aem.asm.org/content/83/18/e01313-17/figures-only
KEGG PATHWAY: mrb00362  KEGG PATHWAY: mrb00362
Characterization of the 4-carboxy-4-hydroxy-2-oxoadipate aldolase gene and operon structure of the protocatechuate 4,5-cleavage ... 3-hydroxyacyl-CoA dehydrogenase NAD-binding protein [KO:K07516] [EC:1.1.1.35] ...
more infohttp://www.genome.jp/dbget-bin/www_bget?pathway+mrb00362
Structural comparison of p-hydroxybenzoate hydroxylase (PobA) from Pseudomonas putida with PobA from other Pseudomonas spp. And...  Structural comparison of p-hydroxybenzoate hydroxylase (PobA) from Pseudomonas putida with PobA from other Pseudomonas spp. And...
And other monooxygenases",. abstract = "The crystal structure is reported of p-hydroxybenzoate hydroxylase (PobA) from ... And other monooxygenases. / Lazar, John T.; Shuvalova, Ludmilla A; Rosas-Lemus, Monica; Kiryukhina, Olga; Satchell, Karla J. F. ... And other monooxygenases. John T. Lazar, Ludmilla A Shuvalova, Monica Rosas-Lemus, Olga Kiryukhina, Karla J. F. Satchell, ... And other monooxygenases. In: Acta Crystallographica Section F: Structural Biology Communications. 2019 ; Vol. 75. pp. 507-514. ...
more infohttps://www.scholars.northwestern.edu/en/publications/structural-comparison-of-p-hydroxybenzoate-hydroxylase-poba-from-
ENZYME entry 1.14.13.33  ENZYME entry 1.14.13.33
4-hydroxybenzoate + NAD(P)H + O(2) <=> 3,4-dihydroxybenzoate + NAD(P)(+) + H(2)O. ... The enzyme from Corynebacterium cyclohexanicum is highly specific for 4-hydroxybenzoate, but uses NADH and NADPH at ...
more infohttps://enzyme.expasy.org/EC/1.14.13.33
Construction and Optimization of a Heterologous Pathway for Protocatechuate Catabolism in Escherichia coli Enables...  Construction and Optimization of a Heterologous Pathway for Protocatechuate Catabolism in Escherichia coli Enables...
B) The monooxygenase gene, praI, is integrated in both JME7 (black) and JME50 (orange). The difference between JME7 and JME50 ... FIG 3 A mutation in the RBS of pcaH is sufficient for reproduction of the increase in the PCA-specific growth rate. (A) The ... A) The 3,4-cleavage pathway of PCA was transferred from P. putida KT2440 to E. coli, allowing growth with PCA as the sole ... PCA and 4-HB were dissolved in water at 5 g/liter, filter sterilized, and added at a final concentration of 1 g/liter. The pH ...
more infohttps://aem.asm.org/content/83/18/e01313-17
PBAL39 25205 protein (Pedobacter sp. BAL39) - STRING interaction network  PBAL39 25205 protein (Pedobacter sp. BAL39) - STRING interaction network
Monooxygenase possible 2-polyprenyl-6-methoxyphenol hydroxylase Probable protein kinase 0.504. PBAL39_21295. PBAL39_25205. ...
more infohttps://string-db.org/network/391596.PBAL39_25205
ENZYME: 1.14.13.  ENZYME: 1.14.13.
Orcinol 2-monooxygenase 1.14.13.7 Phenol 2-monooxygenase (NADPH) 1.14.13.8 Flavin-containing monooxygenase 1.14.13.9 Kynurenine ... 5-monooxygenase 1.14.13.224 Violacein synthase 1.14.13.225 F-actin monooxygenase 1.14.13.226 Acetone monooxygenase (methyl ... 20-monooxygenase 1.14.13.31 2-nitrophenol 2-monooxygenase 1.14.13.32 Albendazole monooxygenase (flavin-containing) 1.14.13.33 4 ... hydroxybenzoate 3-monooxygenase (NAD(P)H) 1.14.13.34 Leukotriene-E(4) 20-monooxygenase 1.14.13.35 Anthranilate 3-monooxygenase ...
more infohttps://enzyme.expasy.org/EC/1.14.13.-
Network Portal - Gene PA2132  Network Portal - Gene PA2132
Functional Annotations (4). Function. System. P pilus assembly protein, chaperone PapD. cog/ cog. protein binding. go/ ... type 4 fimbrial biogenesis protein FimT (NCBI). 80, 471. PA4589. PA4589. probable outer membrane protein precursor (NCBI). 246 ... POSITION A C G T 1 1.0 0.0 0.0 0.0 2 1.0 0.0 0.0 0.0 3 0.0 0.0 1.0 0.0 4 1.0 0.0 0.0 0.0 5 1.0 0.0 0.0 0.0 6 0.0 0.0 1.0 0.0 7 ... POSITION A C G T 1 1.0 0.0 0.0 0.0 2 0.0 0.75 0.0 0.25 3 0.0 0.0 0.0 1.0 4 0.0 0.0 1.0 0.0 5 0.25 0.5 0.0 0.25 6 0.0 0.5 0.0 ...
more infohttp://networks.systemsbiology.net/pae/gene/PA2132
Network Portal - Gene PA5382  Network Portal - Gene PA5382
alkane-1-monooxygenase (NCBI). 30, 192. PA2651. PA2651. hypothetical protein (NCBI). 30, 117. ... Functional Annotations (3). Function. System. Transcriptional regulator. cog/ cog. sequence-specific DNA binding transcription ... POSITION A C G T 1 1.0 0.0 0.0 0.0 2 1.0 0.0 0.0 0.0 3 0.0 0.0 0.0 1.0 4 1.0 0.0 0.0 0.0 5 0.0 0.0 1.0 0.0 6 0.0 0.0 0.0 1.0 7 ... POSITION A C G T 1 0.0 0.0 1.0 0.0 2 0.0 0.2 0.2 0.6 3 0.6 0.0 0.4 0.0 4 0.0 0.0 1.0 0.0 5 0.0 0.6 0.0 0.4 6 0.2 0.4 0.4 0.0 7 ...
more infohttp://networks.systemsbiology.net/pae/gene/PA5382
NWMN RS05395 - AureoWiki  NWMN RS05395 - AureoWiki
2,3-bisphosphoglycerate-independent phosphoglycerate mutase [1] (data from MRSA252). NWMN_RS04215. enolase [1] (data from ... FAD_binding_3; FAD binding domain (PF01494; HMM-score: 20.7) 3HCDH_N; 3-hydroxyacyl-CoA dehydrogenase, NAD binding domain ( ... J. Proteome Res.: 2011, 10(3);1139-50 [PubMed:21166474] [WorldCat.org] [DOI] (I p) ... Pyr_redox_3; Pyridine nucleotide-disulphide oxidoreductase (PF13738; HMM-score: 47.3) GIDA; Glucose inhibited division protein ...
more infohttp://aureowiki.med.uni-greifswald.de/NWMN_RS05395
NWMN 0962 - AureoWiki  NWMN 0962 - AureoWiki
glyceraldehyde 3-phosphate dehydrogenase 1 [1] (data from MRSA252). NWMN_1837. (gatB). aspartyl/glutamyl-tRNA amidotransferase ... FAD_binding_3; FAD binding domain (PF01494; HMM-score: 20.7) 3HCDH_N; 3-hydroxyacyl-CoA dehydrogenase, NAD binding domain ( ... J. Proteome Res.: 2011, 10(3);1139-50 [PubMed:21166474] [WorldCat.org] [DOI] (I p) ... Pyr_redox_3; Pyridine nucleotide-disulphide oxidoreductase (PF13738; HMM-score: 47.3) GIDA; Glucose inhibited division protein ...
more infohttp://aureowiki.med.uni-greifswald.de/NWMN_0962
pcaQ protein (Pseudomonas aeruginosa) - STRING interaction network  pcaQ protein (Pseudomonas aeruginosa) - STRING interaction network
P-hydroxybenzoate hydroxylase; Pbenz_hydroxyl- 4-hydroxybenzoate 3-monooxygenase. 0.402. pcaC. btr_6. DR97_3189. DR97_3206. ... decarb_PcaC- 4-carboxymuconolactone decarboxylase. Pca regulon regulatory protein; pcaR_pcaU- beta-ketoadipate pathway ... decarb_PcaC- 4-carboxymuconolactone decarboxylase. P-hydroxybenzoate hydroxylase; Pbenz_hydroxyl- 4-hydroxybenzoate 3- ...
more infohttps://string-db.org/network/287.DR97_3109
拳皇命运官方论坛:
	Benzoic acid | 65-85 - 拳皇命运图片  拳皇命运官方论坛: Benzoic acid | 65-85 - 拳皇命运图片
... or monophenol monooxygenase; carboxypeptidase A; diamine oxidase; xanthine oxidase; phenylalanine ammonia-lyase; creatine ... salicylate 1-monooxygenase; procollagen-lysine 5-dioxygenase; procollagen-proline 3-dioxygenase; procollagen-proline 4- ... Category 4. Warning. P264, P270, P301+P312, P330, P501. H315 Causes skin irritation. Skin corrosion/irritation. Category 2. ... Category 3. Warning. H336 May cause drowsiness or dizziness. Specific target organ toxicity,single exposure; Narcotic effects. ...
more infohttp://www.ljntc.icu/ChemicalProductProperty_EN_CB8698780.htm
RCSB PDB 









- 1PBC: CRYSTAL STRUCTURES OF WILD-TYPE P-HYDROXYBENZOATE HYDROXYLASE COMPLEXED WITH 4-AMINOBENZOATE, 2,4...  RCSB PDB - 1PBC: CRYSTAL STRUCTURES OF WILD-TYPE P-HYDROXYBENZOATE HYDROXYLASE COMPLEXED WITH 4-AMINOBENZOATE, 2,4...
... and 2-hydroxy-4-aminobenzoate and of the Tyr222Ala mutant complexed with 2-hydroxy-4-aminobenzoate. Evidence for a proton ... Crystal structures of wild-type p-hydroxybenzoate hydroxylase complexed with 4-aminobenzoate,2,4-dihydroxybenzoate, ... P-HYDROXYBENZOATE HYDROXYLASE (1PBC:A) * Monooxygenase Activity * Oxidoreductase Activity * 4 Hydroxybenzoate 3 Monooxygenase ... p-Hydroxybenzoate hydroxylase, PHBH Pseudomonas fluorescens [TaxId: 294] A174-275. d1pbca2. Alpha and beta proteins (a+b) FAD- ...
more infohttp://www.rcsb.org/pdb/explore/derivedData.do?structureId=1PBC
Springer Handbook of Enzymes | SpringerLink  Springer Handbook of Enzymes | SpringerLink
Estradiol 6β-monooxygenase Pages 308-309 * Androst-4-ene-3,17-dione monooxygenase ...
more infohttps://link.springer.com/book/10.1007/3-540-30439-8
Recent Developments in Using Advanced Sequencing Technologies for the Genomic Studies of Lignin and Cellulose Degrading...  Recent Developments in Using Advanced Sequencing Technologies for the Genomic Studies of Lignin and Cellulose Degrading...
YS-1r strain also codes for enzymes like phenol 2 monooxygenase, 4-hydroxybenzoate-3-monooxygenase, catechol-2,3-dioxygenase, ... of MBES04 also revealed information about the genes involved in the aromatic compound degradation such as p-hydroxybenzoate 3- ... monooxygenase and vanillate monooxygenase. MBES04 strain also showed three copies of the protocatechuate 4, 5-dioxygenase α and ... Enzymes involved in aromatic ring oxidation and cleavage such as phenol 2-monooxygenase, 4-hydroxybenzoate 3-monooxygenase, ...
more infohttp://www.ijbs.com/v12p0156.htm
  • The mechanism consists of the following general steps: (1) reduction of the flavin, (2) reaction of the flavin with O2, producing C4a-hydroperoxyflavin, and (3) binding and activation of the substrate, leading to product formation and release. (wikipedia.org)
  • In the presence of benzoate, 4-hydroxybenzoic acid, 3,4-dihydroxybenzoic acid or vanillic acid as growth substrates, the degradation of 21.5 %, 71.71 %, 14.7 5% and 8.16 % of naproxen was observed respectively. (pjmonline.org)
  • The active site limits potential substrates to substituted benzenes, namely 4-hydroxybenzoate (the native substrate), 2,4-dihydroxybenzoate, 4-mercaptobenzoate, and several halogenated aromatic compounds. (wikipedia.org)
  • B) The monooxygenase gene, praI , is integrated in both JME7 (black) and JME50 (orange). (asm.org)
  • Characterization of the 4-carboxy-4-hydroxy-2-oxoadipate aldolase gene and operon structure of the protocatechuate 4,5-cleavage pathway genes in Sphingomonas paucimobilis SYK-6. (genome.jp)
  • Additionally, the structure was compared with two enzymes from the broader class of oxygenases: 2-hydroxybiphenyl 3-monooxygenase (HbpA) from P. nitroreducens and 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase (MHPCO) from Mesorhizobium japonicum. (northwestern.edu)
  • The obtained results suggest that monooxygenase and hydroxyquinol 1,2-dioxygenase are the main enzymes in naproxen degradation by Planococcus sp. (pjmonline.org)
  • In enzymes with known three-dimensional (3-D) structures, there is a cavity suitable for covalent bonding of oxygen to the C4a-position. (schoolbag.info)
  • This pathway is identical in all apicomplexans including Toxoplasma gondii , Neospora caninum and Plasmodium falciparum and the enzymes missing in the genomes of all these species are oxo-acid lyase and 3-octaprenyl-4-hydroxybenzoate carboxy-lyase. (llamp.net)
  • This pathway is identical in Toxoplasma , Plasmodia , Cryptosporidia and Piroplasma species and two enzymes, oxo-acid lyase and 3-octaprenyl-4-hydroxybenzoate carboxy-lyase are missing in the genomes of all apicomplexan species. (llamp.net)
  • Indoleamine 2,3-dioxygenase, whose activity mediates T-cell activation and whose overexpression in cancer may prevent tumor rejection, is inhibited by halicloic acids A and B ( 15 , 16 ) [ 5 ]. (mdpi.com)
  • iii) Lignin is a complex organic biopolymer mainly present in plants in close association with carbohydrates like cellulose and hemicellulose, its main activity is to provide plants with structural stability, impermeability and resistance towards microbial attack [ 3 ]. (ijbs.com)
  • A) The 3,4-cleavage pathway of PCA was transferred from P. putida KT2440 to E. coli , allowing growth with PCA as the sole source of carbon and energy. (asm.org)
  • After optimization of the core pathway, we extended the pathway to enable catabolism of a second model compound, 4-hydroxybenzoate. (asm.org)
  • ii) Hemicellulose is a composite compound with a mixture of pentoses, hexoses and sugar acids [ 3 - 6 ]. (ijbs.com)
  • The toxicols ( 17 - 19 ) and shaagrockol C ( 22 ) inhibit the DNA polymerase function of HIV-1 reverse transcriptase [ 3 ]. (mdpi.com)
  • Akaterpin ( 25 ) inhibits hydrolysis of phosphatidylinositol by phospholipase C, a key step in eukaryotic signaling pathways by its production of diacylglycerol and inositol triphosphate [ 4 ]. (mdpi.com)