The substrate specificity, kinetics, and mechanism of glycerate-3-kinase from spinach leaves
Glycerate-3-kinase (EC 2.7.1.31) from spinach leaves shows absolute specificity for d-glycerate as phosphate acceptor, yielding 3-phosphoglycerate as a product. ATP complexed with either Mg 2+ or Mn 2+ is the preferred phosphate donor. The enzyme has K m (D-glycerate) = 0.25 mM, K m (Mg-ATP) = 0.21...
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| Veröffentlicht in: | Archives of biochemistry and biophysics 1985, Vol.236 (1), p.185-194 |
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| creator | Kleczkowski, Leszek A. Randall, Douglas D. Zahler, Warren L. |
| description | Glycerate-3-kinase (EC 2.7.1.31) from spinach leaves shows absolute specificity for
d-glycerate as phosphate acceptor, yielding 3-phosphoglycerate as a product. ATP complexed with either Mg
2+ or Mn
2+ is the preferred phosphate donor. The enzyme has
K
m
(D-glycerate) = 0.25 mM,
K
m
(Mg-ATP) = 0.21 mM,
V
max = 300 μmol min
−1 mg protein
−1,
and
a
turnover
number = 12,000·min
−1. The equilibrium constant for the reaction is approximately 300 at pH 7.8. Pyrophosphate, 3-phosphoglycerate and ribulose 1,5-bisphosphate are the strongest inhibitors among the phosphorylated and nonphosphorylated metabolites tested; however, their regulatory role
in vivo is questioned. Substrate kinetics, as well as product and analog inhibition data, are consistent with a sequential random mechanism. The distinct characteristic of the glycerate kinase-catalyzed reaction is the formation of a dead-end complex between the enzyme,
d-glycerate, and 3-phosphoglycerate. |
| doi_str_mv | 10.1016/0003-9861(85)90618-6 |
| format | Article |
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d-glycerate as phosphate acceptor, yielding 3-phosphoglycerate as a product. ATP complexed with either Mg
2+ or Mn
2+ is the preferred phosphate donor. The enzyme has
K
m
(D-glycerate) = 0.25 mM,
K
m
(Mg-ATP) = 0.21 mM,
V
max = 300 μmol min
−1 mg protein
−1,
and
a
turnover
number = 12,000·min
−1. The equilibrium constant for the reaction is approximately 300 at pH 7.8. Pyrophosphate, 3-phosphoglycerate and ribulose 1,5-bisphosphate are the strongest inhibitors among the phosphorylated and nonphosphorylated metabolites tested; however, their regulatory role
in vivo is questioned. Substrate kinetics, as well as product and analog inhibition data, are consistent with a sequential random mechanism. The distinct characteristic of the glycerate kinase-catalyzed reaction is the formation of a dead-end complex between the enzyme,
d-glycerate, and 3-phosphoglycerate.</description><identifier>ISSN: 0003-9861</identifier><identifier>EISSN: 1096-0384</identifier><identifier>DOI: 10.1016/0003-9861(85)90618-6</identifier><identifier>PMID: 2981505</identifier><identifier>CODEN: ABBIA4</identifier><language>eng</language><publisher>San Diego, CA: Elsevier Inc</publisher><subject>ACTIVITY ; Adenosine Triphosphate - metabolism ; Agronomy. Soil science and plant productions ; Analytical, structural and metabolic biochemistry ; Biological and medical sciences ; Cations, Divalent - metabolism ; Economic plant physiology ; Enzymes ; Enzymes and enzyme inhibitors ; Fundamental and applied biological sciences. Psychology ; Glyceric Acids - metabolism ; GLYCEROKINASE ; Kinetics ; Nutrition. Photosynthesis. Respiration. Metabolism ; Phosphates - metabolism ; Phosphotransferases (Alcohol Group Acceptor) ; Phosphotransferases - antagonists & inhibitors ; Phosphotransferases - isolation & purification ; Phosphotransferases - metabolism ; Plants - enzymology ; SPINACIA OLERACEA ; Substrate Specificity ; SUBSTRATES ; Transferases</subject><ispartof>Archives of biochemistry and biophysics, 1985, Vol.236 (1), p.185-194</ispartof><rights>1985</rights><rights>1985 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c405t-eb0d43695499ce1075fba800b891512cb6ad9f3553e6e2614b1271953ba3ebda3</citedby><cites>FETCH-LOGICAL-c405t-eb0d43695499ce1075fba800b891512cb6ad9f3553e6e2614b1271953ba3ebda3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0003-9861(85)90618-6$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,778,782,3539,4012,27912,27913,27914,45984</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=9061965$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2981505$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kleczkowski, Leszek A.</creatorcontrib><creatorcontrib>Randall, Douglas D.</creatorcontrib><creatorcontrib>Zahler, Warren L.</creatorcontrib><title>The substrate specificity, kinetics, and mechanism of glycerate-3-kinase from spinach leaves</title><title>Archives of biochemistry and biophysics</title><addtitle>Arch Biochem Biophys</addtitle><description>Glycerate-3-kinase (EC 2.7.1.31) from spinach leaves shows absolute specificity for
d-glycerate as phosphate acceptor, yielding 3-phosphoglycerate as a product. ATP complexed with either Mg
2+ or Mn
2+ is the preferred phosphate donor. The enzyme has
K
m
(D-glycerate) = 0.25 mM,
K
m
(Mg-ATP) = 0.21 mM,
V
max = 300 μmol min
−1 mg protein
−1,
and
a
turnover
number = 12,000·min
−1. The equilibrium constant for the reaction is approximately 300 at pH 7.8. Pyrophosphate, 3-phosphoglycerate and ribulose 1,5-bisphosphate are the strongest inhibitors among the phosphorylated and nonphosphorylated metabolites tested; however, their regulatory role
in vivo is questioned. Substrate kinetics, as well as product and analog inhibition data, are consistent with a sequential random mechanism. The distinct characteristic of the glycerate kinase-catalyzed reaction is the formation of a dead-end complex between the enzyme,
d-glycerate, and 3-phosphoglycerate.</description><subject>ACTIVITY</subject><subject>Adenosine Triphosphate - metabolism</subject><subject>Agronomy. Soil science and plant productions</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Biological and medical sciences</subject><subject>Cations, Divalent - metabolism</subject><subject>Economic plant physiology</subject><subject>Enzymes</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Glyceric Acids - metabolism</subject><subject>GLYCEROKINASE</subject><subject>Kinetics</subject><subject>Nutrition. Photosynthesis. Respiration. Metabolism</subject><subject>Phosphates - metabolism</subject><subject>Phosphotransferases (Alcohol Group Acceptor)</subject><subject>Phosphotransferases - antagonists & inhibitors</subject><subject>Phosphotransferases - isolation & purification</subject><subject>Phosphotransferases - metabolism</subject><subject>Plants - enzymology</subject><subject>SPINACIA OLERACEA</subject><subject>Substrate Specificity</subject><subject>SUBSTRATES</subject><subject>Transferases</subject><issn>0003-9861</issn><issn>1096-0384</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1985</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kF1rFDEYhUOxtNvaP1AqzIUUCx19M5lkkhtBilah4IXtnRCSzJtudD7WZHZh_72Z7rKXvUrCec4hPIRcUfhIgYpPAMBKJQX9IPmNAkFlKY7IgoISJTBZvyGLA3JKzlL6A0BpLaoTclIpSTnwBfn9uMQirW2aopnybYUu-ODCtL0t_oYBp-DSbWGGtujRLc0QUl-Mvnjutg7nRsnKjJmEhY9jn_v54ZZFh2aD6S059qZLeLE_z8nTt6-Pd9_Lh5_3P-6-PJSuBj6VaKGtmVC8VsohhYZ7aySAlYpyWjkrTKs845yhwErQ2tKqoYozaxja1rBzcr3bXcXx3xrTpPuQHHadGXBcJ91wxVjV8AzWO9DFMaWIXq9i6E3cagp6lqpnY3o2piXXL1K1yLV3-_217bE9lPYWc_5-n5vkTOejGVxIB2yeUWLGLneYN6M2zzEjT7-kgKqqmxx-3oWYRW0CRp1cwMFhGyK6SbdjeP2T_wFnhZqx</recordid><startdate>1985</startdate><enddate>1985</enddate><creator>Kleczkowski, Leszek A.</creator><creator>Randall, Douglas D.</creator><creator>Zahler, Warren L.</creator><general>Elsevier Inc</general><general>Elsevier</general><scope>FBQ</scope><scope>IQODW</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>1985</creationdate><title>The substrate specificity, kinetics, and mechanism of glycerate-3-kinase from spinach leaves</title><author>Kleczkowski, Leszek A. ; Randall, Douglas D. ; Zahler, Warren L.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c405t-eb0d43695499ce1075fba800b891512cb6ad9f3553e6e2614b1271953ba3ebda3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1985</creationdate><topic>ACTIVITY</topic><topic>Adenosine Triphosphate - metabolism</topic><topic>Agronomy. Soil science and plant productions</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Biological and medical sciences</topic><topic>Cations, Divalent - metabolism</topic><topic>Economic plant physiology</topic><topic>Enzymes</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Glyceric Acids - metabolism</topic><topic>GLYCEROKINASE</topic><topic>Kinetics</topic><topic>Nutrition. Photosynthesis. Respiration. Metabolism</topic><topic>Phosphates - metabolism</topic><topic>Phosphotransferases (Alcohol Group Acceptor)</topic><topic>Phosphotransferases - antagonists & inhibitors</topic><topic>Phosphotransferases - isolation & purification</topic><topic>Phosphotransferases - metabolism</topic><topic>Plants - enzymology</topic><topic>SPINACIA OLERACEA</topic><topic>Substrate Specificity</topic><topic>SUBSTRATES</topic><topic>Transferases</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kleczkowski, Leszek A.</creatorcontrib><creatorcontrib>Randall, Douglas D.</creatorcontrib><creatorcontrib>Zahler, Warren L.</creatorcontrib><collection>AGRIS</collection><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>Archives of biochemistry and biophysics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kleczkowski, Leszek A.</au><au>Randall, Douglas D.</au><au>Zahler, Warren L.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The substrate specificity, kinetics, and mechanism of glycerate-3-kinase from spinach leaves</atitle><jtitle>Archives of biochemistry and biophysics</jtitle><addtitle>Arch Biochem Biophys</addtitle><date>1985</date><risdate>1985</risdate><volume>236</volume><issue>1</issue><spage>185</spage><epage>194</epage><pages>185-194</pages><issn>0003-9861</issn><eissn>1096-0384</eissn><coden>ABBIA4</coden><abstract>Glycerate-3-kinase (EC 2.7.1.31) from spinach leaves shows absolute specificity for
d-glycerate as phosphate acceptor, yielding 3-phosphoglycerate as a product. ATP complexed with either Mg
2+ or Mn
2+ is the preferred phosphate donor. The enzyme has
K
m
(D-glycerate) = 0.25 mM,
K
m
(Mg-ATP) = 0.21 mM,
V
max = 300 μmol min
−1 mg protein
−1,
and
a
turnover
number = 12,000·min
−1. The equilibrium constant for the reaction is approximately 300 at pH 7.8. Pyrophosphate, 3-phosphoglycerate and ribulose 1,5-bisphosphate are the strongest inhibitors among the phosphorylated and nonphosphorylated metabolites tested; however, their regulatory role
in vivo is questioned. Substrate kinetics, as well as product and analog inhibition data, are consistent with a sequential random mechanism. The distinct characteristic of the glycerate kinase-catalyzed reaction is the formation of a dead-end complex between the enzyme,
d-glycerate, and 3-phosphoglycerate.</abstract><cop>San Diego, CA</cop><pub>Elsevier Inc</pub><pmid>2981505</pmid><doi>10.1016/0003-9861(85)90618-6</doi><tpages>10</tpages></addata></record> |
| fulltext | fulltext |
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| ispartof | Archives of biochemistry and biophysics, 1985, Vol.236 (1), p.185-194 |
| issn | 0003-9861 1096-0384 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_75933275 |
| source | Elsevier ScienceDirect Journals Complete - AutoHoldings; MEDLINE |
| subjects | ACTIVITY Adenosine Triphosphate - metabolism Agronomy. Soil science and plant productions Analytical, structural and metabolic biochemistry Biological and medical sciences Cations, Divalent - metabolism Economic plant physiology Enzymes Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Glyceric Acids - metabolism GLYCEROKINASE Kinetics Nutrition. Photosynthesis. Respiration. Metabolism Phosphates - metabolism Phosphotransferases (Alcohol Group Acceptor) Phosphotransferases - antagonists & inhibitors Phosphotransferases - isolation & purification Phosphotransferases - metabolism Plants - enzymology SPINACIA OLERACEA Substrate Specificity SUBSTRATES Transferases |
| title | The substrate specificity, kinetics, and mechanism of glycerate-3-kinase from spinach leaves |
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