Hydrocarbons and methylotrophy /

Hydrocarbons and methylotrophy /

Εμφάνιση άλλων εκδόσεων (1)

This volume is the first comprehensive compilation of methods for the assay and purification of enzymes involved in the utilization of reduced one-carbon compounds and higher hydrocarbons. In the last decade there has been an explosion of interest in the organisms that grow on one-carbon compounds a...

Πλήρης περιγραφή

Λεπτομέρειες βιβλιογραφικής εγγραφής
Άλλοι συγγραφείς: Lidstrom, Mary E.
Μορφή: Ηλ. βιβλίο
Γλώσσα:English
Έκδοση: San Diego : Academic Press, ©1990.
Σειρά:Methods in enzymology ; v. 188.
Θέματα:
Hydrocarbons > Biodegradation.
Methylotrophic bacteria.
Hydrocarbons [MESH]
Methylation [MESH]
Biotechnology > Use of > Enzymes
Electronic books.
Διαθέσιμο Online:Full Text via HEAL-Link
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245 0 0 |a Hydrocarbons and methylotrophy /  |c edited by Mary E. Lidstrom. 
260 |a San Diego :  |b Academic Press,  |c ©1990. 
300 |a 1 online resource (xxxii, 504 pages) :  |b illustrations. 
336 |a text  |b txt  |2 rdacontent 
337 |a computer  |b c  |2 rdamedia 
338 |a online resource  |b cr  |2 rdacarrier 
490 1 |a Methods in enzymology ;  |v v. 188 
550 |a Made available through: Science Direct. 
504 |a Includes bibliographical references and indexes. 
505 0 0 |t Hydrocarbon monooxygenase system of Pseudomonas oleovorans /  |r Sheldon W. May, Andreas G. Katopodis and Mary E. Lidstrom --  |t Assay methods for long-chain alkane oxidation in Acinetobacter /  |r W.R. Finnerty and Mary E. Lidstrom --  |t Primary alcohol dehydrogenases from Acinetobacter /  |r W.R. Finnerty and Mary E. Lidstrom --  |t Aldehyde dehydrogenases from Acinetobacter /  |r W.R. Finnerty and Mary E. Lidstrom --  |t Propane-specific alcohol dehydrogenase from Rhodococcus rhodochrous PNKb 1 /  |r W. Ashraf, J.C. Murrell and Mary E. Lidstrom --  |t Cell-free assay methods for enzymes of propane utilization /  |r J.C. Murrell, W. Ashraf and Mary E. Lidstrom --  |t Quinoprotein alcohol dehydrogenase from Pseudomonas aeruginosa and quinohemoprotein alcohol dehydrogenase from Pseudomonas testosteroni /  |r B.W. Groen, Duine J.A. and Mary E. Lidstrom --  |t Toluene dioxygenase from Pseudomonas putida F1 /  |r Lawrence P. Wackett and Mary E. Lidstrom --  |t Naphthalene dioxygenase from Pseudomonas NCIB 9816 /  |r Burt D. Ensley, Billy E. Haigler and Mary E. Lidstrom --  |t Benzene dioxygenase from Pseudomonas putida ML2 (NCIB 12190) /  |r Philip J. Geary [and others] --  |t Phthalate dioxygenase /  |r Christopher J. Batie, David P. Ballou and Mary E. Lidstrom --  |t Cyclohexanone 1,2-monooxygenase from Acinetobacter NCIMB 9871 /  |r Peter W. Trudgill and Mary E. Lidstrom --  |t Cyclopentanone 1,2-monooxygenase from Pseudomonas NCIMB 9872 /  |r Peter W. Trudgill and Mary E. Lidstrom --  |t Protocatechuate 3,4-dioxygenase from Brevibacterium fuscum /  |r James W. Whittaker [and others] --  |t Protocatechuate 4,5-dioxygenase from Pseudomonas testosterone /  |r David M. Arciero [and others] --  |t Protocatechuate 2,3-dioxygenase from Bacillus macerans /  |r Sanford A. Wolgel, John D. Lipscomb and Mary E. Lidstrom --  |t Gentisate 1,2-dioxygenase from Pseudomonas acidovorans /  |r Mark R. Harpel, Lipscomb John D. and Mary E. Lidstrom --  |t Synthesis of 17O- or 18O-Enriched dihydroxy aromatic compounds /  |r Allen M. Orville [and others] --  |t Catechol 2,3-dioxygenases from Pseudomonas aeruginosa 2x /  |r I.A. Kataeva, Golovleva L.A. and Mary E. Lidstrom --  |t Catechol and chlorocatechol 1,2-Dioxygenases /  |r Ka-Leung Ngai [and others] --  |t Muconate cycloisemerase /  |r Richard B. Meagher [and others]. 
505 0 0 |t Muconolactone Isomerase /  |r Richard B. Meagher [and others] --  |t cis-1,2-Dihydroxycyclohexa-3,5-diene (NAD) oxidoreductase (cis-benzene dihydrodiol dehydrogenase) from Pseudomonas putida NCIB 12190 /  |r Jeremy R. Mason, Geary Philip J. and Mary E. Lidstrom --  |t Hydroxybenzoate hydroxylase /  |r Barrie Entsch and Mary E. Lidstrom --  |t Polycyclic aromatic hydrocarbon degradation by Mycobacterium /  |r Carl Ecerniglia, Heitkamp Michael A. and Mary E. Lidstrom --  |t Benzoate-CoA ligase from Rhodopseudomonas palustris /  |r Jane Gibson [and others] --  |t Lignin peroxidase from fungi: Phanerochaete chrysosporium /  |r T. Kent Kirk [and others] --  |t Long-chain alcohol dehydrogenase of Candida yeast /  |r Mitsuyoshi Ueda, Atsuo Tanaka and Mary E. Lidstrom --  |t Long-chain aldehyde dehydrogenase of candida yeast /  |r Mitsuyoshi Ueda, Atsuo Tanaka and Mary E. Lidstrom --  |t Soluble methane monooxygenase from Methylococcus capsulatus bath /  |r Simon J. Pilkington, Howard Dalton and Mary E. Lidstrom --  |t Methane monooxygenase from Methylosinus trichosporium OB3b /  |r Brian G. Fox [and others] --  |t Methanol dehydrogenase from Hyphomicrobium X /  |r J. Frank, Duine J.A. and Mary E. Lidstrom --  |t Methanol dehydrogenase from Methylobacterium extorquens AM1 /  |r Darren J. Day, Christopher Anthony and Mary E. Lidstrom --  |t Modifier protein for methanol dehydrogenase of methylotrophs /  |r Antony R. Long, Christopher Anthony and Mary E. Lidstrom. 
505 0 0 |t Methanol dehydrogenase from thermotolerant METHYLOTROPH Bacillus C1 /  |r N. Arfman, L. Dijkhuizen and Mary E. Lidstrom --  |t Methylamine oxidase from Arthrobacter P1 /  |r William S. McIntire and Mary E. Lidstrom --  |t Methylamine dehydrogenase from Thiobacillus versutus /  |r John E. van Wielink [and others] --  |t Methylamine dehydrogenases from methylotrophic bacteria /  |r Victor L. Davidson and Mary E. Lidstrom --  |t Methylamine dehydrogenase from methylobacillus flagellatum /  |r Michael Y. Kiriukhin [and others] --  |t Trimethylamine dehydrogenase from bacterium W3A1 /  |r William S. McIntire and Mary E. Lidstrom --  |t Isolation, preparation, and assay of pyrroloquinoline quinone /  |r R.A. Van Der Meer [and others] --  |t Blue copper proteins involved in methanol and methylamine oxidation /  |r Christopher Anthony and Mary E. Lidstrom --  |t Soluble Cytochromes c from methylomonas A4 /  |r Alan A. Dispirito and Mary E. Lidstrom --  |t Soluble cytochromes c of methanol-utilizing bacteria /  |r Darren J. Day, Christopher Anthony and Mary E. Lidstrom --  |t Cytochrome cL and cytochrome cH from Hyphomicrobium X /  |r J. Frank, Duine J.A. and Mary E. Lidstrom --  |t Electron-transfer flavoproteins from methylophilus methylotrophus and bacterium W3A1 /  |r Mazhar Husain and Mary E. Lidstrom --  |t Formaldehyde dehydrogenases from methylotrophs /  |r Margaret M. Attwood and Mary E. Lidstrom --  |t NAD-linked, factor-independent, and glutathione-independent aldehyde dehydrogenase from Hyphomicrobium X /  |r J.A. Duine and Mary E. Lidstrom --  |t Formate dehydrogenase from Methylosinus trichosporium OB3b /  |r David R. Jollie, John D. Lipscomb and Mary E. Lidstrom --  |t Glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase from Methylobacillus flagellatum /  |r Ludmila V. Kletsova [and others] --  |t Glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase from Arthrobacter globiformis /  |r A.P. Sokolov, Y.A. Trotsenko and Mary E. Lidstrom --  |t Glucose-6-phosphate dehydrogenase from Pseudomonas W6 /  |r Dietmar Miethe, Babel Wolfgang and Mary E. Lidstrom --  |t Citrate synthases from methylotrophs /  |r Gabriele Müller-Kraft, Wolfgang Babel and Mary E. Lidstrom. 
505 0 0 |t Dichloromethane dehalogenase from Hyphomicrobium DM2 /  |r Thomas Leisinger, Kohler-Staub Doris and Mary E. Lidstrom --  |t Assay of assimilatory enzymes in crude extracts of serine pathway methylotrophs /  |r Patricia M. Goodwin and Mary E. Lidstrom --  |t Serine hydroxymethyltransferases from Methylobacterium organophilum XX /  |r Mary E. Lidstrom and Mary E. Lidstrom --  |t Hydroxypyruvate reductase from Methylobacterium extorquens AM 1 /  |r Cinder Krema and Mary E. Lidstrom --  |t Malyl-CoA lyase from methylobacterium extorquens AM 1 /  |r A.J. Hacking, J.R. Quayle and Mary E. Lidstrom --  |t Synthesis of -4-Malyl coenzyme A /  |r Peggy J. Arps and Mary E. Lidstrom --  |t 3-Hexulose-6-phosphate synthase from thermotolerant methylotroph Bacillus C1 /  |r N. Arfman [and others] --  |t 3-Hexulose-6-phosphate synthase from mycobacterium gastri MB 19 /  |r Nobuo Kato and Mary E. Lidstrom --  |t 3-Hexulose-6-phosphate synthase from Acetobacter methanolicus MB58 /  |r Roland H. Müller, Wolfgang Babel and Mary E. Lidstrom --  |t Transaldolase Isoenzymes from Arthrobacter P1 /  |r P.R. Levering, L. Dijkhuizen and Mary E. Lidstrom --  |t Cytochemical staining methods for localization of key enzymes of methanol metabolism in hansenula polymorpha /  |r Marten Veenhuis, Ida J. Van Der Klei and Mary E. Lidstrom --  |t Alcohol Oxidase from Hansenula polymorpha MIE 4732 /  |r Ida J. van der Klei [and others] --  |t Amine oxidases from methylotrophic yeasts /  |r Peter J. Large, Geoffrey Whaywood and Mary E. Lidstrom --  |t Dihydroxyacetone synthase from Candida boidinii KD1 /  |r Leonid V. Bystrykh [and others] --  |t Triokinase from Candida boidinii KD1 /  |r Leonid V. Bystrykh [and others] --  |t Glycerone kinase from Candida methylica /  |r Klaus H. Hofmann, Wolfgang Babel and Mary E. Lidstrom --  |t Formaldehyde dehydrogenase from methylotrophic yeasts /  |r Nobuo Kato and Mary E. Lidstrom --  |t Formate dehydrogenase from methylotrophic yeasts /  |r Nobuo Kato and Mary E. Lidstrom --  |t Catalase from Candida boidinii 2201 /  |r Mitsuyoshi Ueda [and others]. 
520 |a This volume is the first comprehensive compilation of methods for the assay and purification of enzymes involved in the utilization of reduced one-carbon compounds and higher hydrocarbons. In the last decade there has been an explosion of interest in the organisms that grow on one-carbon compounds and in those that grow on higher hydrocarbons. This is due to the commercial interest in the unique enzymes involved in these specialty metabolic pathways and to a growing understanding of the important role these organisms play in carbon cycling in nature. More recent interest in the use of these organisms and their enzymes for detoxification of hazardous waste has once again put the spotlight on these unique microorganisms. This volume will prove to be a valuable source for researchers in academia, government, and industry alike. 
650 0 |a Hydrocarbons  |x Biodegradation. 
650 0 |a Methylotrophic bacteria. 
650 7 |a Hydrocarbons  |x Biodegradation.  |2 fast  |0 (OCoLC)fst00964830 
650 7 |a Methylotrophic bacteria.  |2 fast  |0 (OCoLC)fst01018781 
650 0 2 |a Hydrocarbons [MESH] 
650 0 2 |a Methylation [MESH] 
653 0 |a Biotechnology  |a Use of  |a Enzymes 
655 4 |a Electronic books. 
700 1 |a Lidstrom, Mary E. 
776 0 8 |i Print version:  |t Hydrocarbons and methylotrophy (print)  |w (DLC) 54009110  |w (OCoLC)24591346 
830 0 |a Methods in enzymology ;  |v v. 188. 
856 4 0 |u https://www.sciencedirect.com/science/bookseries/00766879/188  |z Full Text via HEAL-Link 

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