(Pyruvate, phosphate dikinase)-phosphate phosphotransferase: Difference between revisions

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(Pyruvate, phosphate dikinase)-phosphate phosphotransferase
(Pyruvate, phosphate dikinase)-phosphate phosphotransferase
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EC no.	2.7.4.27
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BRENDA	BRENDA entry
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(Pyruvate, phosphate dikinase)-phosphate phosphotransferase (EC 2.7.4.27, PPDK regulatory protein, pyruvate, phosphate dikinase regulatory protein, bifunctional dikinase regulatory protein, PDRP1 (gene)) is an enzyme with systematic name (pyruvate, phosphate dikinase) phosphate:phosphate phosphotransferase.^[1]^[2]^[3]^[4]^[5] This enzyme catalyses the following chemical reaction

[pyruvate, phosphate dikinase] phosphate + phosphate

\rightleftharpoons

[pyruvate, phosphate dikinase] + diphosphate

The enzyme from the plants maize and arabidopsis is bifunctional and also catalyses the phosphorylation of pyruvate (EC 2.7.11.32).

References

^ Burnell JN, Hatch MD (May 1984). "Regulation of C4 photosynthesis: identification of a catalytically important histidine residue and its role in the regulation of pyruvate,Pi dikinase". Archives of Biochemistry and Biophysics. 231 (1): 175–82. doi:10.1016/0003-9861(84)90375-8. PMID 6326674.
^ Burnell JN, Hatch MD (March 1985). "Regulation of C4 photosynthesis: purification and properties of the protein catalyzing ADP-mediated inactivation and Pi-mediated activation of pyruvate,Pi dikinase". Archives of Biochemistry and Biophysics. 237 (2): 490–503. doi:10.1016/0003-9861(85)90302-9. PMID 2983615.
^ Chastain CJ, Botschner M, Harrington GE, Thompson BJ, Mills SE, Sarath G, Chollet R (March 2000). "Further analysis of maize C(4) pyruvate,orthophosphate dikinase phosphorylation by its bifunctional regulatory protein using selective substitutions of the regulatory Thr-456 and catalytic His-458 residues". Archives of Biochemistry and Biophysics. 375 (1): 165–70. doi:10.1006/abbi.1999.1651. PMID 10683263.
^ Burnell JN, Chastain CJ (June 2006). "Cloning and expression of maize-leaf pyruvate, Pi dikinase regulatory protein gene". Biochemical and Biophysical Research Communications. 345 (2): 675–80. doi:10.1016/j.bbrc.2006.04.150. PMID 16696949.
^ Chastain CJ, Xu W, Parsley K, Sarath G, Hibberd JM, Chollet R (March 2008). "The pyruvate, orthophosphate dikinase regulatory proteins of Arabidopsis possess a novel, unprecedented Ser/Thr protein kinase primary structure". The Plant Journal. 53 (5): 854–63. doi:10.1111/j.1365-313x.2007.03366.x. PMID 17996018.

External links

(pyruvate,+phosphate+dikinase)-phosphate+phosphotransferase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

[1] Burnell JN, Hatch MD (May 1984). "Regulation of C4 photosynthesis: identification of a catalytically important histidine residue and its role in the regulation of pyruvate,Pi dikinase". Archives of Biochemistry and Biophysics. 231 (1): 175–82. doi:10.1016/0003-9861(84)90375-8. PMID 6326674.

[2] Burnell JN, Hatch MD (March 1985). "Regulation of C4 photosynthesis: purification and properties of the protein catalyzing ADP-mediated inactivation and Pi-mediated activation of pyruvate,Pi dikinase". Archives of Biochemistry and Biophysics. 237 (2): 490–503. doi:10.1016/0003-9861(85)90302-9. PMID 2983615.

[3] Chastain CJ, Botschner M, Harrington GE, Thompson BJ, Mills SE, Sarath G, Chollet R (March 2000). "Further analysis of maize C(4) pyruvate,orthophosphate dikinase phosphorylation by its bifunctional regulatory protein using selective substitutions of the regulatory Thr-456 and catalytic His-458 residues". Archives of Biochemistry and Biophysics. 375 (1): 165–70. doi:10.1006/abbi.1999.1651. PMID 10683263.

[4] Burnell JN, Chastain CJ (June 2006). "Cloning and expression of maize-leaf pyruvate, Pi dikinase regulatory protein gene". Biochemical and Biophysical Research Communications. 345 (2): 675–80. doi:10.1016/j.bbrc.2006.04.150. PMID 16696949.

[5] Chastain CJ, Xu W, Parsley K, Sarath G, Hibberd JM, Chollet R (March 2008). "The pyruvate, orthophosphate dikinase regulatory proteins of Arabidopsis possess a novel, unprecedented Ser/Thr protein kinase primary structure". The Plant Journal. 53 (5): 854–63. doi:10.1111/j.1365-313x.2007.03366.x. PMID 17996018.

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[2]

[3]

[4]

[5]

@@ Line 1: / Line 1: @@
+{{Short description|Class of enzymes}}
 {{Infobox enzyme
-| Name = (Pyruvate, phosphate dikinase)-phosphate phosphotransferase
+| Name       = (Pyruvate, phosphate dikinase)-phosphate phosphotransferase
-| EC_number = 2.7.4.27
+| EC_number  = 2.7.4.27
 | CAS_number =
+| GO_code    =
-| IUBMB_EC_number = 2/7/4/27
-| GO_code =
+| image      =
-| image =
+| width      =
-| width =
+| caption    =
-| caption =
 }}
-'''(Pyruvate, phosphate dikinase)-phosphate phosphotransferase''' ({{EC number|2.7.4.27}}, ''PPDK regulatory protein'', ''pyruvate, phosphate dikinase regulatory protein'', ''bifunctional dikinase regulatory protein'', ''PDRP1 (gene)'') is an [[enzyme]] with [[List of enzymes|systematic name]] ''(pyruvate, phosphate dikinase) phosphate:phosphate phosphotransferase''.<ref>{{cite journal | title = Regulation of C<sub>4</sub> photosynthesis: identification of a catalytically important histidine residue and its role in the regulation of pyruvate,''P''<sub>i</sub> dikinase |author = Burnell, J.N. and Hatch, M.D. |journal = Arch. Biochem. Biophys. |year = 1984 |volume = 231 |pages = 175–182 |pmid = 6326674 |doi=10.1016/0003-9861(84)90375-8}}</ref><ref>{{cite journal | title = Regulation of C<sub>4</sub> photosynthesis: purification and properties of the protein catalyzing ADP-mediated inactivation and ''P''<sub>i</sub>-mediated activation of pyruvate,''P''<sub>i</sub> dikinase |author = Burnell, J.N. and Hatch, M.D. |journal = Arch. Biochem. Biophys. |year = 1985 |volume = 237 |pages = 490–503 |pmid = 2983615 |doi=10.1016/0003-9861(85)90302-9}}</ref><ref>{{cite journal | title = Further analysis of maize C<sub>4</sub> pyruvate,orthophosphate dikinase phosphorylation by its bifunctional regulatory protein using selective substitutions of the regulatory Thr-456 and catalytic His-458 residues |author = Chastain, C.J., Botschner, M., Harrington, G.E., Thompson, B.J., Mills, S.E., Sarath, G. and Chollet, R. |journal = Arch. Biochem. Biophys. |year = 2000 |volume = 375 |pages = 165–170 |pmid = 10683263 |doi=10.1006/abbi.1999.1651}}</ref><ref>{{cite journal | title = Cloning and expression of maize-leaf pyruvate, ''P''<sub>i</sub> dikinase regulatory protein gene |author = Burnell, J.N. and Chastain, C.J. |journal = Biochem. Biophys. Res. Commun. |year = 2006 |volume = 345 |pages = 675–680 |pmid = 16696949 |doi=10.1016/j.bbrc.2006.04.150}}</ref><ref>{{cite journal | title = The pyruvate, orthophosphate dikinase regulatory proteins of ''Arabidopsis'' possess a novel, unprecedented Ser/Thr protein kinase primary structure |author = Chastain, C.J., Xu, W., Parsley, K., Sarath, G., Hibberd, J.M. and Chollet, R. |journal = Plant J. |year = 2008 |volume = 53 |pages = 854–863 |pmid = 17996018 |doi=10.1111/j.1365-313x.2007.03366.x}}</ref> This enzyme [[catalysis|catalyses]] the following [[chemical reaction]]
+'''(Pyruvate, phosphate dikinase)-phosphate phosphotransferase''' ({{EC number|2.7.4.27}}, ''PPDK regulatory protein'', ''pyruvate, phosphate dikinase regulatory protein'', ''bifunctional dikinase regulatory protein'', ''PDRP1 (gene)'') is an [[enzyme]] with [[List of enzymes|systematic name]] ''(pyruvate, phosphate dikinase) phosphate:phosphate phosphotransferase''.<ref>{{cite journal | vauthors = Burnell JN, Hatch MD | title = Regulation of C4 photosynthesis: identification of a catalytically important histidine residue and its role in the regulation of pyruvate,Pi dikinase | journal = Archives of Biochemistry and Biophysics | volume = 231 | issue = 1 | pages = 175–82 | date = May 1984 | pmid = 6326674 | doi = 10.1016/0003-9861(84)90375-8 }}</ref><ref>{{cite journal | vauthors = Burnell JN, Hatch MD | title = Regulation of C4 photosynthesis: purification and properties of the protein catalyzing ADP-mediated inactivation and Pi-mediated activation of pyruvate,Pi dikinase | journal = Archives of Biochemistry and Biophysics | volume = 237 | issue = 2 | pages = 490–503 | date = March 1985 | pmid = 2983615 | doi = 10.1016/0003-9861(85)90302-9 }}</ref><ref>{{cite journal | vauthors = Chastain CJ, Botschner M, Harrington GE, Thompson BJ, Mills SE, Sarath G, Chollet R | title = Further analysis of maize C(4) pyruvate,orthophosphate dikinase phosphorylation by its bifunctional regulatory protein using selective substitutions of the regulatory Thr-456 and catalytic His-458 residues | journal = Archives of Biochemistry and Biophysics | volume = 375 | issue = 1 | pages = 165–70 | date = March 2000 | pmid = 10683263 | doi = 10.1006/abbi.1999.1651 }}</ref><ref>{{cite journal | vauthors = Burnell JN, Chastain CJ | title = Cloning and expression of maize-leaf pyruvate, Pi dikinase regulatory protein gene | journal = Biochemical and Biophysical Research Communications | volume = 345 | issue = 2 | pages = 675–80 | date = June 2006 | pmid = 16696949 | doi = 10.1016/j.bbrc.2006.04.150 }}</ref><ref>{{cite journal | vauthors = Chastain CJ, Xu W, Parsley K, Sarath G, Hibberd JM, Chollet R | title = The pyruvate, orthophosphate dikinase regulatory proteins of Arabidopsis possess a novel, unprecedented Ser/Thr protein kinase primary structure | journal = The Plant Journal | volume = 53 | issue = 5 | pages = 854–63 | date = March 2008 | pmid = 17996018 | doi = 10.1111/j.1365-313x.2007.03366.x | url = http://digitalcommons.unl.edu/cgi/viewcontent.cgi?article=1021&context=biochemfacpub | doi-access = free }}</ref> This enzyme [[catalysis|catalyses]] the following [[chemical reaction]]
 : [pyruvate, phosphate dikinase] phosphate + [[phosphate]] <math>\rightleftharpoons</math> [pyruvate, phosphate dikinase] + [[diphosphate]]
-The enzyme from the plants [[maize]] and [[Arabidopsis thaliana|arabidopsis]] is bifunctional and also catalyses the [[phosphorylation]] of [[pyruvate]].
+The enzyme from the plants [[maize]] and [[Arabidopsis thaliana|arabidopsis]] is bifunctional and also catalyses the [[phosphorylation]] of [[pyruvate]] ([[EC 2.7.11.32]]).
 == References ==
@@ Line 23: / Line 23: @@
 {{Kinases}}
 {{Enzymes}}
-{{Portal bar|Molecular and Cellular Biology|border=no}}
+{{Portal bar|Biology|border=no}}
 [[Category:EC 2.7.4]]

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)