Purification and characterization of an ADP-dependent phosphofructokinase from Thermococcus zilligii
The ADP-dependent phosphofructokinase (PFK) from Thermococcus zilligii has been purified 950 fold; it had a specific activity of 190 Umg(-1). The enzyme required Mg2+ ions for optimal activity and was specific for ADP. The forward reaction kinetics were hyperbolic for both cosubstrates (pH optimum o...
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| Veröffentlicht in: | Extremophiles : life under extreme conditions 1999-05, Vol.3 (2), p.121-129 |
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| creator | RONIMUS, R. S KONING, J MORGAN, H. W |
| description | The ADP-dependent phosphofructokinase (PFK) from Thermococcus zilligii has been purified 950 fold; it had a specific activity of 190 Umg(-1). The enzyme required Mg2+ ions for optimal activity and was specific for ADP. The forward reaction kinetics were hyperbolic for both cosubstrates (pH optimum of 6.4), and the apparent Km values for ADP and fructose-6-phosphate were 0.6mM (apparent Vmax of 243Umg(-1)) and 1.47mM (apparent Vmax of 197Umg(-1)), respectively. Significantly, the enzyme is indicated to be nonallosteric but was slightly activated by some monovalent cations including Na+ and K+. The protein had a subunit size of 42.2kDa and an estimated native molecular weight of 66kDa (gel filtration). Maximal reaction rates for the reverse reaction were attained at pH 7.5-8.0, and the apparent Km values for fructose-1,6-bisphosphate and AMP were 0.56mM (apparent Vmax of 2.9Umg(-1) and 12.5mM, respectively. The biochemical characteristics of this unique ADP-dependent enzymatic activity are compared to ATP and pyrophosphate-dependent phosphofructokinases. |
| doi_str_mv | 10.1007/s007920050107 |
| format | Article |
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Maximal reaction rates for the reverse reaction were attained at pH 7.5-8.0, and the apparent Km values for fructose-1,6-bisphosphate and AMP were 0.56mM (apparent Vmax of 2.9Umg(-1) and 12.5mM, respectively. The biochemical characteristics of this unique ADP-dependent enzymatic activity are compared to ATP and pyrophosphate-dependent phosphofructokinases.</description><identifier>ISSN: 1431-0651</identifier><identifier>EISSN: 1433-4909</identifier><identifier>DOI: 10.1007/s007920050107</identifier><identifier>PMID: 10356998</identifier><language>eng</language><publisher>Heidelberg: Springer</publisher><subject>Adenosine Diphosphate - metabolism ; Bacteriology ; Biological and medical sciences ; Cations ; Fundamental and applied biological sciences. Psychology ; Hydrogen-Ion Concentration ; Metabolism. 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S</creatorcontrib><creatorcontrib>KONING, J</creatorcontrib><creatorcontrib>MORGAN, H. W</creatorcontrib><title>Purification and characterization of an ADP-dependent phosphofructokinase from Thermococcus zilligii</title><title>Extremophiles : life under extreme conditions</title><addtitle>Extremophiles</addtitle><description>The ADP-dependent phosphofructokinase (PFK) from Thermococcus zilligii has been purified 950 fold; it had a specific activity of 190 Umg(-1). The enzyme required Mg2+ ions for optimal activity and was specific for ADP. The forward reaction kinetics were hyperbolic for both cosubstrates (pH optimum of 6.4), and the apparent Km values for ADP and fructose-6-phosphate were 0.6mM (apparent Vmax of 243Umg(-1)) and 1.47mM (apparent Vmax of 197Umg(-1)), respectively. Significantly, the enzyme is indicated to be nonallosteric but was slightly activated by some monovalent cations including Na+ and K+. The protein had a subunit size of 42.2kDa and an estimated native molecular weight of 66kDa (gel filtration). Maximal reaction rates for the reverse reaction were attained at pH 7.5-8.0, and the apparent Km values for fructose-1,6-bisphosphate and AMP were 0.56mM (apparent Vmax of 2.9Umg(-1) and 12.5mM, respectively. The biochemical characteristics of this unique ADP-dependent enzymatic activity are compared to ATP and pyrophosphate-dependent phosphofructokinases.</description><subject>Adenosine Diphosphate - metabolism</subject><subject>Bacteriology</subject><subject>Biological and medical sciences</subject><subject>Cations</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Hydrogen-Ion Concentration</subject><subject>Metabolism. Enzymes</subject><subject>Microbiology</subject><subject>Molecular Weight</subject><subject>Phosphofructokinase-1 - isolation & purification</subject><subject>Phosphofructokinase-1 - metabolism</subject><subject>Space life sciences</subject><subject>Thermococcus - enzymology</subject><issn>1431-0651</issn><issn>1433-4909</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVkL1PwzAQxS0EolAYWVEGxBY4x3EcjxXfUiU6lDm6ODY1JHGxk4H-9RhaIRjuQ-9-etI9Qs4oXFEAcR1ikxkABwpijxzRnLE0lyD3f3aaQsHphByH8AZAeTwckgkFxgspyyPSLEZvjVU4WNcn2DeJWqFHNWhvN1vRmagns9tF2ui17hvdD8l65UIs40c1uHfbY9CJ8a5LlivtO6ecUmNINrZt7au1J-TAYBv06W5Oycv93fLmMZ0_PzzdzOapYmU-pJyKRoDCpmZGImQgqKTYlCwXktfxF1XWihmd6ToTAgpJa6nyukTOKUWNbEout75r7z5GHYaqs0HptsVeuzFUhRRSsoJHMN2CyrsQvDbV2tsO_WdFofqOtfoXa-TPd8Zj3enmD73NMQIXOwCDwtZ47JUNv1w0YlnG2RddCYCV</recordid><startdate>19990501</startdate><enddate>19990501</enddate><creator>RONIMUS, R. 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Psychology</topic><topic>Hydrogen-Ion Concentration</topic><topic>Metabolism. Enzymes</topic><topic>Microbiology</topic><topic>Molecular Weight</topic><topic>Phosphofructokinase-1 - isolation & purification</topic><topic>Phosphofructokinase-1 - metabolism</topic><topic>Space life sciences</topic><topic>Thermococcus - enzymology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>RONIMUS, R. S</creatorcontrib><creatorcontrib>KONING, J</creatorcontrib><creatorcontrib>MORGAN, H. W</creatorcontrib><collection>Pascal-Francis</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>Extremophiles : life under extreme conditions</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>RONIMUS, R. S</au><au>KONING, J</au><au>MORGAN, H. 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Significantly, the enzyme is indicated to be nonallosteric but was slightly activated by some monovalent cations including Na+ and K+. The protein had a subunit size of 42.2kDa and an estimated native molecular weight of 66kDa (gel filtration). Maximal reaction rates for the reverse reaction were attained at pH 7.5-8.0, and the apparent Km values for fructose-1,6-bisphosphate and AMP were 0.56mM (apparent Vmax of 2.9Umg(-1) and 12.5mM, respectively. The biochemical characteristics of this unique ADP-dependent enzymatic activity are compared to ATP and pyrophosphate-dependent phosphofructokinases.</abstract><cop>Heidelberg</cop><cop>Tokyo</cop><pub>Springer</pub><pmid>10356998</pmid><doi>10.1007/s007920050107</doi><tpages>9</tpages></addata></record> |
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| subjects | Adenosine Diphosphate - metabolism Bacteriology Biological and medical sciences Cations Fundamental and applied biological sciences. Psychology Hydrogen-Ion Concentration Metabolism. Enzymes Microbiology Molecular Weight Phosphofructokinase-1 - isolation & purification Phosphofructokinase-1 - metabolism Space life sciences Thermococcus - enzymology |
| title | Purification and characterization of an ADP-dependent phosphofructokinase from Thermococcus zilligii |
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