On the enzymatic hydrolysis of FAD in spinach leaves
The enzyme destorying FAD in spinach leaves were investigated. 1. FAD was hydrolyzed by nucleotide pyrophosphatase in spinach leaves. 2. The activity of the enzyme was considerably high in comparison with that of FAD pyrophosphorylase in green leaves. 3. The pH optimum was around 5.0 and the activit...
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| Veröffentlicht in: | Journal of vitaminology 1970/03/10, Vol.16(1), pp.31-38 |
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| container_title | Journal of vitaminology |
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| creator | Mistuda, H Tsuge, H Tomozawa, Y Kawai, F |
| description | The enzyme destorying FAD in spinach leaves were investigated. 1. FAD was hydrolyzed by nucleotide pyrophosphatase in spinach leaves. 2. The activity of the enzyme was considerably high in comparison with that of FAD pyrophosphorylase in green leaves. 3. The pH optimum was around 5.0 and the activity decreased remarkably at about pH 7.0, which was the pH optimum of FAD pyrophosphorylase. 4. The optimum temperature for the enzyme activity was approximately 60° when the reaction mixture was incubated for 20 min. 5. The Km value was 4×10-5M and the relative substrate specificity of the enzyme for FAD was higher than those for NAD, NADP and ADP. 6. The hydrolysis of FAD was strongly inhibited by ATP, ADP, NAD and NADP occurring in green leaves about 10 times as much as flavins in concentration. 7. No hydrolysis of the tightly bound FAD with the apoprotein of glucose oxidase was recognized. |
| doi_str_mv | 10.5925/jnsv1954.16.31 |
| format | Article |
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FAD was hydrolyzed by nucleotide pyrophosphatase in spinach leaves. 2. The activity of the enzyme was considerably high in comparison with that of FAD pyrophosphorylase in green leaves. 3. The pH optimum was around 5.0 and the activity decreased remarkably at about pH 7.0, which was the pH optimum of FAD pyrophosphorylase. 4. The optimum temperature for the enzyme activity was approximately 60° when the reaction mixture was incubated for 20 min. 5. The Km value was 4×10-5M and the relative substrate specificity of the enzyme for FAD was higher than those for NAD, NADP and ADP. 6. The hydrolysis of FAD was strongly inhibited by ATP, ADP, NAD and NADP occurring in green leaves about 10 times as much as flavins in concentration. 7. No hydrolysis of the tightly bound FAD with the apoprotein of glucose oxidase was recognized.</description><identifier>ISSN: 0022-5398</identifier><identifier>DOI: 10.5925/jnsv1954.16.31</identifier><identifier>PMID: 4393601</identifier><language>eng</language><publisher>Japan: THE VITAMIN SOCIETY OF JAPAN</publisher><subject>Adenosine Triphosphate ; botany ; Chemical Phenomena ; Chemistry ; Chromatography ; Flavin-Adenine Dinucleotide ; Glucose Oxidase ; Hydrogen-Ion Concentration ; Metals ; NAD ; NADP ; Nucleosides - antagonists & inhibitors ; Plant Science and Plant Products ; plants ; Pyrophosphatases - analysis ; Temperature ; Vegetables - analysis</subject><ispartof>THE JOURNAL OF VITAMINOLOGY, 1970/03/10, Vol.16(1), pp.31-38</ispartof><rights>THE VITAMIN SOCIETY OF JAPAN</rights><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c537t-73a55488598bb0d3f4ab2375a55b7b126ae3717e47f406d222e1b374ff9d8f0d3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,1883,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/4393601$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Mistuda, H</creatorcontrib><creatorcontrib>Tsuge, H</creatorcontrib><creatorcontrib>Tomozawa, Y</creatorcontrib><creatorcontrib>Kawai, F</creatorcontrib><title>On the enzymatic hydrolysis of FAD in spinach leaves</title><title>Journal of vitaminology</title><addtitle>J. Vitaminol</addtitle><description>The enzyme destorying FAD in spinach leaves were investigated. 1. FAD was hydrolyzed by nucleotide pyrophosphatase in spinach leaves. 2. The activity of the enzyme was considerably high in comparison with that of FAD pyrophosphorylase in green leaves. 3. The pH optimum was around 5.0 and the activity decreased remarkably at about pH 7.0, which was the pH optimum of FAD pyrophosphorylase. 4. The optimum temperature for the enzyme activity was approximately 60° when the reaction mixture was incubated for 20 min. 5. The Km value was 4×10-5M and the relative substrate specificity of the enzyme for FAD was higher than those for NAD, NADP and ADP. 6. The hydrolysis of FAD was strongly inhibited by ATP, ADP, NAD and NADP occurring in green leaves about 10 times as much as flavins in concentration. 7. No hydrolysis of the tightly bound FAD with the apoprotein of glucose oxidase was recognized.</description><subject>Adenosine Triphosphate</subject><subject>botany</subject><subject>Chemical Phenomena</subject><subject>Chemistry</subject><subject>Chromatography</subject><subject>Flavin-Adenine Dinucleotide</subject><subject>Glucose Oxidase</subject><subject>Hydrogen-Ion Concentration</subject><subject>Metals</subject><subject>NAD</subject><subject>NADP</subject><subject>Nucleosides - antagonists & inhibitors</subject><subject>Plant Science and Plant Products</subject><subject>plants</subject><subject>Pyrophosphatases - analysis</subject><subject>Temperature</subject><subject>Vegetables - analysis</subject><issn>0022-5398</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1970</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVkDtPwzAUhT2ASlW6siE8sSX47WSsCgWkSh2gs-UkdpMqj2KnlcKvxyilEne4V7rnnG84ANxhFPOU8Kd960845SzGIqb4CkwRIiTiNE1uwNz7PQojiGSYTMCE0ZQKhKeAbVrYlwaa9ntodF_lsBwK19WDrzzsLFwtnmHVQn-oWp2XsDb6ZPwtuLa69mZ-vjOwXb18Lt-i9eb1fblYRzmnso8k1ZyzJOFpkmWooJbpjFDJwzeTGSZCGyqxNExahkRBCDE4o5JZmxaJDYEZeBy5B9d9HY3vVVP53NS1bk139CphQghJRDDGozF3nffOWHVwVaPdoDBSv-2ov3YUForiELg_k49ZY4qL_dxL0Jejvve93pmLrl2oqDb_cHhcFF_UvNROmTZQHkaK1Z3SO1d5tf0gAY8w5gnlgv4AIFiB-w</recordid><startdate>19700101</startdate><enddate>19700101</enddate><creator>Mistuda, H</creator><creator>Tsuge, H</creator><creator>Tomozawa, Y</creator><creator>Kawai, F</creator><general>THE VITAMIN SOCIETY OF JAPAN</general><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>7X8</scope></search><sort><creationdate>19700101</creationdate><title>On the enzymatic hydrolysis of FAD in spinach leaves</title><author>Mistuda, H ; Tsuge, H ; Tomozawa, Y ; Kawai, F</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c537t-73a55488598bb0d3f4ab2375a55b7b126ae3717e47f406d222e1b374ff9d8f0d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1970</creationdate><topic>Adenosine Triphosphate</topic><topic>botany</topic><topic>Chemical Phenomena</topic><topic>Chemistry</topic><topic>Chromatography</topic><topic>Flavin-Adenine Dinucleotide</topic><topic>Glucose Oxidase</topic><topic>Hydrogen-Ion Concentration</topic><topic>Metals</topic><topic>NAD</topic><topic>NADP</topic><topic>Nucleosides - antagonists & inhibitors</topic><topic>Plant Science and Plant Products</topic><topic>plants</topic><topic>Pyrophosphatases - analysis</topic><topic>Temperature</topic><topic>Vegetables - analysis</topic><toplevel>online_resources</toplevel><creatorcontrib>Mistuda, H</creatorcontrib><creatorcontrib>Tsuge, H</creatorcontrib><creatorcontrib>Tomozawa, Y</creatorcontrib><creatorcontrib>Kawai, F</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>MEDLINE - Academic</collection><jtitle>Journal of vitaminology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Mistuda, H</au><au>Tsuge, H</au><au>Tomozawa, Y</au><au>Kawai, F</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>On the enzymatic hydrolysis of FAD in spinach leaves</atitle><jtitle>Journal of vitaminology</jtitle><addtitle>J. Vitaminol</addtitle><date>1970-01-01</date><risdate>1970</risdate><volume>16</volume><issue>1</issue><spage>31</spage><epage>38</epage><pages>31-38</pages><issn>0022-5398</issn><abstract>The enzyme destorying FAD in spinach leaves were investigated. 1. FAD was hydrolyzed by nucleotide pyrophosphatase in spinach leaves. 2. The activity of the enzyme was considerably high in comparison with that of FAD pyrophosphorylase in green leaves. 3. The pH optimum was around 5.0 and the activity decreased remarkably at about pH 7.0, which was the pH optimum of FAD pyrophosphorylase. 4. The optimum temperature for the enzyme activity was approximately 60° when the reaction mixture was incubated for 20 min. 5. The Km value was 4×10-5M and the relative substrate specificity of the enzyme for FAD was higher than those for NAD, NADP and ADP. 6. The hydrolysis of FAD was strongly inhibited by ATP, ADP, NAD and NADP occurring in green leaves about 10 times as much as flavins in concentration. 7. No hydrolysis of the tightly bound FAD with the apoprotein of glucose oxidase was recognized.</abstract><cop>Japan</cop><pub>THE VITAMIN SOCIETY OF JAPAN</pub><pmid>4393601</pmid><doi>10.5925/jnsv1954.16.31</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | THE JOURNAL OF VITAMINOLOGY, 1970/03/10, Vol.16(1), pp.31-38 |
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| language | eng |
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| source | J-STAGE Free; MEDLINE; EZB-FREE-00999 freely available EZB journals |
| subjects | Adenosine Triphosphate botany Chemical Phenomena Chemistry Chromatography Flavin-Adenine Dinucleotide Glucose Oxidase Hydrogen-Ion Concentration Metals NAD NADP Nucleosides - antagonists & inhibitors Plant Science and Plant Products plants Pyrophosphatases - analysis Temperature Vegetables - analysis |
| title | On the enzymatic hydrolysis of FAD in spinach leaves |
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