PRKAA2: Difference between revisions

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Revision as of 18:40, 7 September 2017

5'-AMP-activated protein kinase catalytic subunit alpha-2 is an enzyme that in humans is encoded by the PRKAA2 gene.^[1]^[2]

Function

The protein encoded by this gene is a catalytic subunit of the AMP-activated protein kinase (AMPK). AMPK is a heterotrimer consisting of an alpha catalytic subunit, and non-catalytic beta and gamma subunits. AMPK is an important energy-sensing enzyme that monitors cellular energy status. In response to cellular metabolic stresses, AMPK is activated, and thus phosphorylates and inactivates acetyl-CoA carboxylase (ACC) and beta-hydroxy beta-methylglutaryl-CoA reductase (HMGCR), key enzymes involved in regulating de novo biosynthesis of fatty acid and cholesterol. Studies of the mouse counterpart suggest that this catalytic subunit may control whole-body insulin sensitivity and is necessary for maintaining myocardial energy homeostasis during ischemia.^[2]

References

↑ Aguan K, Scott J, See CG, Sarkar NH (Dec 1994). "Characterization and chromosomal localization of the human homologue of a rat AMP-activated protein kinase-encoding gene: a major regulator of lipid metabolism in mammals". Gene. 149 (2): 345–50. doi:10.1016/0378-1119(94)90174-0. PMID 7959015.
↑ ^2.0 ^2.1 "Entrez Gene: PRKAA2 protein kinase, AMP-activated, alpha 2 catalytic subunit".

Hardie DG, MacKintosh RW (1995). "AMP-activated protein kinase--an archetypal protein kinase cascade?". BioEssays. 14 (10): 699–704. doi:10.1002/bies.950141011. PMID 1365882.
Hardie DG (1992). "Regulation of fatty acid and cholesterol metabolism by the AMP-activated protein kinase". Biochim. Biophys. Acta. 1123 (3): 231–8. doi:10.1016/0005-2760(92)90001-c. PMID 1536860.
Carling D (2004). "The AMP-activated protein kinase cascade--a unifying system for energy control". Trends Biochem. Sci. 29 (1): 18–24. doi:10.1016/j.tibs.2003.11.005. PMID 14729328.
Beri RK, Marley AE, See CG, Sopwith WF, Aguan K, Carling D, Scott J, Carey F (1995). "Molecular cloning, expression and chromosomal localisation of human AMP-activated protein kinase". FEBS Lett. 356 (1): 117–21. doi:10.1016/0014-5793(94)01247-4. PMID 7988703.
Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
Vavvas D, Apazidis A, Saha AK, Gamble J, Patel A, Kemp BE, Witters LA, Ruderman NB (1997). "Contraction-induced changes in acetyl-CoA carboxylase and 5'-AMP-activated kinase in skeletal muscle". J. Biol. Chem. 272 (20): 13255–61. doi:10.1074/jbc.272.20.13255. PMID 9148944.
Stapleton D, Woollatt E, Mitchelhill KI, Nicholl JK, Fernandez CS, Michell BJ, Witters LA, Power DA, Sutherland GR, Kemp BE (1997). "AMP-activated protein kinase isoenzyme family: subunit structure and chromosomal location". FEBS Lett. 409 (3): 452–6. doi:10.1016/S0014-5793(97)00569-3. PMID 9224708.
Stein SC, Woods A, Jones NA, Davison MD, Carling D (2000). "The regulation of AMP-activated protein kinase by phosphorylation". Biochem. J. 345 (3): 437–43. doi:10.1042/0264-6021:3450437. PMC 1220775. PMID 10642499.
da Silva Xavier G, Leclerc I, Salt IP, Doiron B, Hardie DG, Kahn A, Rutter GA (2000). "Role of AMP-activated protein kinase in the regulation by glucose of islet beta cell gene expression". Proc. Natl. Acad. Sci. U.S.A. 97 (8): 4023–8. doi:10.1073/pnas.97.8.4023. PMC 18135. PMID 10760274.
Mu J, Brozinick JT, Valladares O, Bucan M, Birnbaum MJ (2001). "A role for AMP-activated protein kinase in contraction- and hypoxia-regulated glucose transport in skeletal muscle". Mol. Cell. 7 (5): 1085–94. doi:10.1016/S1097-2765(01)00251-9. PMID 11389854.
Minokoshi Y, Kim YB, Peroni OD, Fryer LG, Müller C, Carling D, Kahn BB (2002). "Leptin stimulates fatty-acid oxidation by activating AMP-activated protein kinase". Nature. 415 (6869): 339–43. doi:10.1038/415339a. PMID 11797013.
Dubbelhuis PF, Meijer AJ (2002). "Hepatic amino acid-dependent signaling is under the control of AMP-dependent protein kinase". FEBS Lett. 521 (1–3): 39–42. doi:10.1016/S0014-5793(02)02815-6. PMID 12067722.
Esumi H, Izuishi K, Kato K, Hashimoto K, Kurashima Y, Kishimoto A, Ogura T, Ozawa T (2002). "Hypoxia and nitric oxide treatment confer tolerance to glucose starvation in a 5'-AMP-activated protein kinase-dependent manner". J. Biol. Chem. 277 (36): 32791–8. doi:10.1074/jbc.M112270200. PMID 12091379.
Nielsen JN, Mustard KJ, Graham DA, Yu H, MacDonald CS, Pilegaard H, Goodyear LJ, Hardie DG, Richter EA, Wojtaszewski JF (2003). "5'-AMP-activated protein kinase activity and subunit expression in exercise-trained human skeletal muscle". J. Appl. Physiol. 94 (2): 631–41. doi:10.1152/japplphysiol.00642.2002. PMID 12391032.
Wojtaszewski JF, Mourtzakis M, Hillig T, Saltin B, Pilegaard H (2002). "Dissociation of AMPK activity and ACCbeta phosphorylation in human muscle during prolonged exercise". Biochem. Biophys. Res. Commun. 298 (3): 309–16. doi:10.1016/S0006-291X(02)02465-8. PMID 12413941.
Hallows KR, McCane JE, Kemp BE, Witters LA, Foskett JK (2003). "Regulation of channel gating by AMP-activated protein kinase modulates cystic fibrosis transmembrane conductance regulator activity in lung submucosal cells". J. Biol. Chem. 278 (2): 998–1004. doi:10.1074/jbc.M210621200. PMID 12427743.
Zong H, Ren JM, Young LH, Pypaert M, Mu J, Birnbaum MJ, Shulman GI (2003). "AMP kinase is required for mitochondrial biogenesis in skeletal muscle in response to chronic energy deprivation". Proc. Natl. Acad. Sci. U.S.A. 99 (25): 15983–7. doi:10.1073/pnas.252625599. PMC 138551. PMID 12444247.

This article on a gene on human chromosome 1 is a stub. You can help Wikipedia by expanding it.

[pmid7959015-1] Aguan K, Scott J, See CG, Sarkar NH (Dec 1994). "Characterization and chromosomal localization of the human homologue of a rat AMP-activated protein kinase-encoding gene: a major regulator of lipid metabolism in mammals". Gene. 149 (2): 345–50. doi:10.1016/0378-1119(94)90174-0. PMID 7959015.

[entrez-2] 2.0 ^2.1 "Entrez Gene: PRKAA2 protein kinase, AMP-activated, alpha 2 catalytic subunit".

[1]

[2]

@@ Line 1: / Line 1: @@
-<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
+{{Underlinked|date=June 2016}}
-{{PBB_Controls
+{{Infobox_gene}}
-| update_page = yes
+'''5'-AMP-activated protein kinase catalytic subunit alpha-2''' is an [[enzyme]] that in humans is encoded by the ''PRKAA2'' [[gene]].<ref name="pmid7959015">{{cite journal | vauthors = Aguan K, Scott J, See CG, Sarkar NH | title = Characterization and chromosomal localization of the human homologue of a rat AMP-activated protein kinase-encoding gene: a major regulator of lipid metabolism in mammals | journal = Gene | volume = 149 | issue = 2 | pages = 345–50 | date = Dec 1994 | pmid = 7959015 | pmc =  | doi = 10.1016/0378-1119(94)90174-0 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: PRKAA2 protein kinase, AMP-activated, alpha 2 catalytic subunit| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5563| accessdate = }}</ref>
-| require_manual_inspection = no
-| update_protein_box = yes
-| update_summary = yes
-| update_citations = yes
-}}
-<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
+== Function ==
-{{GNF_Protein_box
- | image = PBB_Protein_PRKAA2_image.jpg
- | image_source = [[Protein_Data_Bank|PDB]] rendering based on 2h6d.
- | PDB = {{PDB2|2h6d}}
- | Name = Protein kinase, AMP-activated, alpha 2 catalytic subunit
- | HGNCid = 9377
- | Symbol = PRKAA2
- | AltSymbols =; AMPK; AMPK2; PRKAA
- | OMIM = 600497
- | ECnumber =
- | Homologene = 4551
- | MGIid = 1336173
- | GeneAtlas_image1 = PBB_GE_PRKAA2_207709_at_tn.png
- | Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0000287 |text = magnesium ion binding}} {{GNF_GO|id=GO:0004674 |text = protein serine/threonine kinase activity}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
- | Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
- | Process = {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0006633 |text = fatty acid biosynthetic process}} {{GNF_GO|id=GO:0006695 |text = cholesterol biosynthetic process}} {{GNF_GO|id=GO:0007165 |text = signal transduction}}
- | Orthologs = {{GNF_Ortholog_box
-    | Hs_EntrezGene = 5563
-    | Hs_Ensembl = ENSG00000162409
-    | Hs_RefseqProtein = NP_006243
-    | Hs_RefseqmRNA = NM_006252
-    | Hs_GenLoc_db =
-    | Hs_GenLoc_chr = 1
-    | Hs_GenLoc_start = 56883583
-    | Hs_GenLoc_end = 56953596
-    | Hs_Uniprot = P54646
-    | Mm_EntrezGene = 108079
-    | Mm_Ensembl = ENSMUSG00000028518
-    | Mm_RefseqmRNA = NM_178143
-    | Mm_RefseqProtein = NP_835279
-    | Mm_GenLoc_db =
-    | Mm_GenLoc_chr = 4
-    | Mm_GenLoc_start = 104532922
-    | Mm_GenLoc_end = 104607801
-    | Mm_Uniprot = Q8BRK8
-  }}
-}}
-'''Protein kinase, AMP-activated, alpha 2 catalytic subunit''', also known as '''PRKAA2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PRKAA2 protein kinase, AMP-activated, alpha 2 catalytic subunit| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5563| accessdate = }}</ref>
-<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
+The protein encoded by this gene is a catalytic subunit of the AMP-activated protein kinase (AMPK). AMPK is a heterotrimer consisting of an alpha catalytic subunit, and non-catalytic beta and gamma subunits. AMPK is an important energy-sensing enzyme that monitors cellular energy status. In response to cellular metabolic stresses, AMPK is activated, and thus phosphorylates and inactivates acetyl-CoA carboxylase (ACC) and beta-hydroxy beta-methylglutaryl-CoA reductase (HMGCR), key enzymes involved in regulating de novo biosynthesis of fatty acid and cholesterol. Studies of the mouse counterpart suggest that this catalytic subunit may control whole-body insulin sensitivity and is necessary for maintaining myocardial energy homeostasis during ischemia.<ref name="entrez" />
-{{PBB_Summary
-| section_title =
-| summary_text = The protein encoded by this gene is a catalytic subunit of the AMP-activated protein kinase (AMPK). AMPK is a heterotrimer consisting of an alpha catalytic subunit, and non-catalytic beta and gamma subunits. AMPK is an important energy-sensing enzyme that monitors cellular energy status. In response to cellular metabolic stresses, AMPK is activated, and thus phosphorylates and inactivates acetyl-CoA carboxylase (ACC) and beta-hydroxy beta-methylglutaryl-CoA reductase (HMGCR), key enzymes involved in regulating de novo biosynthesis of fatty acid and cholesterol. Studies of the mouse counterpart suggest that this catalytic subunit may control whole-body insulin sensitivity and is necessary for maintaining myocardial energy homeostasis during ischemia.<ref name="entrez">{{cite web | title = Entrez Gene: PRKAA2 protein kinase, AMP-activated, alpha 2 catalytic subunit| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5563| accessdate = }}</ref>
-}}
-==References==
+== References ==
-{{reflist|2}}
+{{reflist}}
-==Further reading==
+== Further reading ==
 {{refbegin | 2}}
-{{PBB_Further_reading
+* {{cite journal | vauthors = Hardie DG, MacKintosh RW | title = AMP-activated protein kinase--an archetypal protein kinase cascade? | journal = BioEssays | volume = 14 | issue = 10 | pages = 699–704 | year = 1995 | pmid = 1365882 | doi = 10.1002/bies.950141011 }}
-| citations =
+* {{cite journal | vauthors = Hardie DG | title = Regulation of fatty acid and cholesterol metabolism by the AMP-activated protein kinase | journal = Biochim. Biophys. Acta | volume = 1123 | issue = 3 | pages = 231–8 | year = 1992 | pmid = 1536860 | doi = 10.1016/0005-2760(92)90001-c }}
-*{{cite journal  | author=Hardie DG, MacKintosh RW |title=AMP-activated protein kinase--an archetypal protein kinase cascade? |journal=Bioessays |volume=14 |issue= 10 |pages= 699-704 |year= 1995 |pmid= 1365882 |doi= 10.1002/bies.950141011 }}
+* {{cite journal | vauthors = Carling D | title = The AMP-activated protein kinase cascade--a unifying system for energy control | journal = Trends Biochem. Sci. | volume = 29 | issue = 1 | pages = 18–24 | year = 2004 | pmid = 14729328 | doi = 10.1016/j.tibs.2003.11.005 }}
-*{{cite journal  | author=Hardie DG |title=Regulation of fatty acid and cholesterol metabolism by the AMP-activated protein kinase. |journal=Biochim. Biophys. Acta |volume=1123 |issue= 3 |pages= 231-8 |year= 1992 |pmid= 1536860 |doi=  }}
+* {{cite journal | vauthors = Beri RK, Marley AE, See CG, Sopwith WF, Aguan K, Carling D, Scott J, Carey F | title = Molecular cloning, expression and chromosomal localisation of human AMP-activated protein kinase | journal = FEBS Lett. | volume = 356 | issue = 1 | pages = 117–21 | year = 1995 | pmid = 7988703 | doi = 10.1016/0014-5793(94)01247-4 }}
-*{{cite journal  | author=Carling D |title=The AMP-activated protein kinase cascade--a unifying system for energy control. |journal=Trends Biochem. Sci. |volume=29 |issue= 1 |pages= 18-24 |year= 2004 |pmid= 14729328 |doi=  }}
+* {{cite journal | vauthors = Bonaldo MF, Lennon G, Soares MB | title = Normalization and subtraction: two approaches to facilitate gene discovery | journal = Genome Res. | volume = 6 | issue = 9 | pages = 791–806 | year = 1997 | pmid = 8889548 | doi = 10.1101/gr.6.9.791 }}
-*{{cite journal  | author=Aguan K, Scott J, See CG, Sarkar NH |title=Characterization and chromosomal localization of the human homologue of a rat AMP-activated protein kinase-encoding gene: a major regulator of lipid metabolism in mammals. |journal=Gene |volume=149 |issue= 2 |pages= 345-50 |year= 1994 |pmid= 7959015 |doi=  }}
+* {{cite journal | vauthors = Vavvas D, Apazidis A, Saha AK, Gamble J, Patel A, Kemp BE, Witters LA, Ruderman NB | title = Contraction-induced changes in acetyl-CoA carboxylase and 5'-AMP-activated kinase in skeletal muscle | journal = J. Biol. Chem. | volume = 272 | issue = 20 | pages = 13255–61 | year = 1997 | pmid = 9148944 | doi = 10.1074/jbc.272.20.13255 }}
-*{{cite journal  | author=Beri RK, Marley AE, See CG, ''et al.'' |title=Molecular cloning, expression and chromosomal localisation of human AMP-activated protein kinase. |journal=FEBS Lett. |volume=356 |issue= 1 |pages= 117-21 |year= 1995 |pmid= 7988703 |doi=  }}
+* {{cite journal | vauthors = Stapleton D, Woollatt E, Mitchelhill KI, Nicholl JK, Fernandez CS, Michell BJ, Witters LA, Power DA, Sutherland GR, Kemp BE | title = AMP-activated protein kinase isoenzyme family: subunit structure and chromosomal location | journal = FEBS Lett. | volume = 409 | issue = 3 | pages = 452–6 | year = 1997 | pmid = 9224708 | doi = 10.1016/S0014-5793(97)00569-3 }}
-*{{cite journal  | author=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791-806 |year= 1997 |pmid= 8889548 |doi=  }}
+* {{cite journal | vauthors = Stein SC, Woods A, Jones NA, Davison MD, Carling D | title = The regulation of AMP-activated protein kinase by phosphorylation | journal = Biochem. J. | volume = 345 | issue = 3 | pages = 437–43 | year = 2000 | pmid = 10642499 | pmc = 1220775 | doi = 10.1042/0264-6021:3450437 }}
-*{{cite journal  | author=Vavvas D, Apazidis A, Saha AK, ''et al.'' |title=Contraction-induced changes in acetyl-CoA carboxylase and 5'-AMP-activated kinase in skeletal muscle. |journal=J. Biol. Chem. |volume=272 |issue= 20 |pages= 13255-61 |year= 1997 |pmid= 9148944 |doi=  }}
+* {{cite journal | vauthors = da Silva Xavier G, Leclerc I, Salt IP, Doiron B, Hardie DG, Kahn A, Rutter GA | title = Role of AMP-activated protein kinase in the regulation by glucose of islet beta cell gene expression | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 97 | issue = 8 | pages = 4023–8 | year = 2000 | pmid = 10760274 | pmc = 18135 | doi = 10.1073/pnas.97.8.4023 }}
-*{{cite journal  | author=Stapleton D, Woollatt E, Mitchelhill KI, ''et al.'' |title=AMP-activated protein kinase isoenzyme family: subunit structure and chromosomal location. |journal=FEBS Lett. |volume=409 |issue= 3 |pages= 452-6 |year= 1997 |pmid= 9224708 |doi=  }}
+* {{cite journal | vauthors = Mu J, Brozinick JT, Valladares O, Bucan M, Birnbaum MJ | title = A role for AMP-activated protein kinase in contraction- and hypoxia-regulated glucose transport in skeletal muscle | journal = Mol. Cell | volume = 7 | issue = 5 | pages = 1085–94 | year = 2001 | pmid = 11389854 | doi = 10.1016/S1097-2765(01)00251-9 }}
-*{{cite journal  | author=Stein SC, Woods A, Jones NA, ''et al.'' |title=The regulation of AMP-activated protein kinase by phosphorylation. |journal=Biochem. J. |volume=345 Pt 3 |issue=  |pages= 437-43 |year= 2000 |pmid= 10642499 |doi=  }}
+* {{cite journal | vauthors = Minokoshi Y, Kim YB, Peroni OD, Fryer LG, Müller C, Carling D, Kahn BB | title = Leptin stimulates fatty-acid oxidation by activating AMP-activated protein kinase | journal = Nature | volume = 415 | issue = 6869 | pages = 339–43 | year = 2002 | pmid = 11797013 | doi = 10.1038/415339a }}
-*{{cite journal  | author=da Silva Xavier G, Leclerc I, Salt IP, ''et al.'' |title=Role of AMP-activated protein kinase in the regulation by glucose of islet beta cell gene expression. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 8 |pages= 4023-8 |year= 2000 |pmid= 10760274 |doi=  }}
+* {{cite journal | vauthors = Dubbelhuis PF, Meijer AJ | title = Hepatic amino acid-dependent signaling is under the control of AMP-dependent protein kinase | journal = FEBS Lett. | volume = 521 | issue = 1–3 | pages = 39–42 | year = 2002 | pmid = 12067722 | doi = 10.1016/S0014-5793(02)02815-6 }}
-*{{cite journal  | author=Mu J, Brozinick JT, Valladares O, ''et al.'' |title=A role for AMP-activated protein kinase in contraction- and hypoxia-regulated glucose transport in skeletal muscle. |journal=Mol. Cell |volume=7 |issue= 5 |pages= 1085-94 |year= 2001 |pmid= 11389854 |doi=  }}
+* {{cite journal | vauthors = Esumi H, Izuishi K, Kato K, Hashimoto K, Kurashima Y, Kishimoto A, Ogura T, Ozawa T | title = Hypoxia and nitric oxide treatment confer tolerance to glucose starvation in a 5'-AMP-activated protein kinase-dependent manner | journal = J. Biol. Chem. | volume = 277 | issue = 36 | pages = 32791–8 | year = 2002 | pmid = 12091379 | doi = 10.1074/jbc.M112270200 }}
-*{{cite journal  | author=Minokoshi Y, Kim YB, Peroni OD, ''et al.'' |title=Leptin stimulates fatty-acid oxidation by activating AMP-activated protein kinase. |journal=Nature |volume=415 |issue= 6869 |pages= 339-43 |year= 2002 |pmid= 11797013 |doi= 10.1038/415339a }}
+* {{cite journal | vauthors = Nielsen JN, Mustard KJ, Graham DA, Yu H, MacDonald CS, Pilegaard H, Goodyear LJ, Hardie DG, Richter EA, Wojtaszewski JF | title = 5'-AMP-activated protein kinase activity and subunit expression in exercise-trained human skeletal muscle | journal = J. Appl. Physiol. | volume = 94 | issue = 2 | pages = 631–41 | year = 2003 | pmid = 12391032 | doi = 10.1152/japplphysiol.00642.2002 }}
-*{{cite journal  | author=Dubbelhuis PF, Meijer AJ |title=Hepatic amino acid-dependent signaling is under the control of AMP-dependent protein kinase. |journal=FEBS Lett. |volume=521 |issue= 1-3 |pages= 39-42 |year= 2002 |pmid= 12067722 |doi=  }}
+* {{cite journal | vauthors = Wojtaszewski JF, Mourtzakis M, Hillig T, Saltin B, Pilegaard H | title = Dissociation of AMPK activity and ACCbeta phosphorylation in human muscle during prolonged exercise | journal = Biochem. Biophys. Res. Commun. | volume = 298 | issue = 3 | pages = 309–16 | year = 2002 | pmid = 12413941 | doi = 10.1016/S0006-291X(02)02465-8 }}
-*{{cite journal  | author=Esumi H, Izuishi K, Kato K, ''et al.'' |title=Hypoxia and nitric oxide treatment confer tolerance to glucose starvation in a 5'-AMP-activated protein kinase-dependent manner. |journal=J. Biol. Chem. |volume=277 |issue= 36 |pages= 32791-8 |year= 2002 |pmid= 12091379 |doi= 10.1074/jbc.M112270200 }}
+* {{cite journal | vauthors = Hallows KR, McCane JE, Kemp BE, Witters LA, Foskett JK | title = Regulation of channel gating by AMP-activated protein kinase modulates cystic fibrosis transmembrane conductance regulator activity in lung submucosal cells | journal = J. Biol. Chem. | volume = 278 | issue = 2 | pages = 998–1004 | year = 2003 | pmid = 12427743 | doi = 10.1074/jbc.M210621200 }}
-*{{cite journal  | author=Nielsen JN, Mustard KJ, Graham DA, ''et al.'' |title=5'-AMP-activated protein kinase activity and subunit expression in exercise-trained human skeletal muscle. |journal=J. Appl. Physiol. |volume=94 |issue= 2 |pages= 631-41 |year= 2003 |pmid= 12391032 |doi= 10.1152/japplphysiol.00642.2002 }}
+* {{cite journal | vauthors = Zong H, Ren JM, Young LH, Pypaert M, Mu J, Birnbaum MJ, Shulman GI | title = AMP kinase is required for mitochondrial biogenesis in skeletal muscle in response to chronic energy deprivation | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 99 | issue = 25 | pages = 15983–7 | year = 2003 | pmid = 12444247 | pmc = 138551 | doi = 10.1073/pnas.252625599 }}
-*{{cite journal  | author=Wojtaszewski JF, Mourtzakis M, Hillig T, ''et al.'' |title=Dissociation of AMPK activity and ACCbeta phosphorylation in human muscle during prolonged exercise. |journal=Biochem. Biophys. Res. Commun. |volume=298 |issue= 3 |pages= 309-16 |year= 2002 |pmid= 12413941 |doi=  }}
-*{{cite journal  | author=Hallows KR, McCane JE, Kemp BE, ''et al.'' |title=Regulation of channel gating by AMP-activated protein kinase modulates cystic fibrosis transmembrane conductance regulator activity in lung submucosal cells. |journal=J. Biol. Chem. |volume=278 |issue= 2 |pages= 998-1004 |year= 2003 |pmid= 12427743 |doi= 10.1074/jbc.M210621200 }}
-*{{cite journal  | author=Zong H, Ren JM, Young LH, ''et al.'' |title=AMP kinase is required for mitochondrial biogenesis in skeletal muscle in response to chronic energy deprivation. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 25 |pages= 15983-7 |year= 2003 |pmid= 12444247 |doi= 10.1073/pnas.252625599 }}
-}}
 {{refend}}
-{{protein-stub}}
+{{PDB Gallery|geneid=5563}}
-{{WikiDoc Sources}}
+{{Serine/threonine-specific protein kinases}}
+{{Enzymes}}
+{{Portal bar|Molecular and Cellular Biology|border=no}}
+[[Category:EC 2.7.11]]
+{{gene-1-stub}}

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme 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)

PRKAA2: Difference between revisions

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