Purification and some properties of alcohol oxidase from alkane-grown Candida tropicalis
Alcohol oxidase was purified to homogeneity from membrane fractions obtained from alkane-grown Candida tropicalis. The enzyme appears to be a dimer of equal-sized subunits of Mr 70000. The purified enzyme is photosensitive and contains flavin-type material which is released by a combination of boili...
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| Veröffentlicht in: | Biochemical journal 1992-03, Vol.282 (2), p.325-331 |
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| container_title | Biochemical journal |
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| creator | Dickinson, F.M Wadforth, C |
| description | Alcohol oxidase was purified to homogeneity from membrane fractions obtained from alkane-grown Candida tropicalis. The enzyme appears to be a dimer of equal-sized subunits of Mr 70000. The purified enzyme is photosensitive and contains flavin-type material which is released by a combination of boiling and proteolytic digestion. The identity of the flavin material is not yet known, but it is not FMN, FAD or riboflavin. The enzyme is most active with dodecan-1-ol, but other long-chain alcohols are also attacked. The enzyme shows a weak, but significant activity towards long-chain aldehydes. Detailed kinetic studies with decan-1-o1 as substrate suggest a group-transfer (Ping-Pong)-type mechanism of catalysis. |
| doi_str_mv | 10.1042/bj2820325 |
| format | Article |
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The enzyme appears to be a dimer of equal-sized subunits of Mr 70000. The purified enzyme is photosensitive and contains flavin-type material which is released by a combination of boiling and proteolytic digestion. The identity of the flavin material is not yet known, but it is not FMN, FAD or riboflavin. The enzyme is most active with dodecan-1-ol, but other long-chain alcohols are also attacked. The enzyme shows a weak, but significant activity towards long-chain aldehydes. Detailed kinetic studies with decan-1-o1 as substrate suggest a group-transfer (Ping-Pong)-type mechanism of catalysis.</description><identifier>ISSN: 0264-6021</identifier><identifier>EISSN: 1470-8728</identifier><identifier>DOI: 10.1042/bj2820325</identifier><identifier>PMID: 1546949</identifier><language>eng</language><publisher>England</publisher><subject>alcohol oxidase ; alcohol oxidoreductases ; Alcohol Oxidoreductases - antagonists & inhibitors ; Alcohol Oxidoreductases - isolation & purification ; Alcohol Oxidoreductases - metabolism ; Alkanes ; Candida - enzymology ; Candida tropicalis ; Catalysis ; cell membranes ; characterization ; Chromatography, Gel ; Chromatography, Thin Layer ; Culture Media ; enzyme activity ; flavins ; Flavins - metabolism ; Kinetics ; microsomes ; Oxidation-Reduction ; Photochemistry ; photosensitivity ; physicochemical properties ; purification ; Spectrometry, Fluorescence ; Spectrophotometry, Ultraviolet ; Substrate Specificity</subject><ispartof>Biochemical journal, 1992-03, Vol.282 (2), p.325-331</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c491t-3713c5008b2e87c9ebb57d8f3198f450ba4e7039d693799a64fbf99a33aec6ed3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1130782/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1130782/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,27924,27925,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1546949$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Dickinson, F.M</creatorcontrib><creatorcontrib>Wadforth, C</creatorcontrib><title>Purification and some properties of alcohol oxidase from alkane-grown Candida tropicalis</title><title>Biochemical journal</title><addtitle>Biochem J</addtitle><description>Alcohol oxidase was purified to homogeneity from membrane fractions obtained from alkane-grown Candida tropicalis. The enzyme appears to be a dimer of equal-sized subunits of Mr 70000. The purified enzyme is photosensitive and contains flavin-type material which is released by a combination of boiling and proteolytic digestion. The identity of the flavin material is not yet known, but it is not FMN, FAD or riboflavin. The enzyme is most active with dodecan-1-ol, but other long-chain alcohols are also attacked. The enzyme shows a weak, but significant activity towards long-chain aldehydes. Detailed kinetic studies with decan-1-o1 as substrate suggest a group-transfer (Ping-Pong)-type mechanism of catalysis.</description><subject>alcohol oxidase</subject><subject>alcohol oxidoreductases</subject><subject>Alcohol Oxidoreductases - antagonists & inhibitors</subject><subject>Alcohol Oxidoreductases - isolation & purification</subject><subject>Alcohol Oxidoreductases - metabolism</subject><subject>Alkanes</subject><subject>Candida - enzymology</subject><subject>Candida tropicalis</subject><subject>Catalysis</subject><subject>cell membranes</subject><subject>characterization</subject><subject>Chromatography, Gel</subject><subject>Chromatography, Thin Layer</subject><subject>Culture Media</subject><subject>enzyme activity</subject><subject>flavins</subject><subject>Flavins - metabolism</subject><subject>Kinetics</subject><subject>microsomes</subject><subject>Oxidation-Reduction</subject><subject>Photochemistry</subject><subject>photosensitivity</subject><subject>physicochemical properties</subject><subject>purification</subject><subject>Spectrometry, Fluorescence</subject><subject>Spectrophotometry, Ultraviolet</subject><subject>Substrate Specificity</subject><issn>0264-6021</issn><issn>1470-8728</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkd1LHDEUxUNp2a62D_4B0jwJPozefMwkeSnI4hcICu1C30Imk6yxM5NtMqv2vzeyovapTxdyfvdwcg9CewSOCHB63N5RSYHR-gOaEy6gkoLKj2gOtOFVA5R8Rjs53wEQDhxmaEZq3iiu5ujXzSYFH6yZQhyxGTuc4-DwOsW1S1NwGUePTW_jbexxfAydyQ77FIfy-NuMrlql-DDiRdksGp7KXjHrQ_6CPnnTZ_f1Ze6i5dnpz8VFdXV9frk4uaosV2SqmCDM1gCypU4Kq1zb1qKTnhElPa-hNdwJYKprFBNKmYb71pfJmHG2cR3bRd-3vutNO7jOunFKptfrFAaT_upogv5XGcOtXsV7TQgDIWkxOHgxSPHPxuVJDyFb1_fld3GTdbkkV4LJ_4KkKcdt6DN4uAVtijkn51_TENDPfenXvgq7_z7-G7ktqOjftro3UZtVClkvf1Ao2YmoQQFjT4gnmyU</recordid><startdate>19920301</startdate><enddate>19920301</enddate><creator>Dickinson, F.M</creator><creator>Wadforth, C</creator><scope>FBQ</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M7N</scope><scope>M81</scope><scope>P64</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19920301</creationdate><title>Purification and some properties of alcohol oxidase from alkane-grown Candida tropicalis</title><author>Dickinson, F.M ; Wadforth, C</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c491t-3713c5008b2e87c9ebb57d8f3198f450ba4e7039d693799a64fbf99a33aec6ed3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>alcohol oxidase</topic><topic>alcohol oxidoreductases</topic><topic>Alcohol Oxidoreductases - antagonists & inhibitors</topic><topic>Alcohol Oxidoreductases - isolation & purification</topic><topic>Alcohol Oxidoreductases - metabolism</topic><topic>Alkanes</topic><topic>Candida - enzymology</topic><topic>Candida tropicalis</topic><topic>Catalysis</topic><topic>cell membranes</topic><topic>characterization</topic><topic>Chromatography, Gel</topic><topic>Chromatography, Thin Layer</topic><topic>Culture Media</topic><topic>enzyme activity</topic><topic>flavins</topic><topic>Flavins - metabolism</topic><topic>Kinetics</topic><topic>microsomes</topic><topic>Oxidation-Reduction</topic><topic>Photochemistry</topic><topic>photosensitivity</topic><topic>physicochemical properties</topic><topic>purification</topic><topic>Spectrometry, Fluorescence</topic><topic>Spectrophotometry, Ultraviolet</topic><topic>Substrate Specificity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Dickinson, F.M</creatorcontrib><creatorcontrib>Wadforth, C</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biochemistry Abstracts 3</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Biochemical journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Dickinson, F.M</au><au>Wadforth, C</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification and some properties of alcohol oxidase from alkane-grown Candida tropicalis</atitle><jtitle>Biochemical journal</jtitle><addtitle>Biochem J</addtitle><date>1992-03-01</date><risdate>1992</risdate><volume>282</volume><issue>2</issue><spage>325</spage><epage>331</epage><pages>325-331</pages><issn>0264-6021</issn><eissn>1470-8728</eissn><abstract>Alcohol oxidase was purified to homogeneity from membrane fractions obtained from alkane-grown Candida tropicalis. The enzyme appears to be a dimer of equal-sized subunits of Mr 70000. The purified enzyme is photosensitive and contains flavin-type material which is released by a combination of boiling and proteolytic digestion. The identity of the flavin material is not yet known, but it is not FMN, FAD or riboflavin. The enzyme is most active with dodecan-1-ol, but other long-chain alcohols are also attacked. The enzyme shows a weak, but significant activity towards long-chain aldehydes. Detailed kinetic studies with decan-1-o1 as substrate suggest a group-transfer (Ping-Pong)-type mechanism of catalysis.</abstract><cop>England</cop><pmid>1546949</pmid><doi>10.1042/bj2820325</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Biochemical journal, 1992-03, Vol.282 (2), p.325-331 |
| issn | 0264-6021 1470-8728 |
| language | eng |
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| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; PubMed Central; Alma/SFX Local Collection |
| subjects | alcohol oxidase alcohol oxidoreductases Alcohol Oxidoreductases - antagonists & inhibitors Alcohol Oxidoreductases - isolation & purification Alcohol Oxidoreductases - metabolism Alkanes Candida - enzymology Candida tropicalis Catalysis cell membranes characterization Chromatography, Gel Chromatography, Thin Layer Culture Media enzyme activity flavins Flavins - metabolism Kinetics microsomes Oxidation-Reduction Photochemistry photosensitivity physicochemical properties purification Spectrometry, Fluorescence Spectrophotometry, Ultraviolet Substrate Specificity |
| title | Purification and some properties of alcohol oxidase from alkane-grown Candida tropicalis |
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