同: PGK

WordNet

an enzyme that catalyzes the conversion of a proenzyme to an active enzyme
the basic unit of money in Papua New Guinea

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〈U〉〈C〉(…の)(量・額などの)不足,欠乏《+『of』(『in』)+『名』》 / 〈C〉不足分,不足量,不足額 / 〈C〉(精神・肉体などの)欠陥

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2015/05/18 03:49:20」(JST)

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Phosphoglycerate kinase (EC 2.7.2.3) (PGK) is an enzyme that catalyzes the reversible transfer of a phosphate group from 1,3-bisphosphoglycerate (1,3-BPG) to ADP producing 3-phosphoglycerate (3-PG) and ATP. Like all kinases it is a transferase. PGK is a major enzyme used in glycolysis, in the first ATP-generating step of the glycolytic pathway. In gluconeogenesis, the reaction catalyzed by PGK proceeds in the opposite direction, generating ADP and 1,3-BPG.

In humans, two isozymes of PGK have been so far identified, PGK1 and PGK2. The isozymes have 87-88% identical amino acid sequence identity and though they are structurally and functionally similar, they have different localizations: PGK2, encoded by an autosomal gene, is unique to meiotic and postmeiotic spermatogenic cells, while PGK1, encoded on the X-chromosome, is ubiquitously expressed in all cells.^[2]

Biological function

Diagram showing glycolytic and gluconeogenic pathways. Note that phosphoglycerate kinase is used in both directions.

PGK is present in all living organisms as one of the two ATP-generating enzymes in glycolysis. In the gluconeogenic pathway, PGK catalyzes the reverse reaction. Under biochemical standard conditions, the glycolytic direction is favored.^[1]

In the Calvin cycle in photosynthetic organisms, PGK catalyzes the phosphorylation of 3-PG, producing 1,3-BPG and ADP, as part of the reactions that regenerate ribulose-1,5-bisphosphate.

PGK has been reported to exhibit thiol reductase activity on plasmin, leading to angiostatin formation, which inhibits angiogenesis and tumor growth. The enzyme was also shown to participate in DNA replication and repair in mammal cell nuclei.^[3]

The human isozyme PGK2, which is only expressed during spermatogenesis, was shown to be essential for sperm function in mice.^[4]

Interactive pathway map

Click on genes, proteins and metabolites below to link to respective articles. ^{[§ 1]}

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|{{{bSize}}}px|alt=Glycolysis and Gluconeogenesis edit||]]

File:WP534.png

Glycolysis and Gluconeogenesis edit

^ The interactive pathway map can be edited at WikiPathways: "GlycolysisGluconeogenesis_WP534".

Structure

Overview

PGK is found in all living organisms and its sequence has been highly conserved throughout evolution. The enzyme exists as a 415-residue monomer containing two nearly equal-sized domains that correspond to the N- and C-termini of the protein.^[5] 3-phosphoglycerate (3-PG) binds to the N-terminal, while the nucleotide substrates, MgATP or MgADP, bind to the C-terminal domain of the enzyme. This extended two-domain structure is associated with large-scale 'hinge-bending' conformational changes, similar to those found in hexokinase.^[6] The two domains of the protein are separated by a cleft and linked by two alpha-helices.^[2] At the core of each domain is a 6-stranded parallel beta-sheet surrounded by alpha helices. The two lobes are capable of folding independently, consistent with the presence of intermediates on the folding pathway with a single domain folded.^[7]^[8] Though the binding of either substrate triggers a conformational change, only through the binding of both substrates does domain closure occur, leading to the transfer of the phosphate group.^[2]

The enzyme has a tendency to exist in the open conformation with short periods of closure and catalysis, which allow for rapid diffusion of substrate and products through the binding sites; the open conformation of PGK is more conformationally stable due to the exposure of a hydrophobic region of the protein upon domain closure.^[7]

Role of magnesium

Magnesium ions are normally complexed to the phosphate groups the nucleotide substrates of PGK. It is known that in the absence of magnesium, no enzyme activity occurs.^[9] The bivalent metal assists the enzyme ligands in shielding the bound phosphate group's negative charges, allowing the nucleophilic attack to occur; this charge-stabilization is a typical characteristic of phosphotransfer reaction.^[10] It is theorized that the ion may also encourage domain closure when PGK has bound both substrates.^[9]

Mechanism

Phosphoglycerate kinase mechanism in glycolysis.

Without either substrate bound, PGK exists in an "open" conformation^{[disambiguation needed]}. After both the triose and nucleotide substrates are bound to the N- and C-terminal domains, respectively, an extensive hinge-bending motion occurs, bringing the domains and their bound substrates into close proximity and leading to a "closed" conformation.^[11] Then, in the case of the forward glycolytic reaction, the beta-phosphate of ADP initiates a nucleophilic attack on the 1-phosphate of 1,3-BPG in an SN2 substitution reaction.^[12] The Lys219 on the enzyme guides the phosphate group to the substrate.

PGK proceeds through a charge-stabilized transition state that is favored over the arrangement of the bound substrate in the closed enzyme because in the transition state, all three phosphate oxygens are stabilized by ligands, as opposed to only two stabilized oxygens in the initial bound state.^[13]

In the glycolytic pathyway, 1,3-BPG is the phosphate donor and has a high phosphoryl-transfer potential. The PGK-catalyzed transfer of the phosphate group from 1,3-BPG to ADP to yield ATP can power the carbon-oxidation reaction of the previous glycolytic step (converting glyceraldehyde 3-phosphate to 3-phosphoglycerate).

Regulation

The enzyme is activated by low concentrations of various multivalent anions, such as pyrophosphate, sulfate, phosphate, and citrate. High concentrations of MgATP and 3-PG activates PGK, while Mg2+ at high concentrations non-competitively inhibits the enzyme.^[14]

PGK exhibits a wide specificity toward nucleotide substrates.^[15] Its activity is inhibited by salicylates, which appear to mimic the enzyme's nucleotide substrate.^[16]

Macromolecular crowding has been shown to increase PGK activity in both computer simluations and in vitro environments simulating a cell interior; as a result of crowding, the enzyme becomes more enyzmatically active and more compact.^[5]

Disease relevance

Phosphoglycerate kinase (PGK) deficiency is an X-linked recessive trait associated with hemolytic anemia, mental disorders and myopathy in humans.^[17]^[18] Since the trait is X-linked, it is usually fully expressed in males, who have one X chromosome; affected females are typically asymptomatic.^[2]^[18] The condition results from mutations in Pgk1, the gene encoding PGK1, and twenty mutations have been identified.^[18]^[2] On a molecular level, the mutation in Pgk1 impairs the thermal stability and inhibits the catalytic activity of the enzyme.^[2] PGK is the only enzyme in the immediate glycolytic pathway encoded by an X-linked gene. In the case of hemolytic anemia, PGK deficiency occurs in the erythrocytes. Currently, no definitive treatment exists for PGK deficiency.^[19]

PGK1 overexpression has been associated with gastric cancer and has been found to increase the invasiveness of gastric cancer cells in vitro.^[20] The enzyme is secreted by tumor cells and participates in the angiogenic process, leading to the release of angiostatin and the inhibition of tumor blood vessel growth.^[3]^[3]

Due to its wide specificity towards nucleotide substrates, PGK is known to participate in the phosphorylation and activation of HIV antiretroviral drugs, which are nucleotide-based.^[15]^[21]

Human isozymes

phosphoglycerate kinase 1
Identifiers
Symbol	PGK1
Entrez	5230
HUGO	8896
OMIM	311800
RefSeq	NM_000291
UniProt	P00558
Other data
EC number	2.7.2.3
Locus	Chr. X q13.3

phosphoglycerate kinase 2
Identifiers
Symbol	PGK2
Entrez	5232
HUGO	8898
OMIM	172270
RefSeq	NM_138733
UniProt	P07205
Other data
EC number	2.7.2.3
Locus	Chr. 6 p21-q12

References

^ ^a ^b Watson HC, Walker NP, Shaw PJ et al. (1982). "Sequence and structure of yeast phosphoglycerate kinase". EMBO J. 1 (12): 1635–40. PMC 553262. PMID 6765200.
^ ^a ^b ^c ^d ^e ^f Chiarelli LR, Morera SM, Bianchi P, Fermo E, Zanella A, Galizzi A, Valentini G (2012). "Molecular insights on pathogenic effects of mutations causing phosphoglycerate kinase deficiency". PLoS ONE 7 (2): e32065. doi:10.1371/journal.pone.0032065. PMC 3279470. PMID 22348148.
^ ^a ^b ^c Hogg, Philip J.; Lay, Angelina J.; Jiang, Xing-Mai; Kisker, Oliver; Flynn, Evelyn; Underwood, Anne; Condron, Rosemary (14 December 2000). Nature 408 (6814): 869–873. doi:10.1038/35048596. Missing or empty |title= (help); |accessdate= requires |url= (help)
^ Danshina, Polina; GB Geyer; Q Dai; EH Goulding; WD Willis et al. (1 January 2010). "Phosphoglycerate Kinase 2 (PGK2) Is Essential for Sperm Function and Male Fertility in Mice". Biology of Reproduction 82 (1): 136–145. doi:10.1095/biolreprod.109.079699.
^ ^a ^b Dhar, A.; Samiotakis, A.; Ebbinghaus, S.; Nienhaus, L.; Homouz, D.; Gruebele, M.; Cheung, M. S. (4 October 2010). "Structure, function, and folding of phosphoglycerate kinase are strongly perturbed by macromolecular crowding". Proceedings of the National Academy of Sciences 107 (41): 17586–17591. doi:10.1073/pnas.1006760107. |accessdate= requires |url= (help)
^ Kumar S, Ma B, Tsai CJ, Wolfson H, Nussinov R (1999). "Folding funnels and conformational transitions via hinge-bending motions". Cell Biochem. Biophys. 31 (2): 141–64. doi:10.1007/BF02738169. PMID 10593256.
^ ^a ^b Yon JM, Desmadril M, Betton JM, Minard P, Ballery N, Missiakas D, Gaillard-Miran S, Perahia D, Mouawad L (1990). "Flexibility and folding of phosphoglycerate kinase". Biochimie 72 (6-7): 417–29. doi:10.1016/0300-9084(90)90066-p. PMID 2124145.
^ Zerrad L, Merli A, Schröder GF, Varga A, Gráczer É, Pernot P, Round A, Vas M, Bowler MW (April 2011). "A spring-loaded release mechanism regulates domain movement and catalysis in phosphoglycerate kinase". J. Biol. Chem. 286 (16): 14040–8. doi:10.1074/jbc.M110.206813. PMC 3077604. PMID 21349853.
^ ^a ^b Varga, Andrea; Palmai, Zoltan; Gugolya, Zoltán; Gráczer, Éva; Vonderviszt, Ferenc; Závodszky, Péter; Balog, Erika; Vas, Mária (21 December 2012). "Importance of Aspartate Residues in Balancing the Flexibility and Fine-Tuning the Catalysis of Human 3-Phosphoglycerate Kinase". Biochemistry 51 (51): 10197–10207. doi:10.1021/bi301194t. |accessdate= requires |url= (help)
^ Cliff, MJ; Bowler MW; Varga A; Marston JP et al. (12 May 2010). "Transition state analogue structures of human phosphoglycerate kinase establish the importance of charge balance in catalysis". J Am Chem Soc 132 (18): 6507–6516. doi:10.1021/ja100974t. PMID 20397725. Retrieved 6 March 2013.
^ Banks, R. D.; Blake, C. C. F.; Evans, P. R.; Haser, R.; Rice, D. W.; Hardy, G. W.; Merrett, M.; Phillips, A. W. (28 June 1979). "Sequence, structure and activity of phosphoglycerate kinase: a possible hinge-bending enzyme". Nature 279 (5716): 773–777. doi:10.1038/279773a0.
^ "Phosphoglycerate kinase". Mechanism, Annotation and Classification In Enzymes (MACiE). Retrieved 4 March 2013.
^ Bernstein, Bradley E; Wim G; Hol J (17 March 1998). "Crystal structures of substrates and products bound to the phosphoglycerate kinase active site reveal the catalytic mechanism". Biochemistry 37 (13): 4429–4436. doi:10.1021/bi9724117. |accessdate= requires |url= (help)
^ Larsson-Raźnikiewicz M (January 1967). "Kinetic studies on the reaction catalyzed by phosphoglycerate kinase. II. The kinetic relationships between 3-phosphoglycerate, MgATP2-and activating metal ion". Biochim. Biophys. Acta 132 (1): 33–40. doi:10.1016/0005-2744(67)90189-1. PMID 6030358.
^ ^a ^b Varga, A; Chaloin K; Sagi G; Sendula R et al. (20 April 2011). "Nucleotide promiscuity of 3-phosphoglycerate kinase is in focus: implications for the design of better anti-HIV analogues". Mol Biosyst 7 (6): 1863–73. doi:10.1039/c1mb05051f. PMID 21505655. |accessdate= requires |url= (help)
^ Larsson-Raźnikiewicz, Märtha; Wiksell, Eva (1 March 1978). "Inhibition of phosphoglycerate kinase by salicylates". Biochimica et Biophysica Acta (BBA) - Enzymology 523 (1): 94–100. doi:10.1016/0005-2744(78)90012-8. |accessdate= requires |url= (help)
^ Yoshida A, Tani K (1983). "Phosphoglycerate kinase abnormalities: functional, structural and genomic aspects". Biomed. Biochim. Acta 42 (11-12): S263–7. PMID 6689547.
^ ^a ^b ^c Beutler E (January 2007). "PGK deficiency". Br. J. Haematol. 136 (1): 3–11. doi:10.1111/j.1365-2141.2006.06351.x. PMID 17222195.
^ Rhodes, Melissa; Ashford, Linda; Manes, Becky; Calder, Cassie; Domm, Jennifer; Frangoul, Haydar (1 February 2011). "Bone marrow transplantation in phosphoglycerate kinase (PGK) deficiency". British Journal of Haematology 152 (4): 500–502. doi:10.1111/j.1365-2141.2010.08474.x.
^ Zieker, Derek; Königsrainer, Ingmar; Tritschler, Isabel; Löffler, Markus; Beckert, Stefan; Traub, Frank; Nieselt, Kay; Bühler, Sarah; Weller, Michael; Gaedcke, Jochen; Taichman, Russell S.; Northoff, Hinnak; Brücher BL; Königsrainer, Alfred (1 January 2010). "Phosphoglycerate kinase 1 a promoting enzyme for peritoneal dissemination in gastric cancer". International Journal of Cancer: NA–NA. doi:10.1002/ijc.24835. |accessdate= requires |url= (help)
^ Gallois-Mantbrun, Sarah; Faraj A; Seclaman E; Sommadossi JP et al. (1 November 2004). "Broad specificity of human phosphoglycerate kinase for antiviral nucleoside analogs". Biochemical Pharmacology 68 (9): 1749–1756. doi:10.1016/j.bcp.2004.06.012. PMID 15450940.

External links

-858783685 at GPnotebook
Phosphoglycerate kinase at the US National Library of Medicine Medical Subject Headings (MeSH)
Illustration at arizona.edu

Category:EC 2.7.2 This article incorporates text from the public domain Pfam and InterPro IPR001576

UpToDate Contents

全文を閲覧するには購読必要です。 To read the full text you will need to subscribe.

1. ホスホグリセリン酸キナーゼ欠損症およびホスホグリセリン酸ムターゼ欠損症 phosphoglycerate kinase deficiency and phosphoglycerate mutase deficiency
2. グルコースおよびグリコーゲン代謝の遺伝性疾患の概要 overview of inherited disorders of glucose and glycogen metabolism
3. 新生児における筋緊張低下を引き起こす末梢神経および筋肉の障害に関する概要 overview of peripheral nerve and muscle disorders causing hypotonia in the newborn
4. 小児における溶血性貧血の概要 overview of hemolytic anemias in children
5. 代謝性ミオパチーへのアプローチ approach to the metabolic myopathies

English Journal

Long-term and stable correction of uremic anemia by intramuscular injection of plasmids containing hypoxia-regulated system of Epo expression.

Sun J, Wang Y, Yang J, Du D, Li Z, Wei J, Yang A.AbstractAims: Relative deficiency in production of glycoprotein hormone erythropoietin (Epo) is a major cause of renal anemia. This study planned to investigate whether the hypoxia-regulated system of Epo expression, constructed by fusing Epo gene to the chimeric phosphoglycerate kinase (PGK) hypoxia response elements (HRE) in combination with cytomegalovirus immediate-early (CMV IE) basal gene promoter and delivered by plasmid intramuscular injection, might provide a long-term physiologically regulated Epo secretion expression to correct the anemia in adenine-induced uremic rats. Methods: Plasmid vectors (pHRE-Epo) were synthesized by fusing human Epo cDNA to the HRE/CMV promoter. Hypoxia-inducible activity of this promoter was evaluated first in vitro and then in vivo in healthy and uremic rats (n = 30 per group). The vectors (pCMV-Epo) in which Epo expression was directed by a constitutive CMV gene promoter served as control. ANOVA and Student's t-test were used to analyze between-group differences. Results: A high-level expression of Epo was induced by hypoxia in vitro and in vivo. Though both pHRE-Epo and pCMV-Epo corrected anemia, the hematocrit of the pCMV-Epo-treated rats exceeded the normal (P<0.05), but that of the pHRE-Epo-treated rats didn't. Conclusions: Hypoxia-regulated system of Epo gene expression constructed by fusing Epo to the HRE/CMV promoter and delivered by plasmid intramuscular injection may provide a long-term and stable Epo expression and secretion in vivo to correct the anemia in adenine-induced uremic rats.
Experimental & molecular medicine.Exp Mol Med.2012 Sep 18. [Epub ahead of print]
Aims: Relative deficiency in production of glycoprotein hormone erythropoietin (Epo) is a major cause of renal anemia. This study planned to investigate whether the hypoxia-regulated system of Epo expression, constructed by fusing Epo gene to the chimeric phosphoglycerate kinase (PGK) hypoxia respon
PMID 22990115

Correction of brain oligodendrocytes by AAVrh.10 intracerebral gene therapy in metachromatic leukodystrophy mice.

Piguet F, Sondhi D, Piraud M, Fouquet F, Hackett NR, Ahouansou O, Vanier MT, Bieche I, Aubourg P, Crystal RG, Cartier N, Sevin C.SourceINSERM U745, University Paris-Descartes, 75005, Paris, France.
Human gene therapy.Hum Gene Ther.2012 Aug;23(8):903-14. doi: 10.1089/hum.2012.015. Epub 2012 Jul 23.
Metachromatic leukodystrophy (MLD) is a lysosomal storage disorder characterized by accumulation of sulfatides in glial cells and neurons, the result of an inherited deficiency of arylsulfatase A (ARSA; EC 3.1.6.8) and myelin degeneration in the central and peripheral nervous systems. No effective t
PMID 22642214

Japanese Journal

筋型 phosphoglycerate kinase (PGK) 欠損症の生化学的及び遺伝子変異の検討

日本先天代謝異常学会雑誌 15(2), 181, 1999-10-22
NAID 10018938764

｀１´Ｈ，｀３１´Ｐ‐ｍａｇｎｅｔｉｃ　ｒｅｓｏｎａｎｃｅ　ｓｐｅｃｔｒｏｓｃｏｐｙ（ＭＲＳ）による筋型糖原病ｐｈｏｓｐｈｏｇｌｙｃｅｒａｔｅ‐ｋｉｎａｓｅ（ＰＧＫ）欠損症の阻血下運動における生化学的動態の検討

脳と発達 24(3), 244-249, 1992
NAID 130004182744

酵素異常症の分子レベルでの解明　　ホスホグリセリン酸キナーゼ異常症を中心として:—ホスホグリセリン酸キナーゼ異常症を中心として—

臨床血液 27(7), 1123-1130, 1986
NAID 130004918428

Related Pictures

★リンクテーブル★

リンク元	「ホスホグリセリン酸キナーゼ欠損症」
拡張検索	「muscle phosphoglycerate kinase deficiency syndrome」
関連記事	「deficiency」「kinase」「phosphoglycerate」

「ホスホグリセリン酸キナーゼ欠損症」

Phosphoglycerate kinase
	Structure of yeast phosphoglycerate kinase.
Identifiers
Symbol	PGK
Pfam	PF00162
InterPro	IPR001576
PROSITE	PDOC00102
SCOP	3pgk
SUPERFAMILY	3pgk
Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

Search
PMC	articles
PubMed	articles
NCBI	proteins

Phosphoglycerate kinase
Identifiers
EC number	2.7.2.3
CAS number	9001-83-6
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / EGO
Search
PMC	articles
PubMed	articles
NCBI	proteins

　　[★]

英: phosphoglycerate kinase deficiency
同: PGK欠損症 PGK deficiency、ホスホグリセリン酸キナーゼ欠乏症？、phosphoglycerate kinase欠乏症
同: PGK deficiency

[show details]

ホスホグリセリン酸キナーゼ欠乏症 : 14 件
ホスホグリセリン酸キナーゼ欠損症 : 27 件

ホスホグリセリン酸キナーゼ欠乏症 deficiency : 15 件
ホスホグリセリン酸キナーゼ欠損症 deficiency : 16 件

「muscle phosphoglycerate kinase deficiency syndrome」

　　[★] 筋ホスホグリセリン酸キナーゼ欠損症候群

「deficiency」

　　[★]

n.

不足、欠乏、欠失、欠如、欠損、不十分。栄養不足、栄養素欠乏、欠乏症。(遺伝子)(染色体内の)遺伝子欠失
欠けているもの、不足している物。不足分。不完全なもの、欠点のあるもの

関: absence, agenesis, dearth, defect, defective, deficient, deficit, delete, deletion, deletional, depletion, deprivation, deprive, lack, miss, missing, morphological defect, paucity, scarce, scarcity, starve

「kinase」

　　[★] キナーゼカイネースリン酸化酵素 phosphoenzyme phosphotransferase 　

「phosphoglycerate」

　　[★]

ホスホグリセリン酸

[WikiPathways-5] The interactive pathway map can be edited at WikiPathways: "GlycolysisGluconeogenesis_WP534".

[pmid6765200-1] Watson HC, Walker NP, Shaw PJ et al. (1982). "Sequence and structure of yeast phosphoglycerate kinase". EMBO J. 1 (12): 1635–40. PMC 553262. PMID 6765200.

[Chiarelli2012-2] ^ ^a ^b ^c ^d ^e ^f Chiarelli LR, Morera SM, Bianchi P, Fermo E, Zanella A, Galizzi A, Valentini G (2012). "Molecular insights on pathogenic effects of mutations causing phosphoglycerate kinase deficiency". PLoS ONE 7 (2): e32065. doi:10.1371/journal.pone.0032065. PMC 3279470. PMID 22348148.

[Hogg-3] Hogg, Philip J.; Lay, Angelina J.; Jiang, Xing-Mai; Kisker, Oliver; Flynn, Evelyn; Underwood, Anne; Condron, Rosemary (14 December 2000). Nature 408 (6814): 869–873. doi:10.1038/35048596. Missing or empty |title= (help); |accessdate= requires |url= (help)

[4] Danshina, Polina; GB Geyer; Q Dai; EH Goulding; WD Willis et al. (1 January 2010). "Phosphoglycerate Kinase 2 (PGK2) Is Essential for Sperm Function and Male Fertility in Mice". Biology of Reproduction 82 (1): 136–145. doi:10.1095/biolreprod.109.079699.

[Dhar-6] Dhar, A.; Samiotakis, A.; Ebbinghaus, S.; Nienhaus, L.; Homouz, D.; Gruebele, M.; Cheung, M. S. (4 October 2010). "Structure, function, and folding of phosphoglycerate kinase are strongly perturbed by macromolecular crowding". Proceedings of the National Academy of Sciences 107 (41): 17586–17591. doi:10.1073/pnas.1006760107. |accessdate= requires |url= (help)

[pmid10593256-7] Kumar S, Ma B, Tsai CJ, Wolfson H, Nussinov R (1999). "Folding funnels and conformational transitions via hinge-bending motions". Cell Biochem. Biophys. 31 (2): 141–64. doi:10.1007/BF02738169. PMID 10593256.

[pmid2124145-8] Yon JM, Desmadril M, Betton JM, Minard P, Ballery N, Missiakas D, Gaillard-Miran S, Perahia D, Mouawad L (1990). "Flexibility and folding of phosphoglycerate kinase". Biochimie 72 (6-7): 417–29. doi:10.1016/0300-9084(90)90066-p. PMID 2124145.

[Zerrad11-9] Zerrad L, Merli A, Schröder GF, Varga A, Gráczer É, Pernot P, Round A, Vas M, Bowler MW (April 2011). "A spring-loaded release mechanism regulates domain movement and catalysis in phosphoglycerate kinase". J. Biol. Chem. 286 (16): 14040–8. doi:10.1074/jbc.M110.206813. PMC 3077604. PMID 21349853.

[Varga-10] Varga, Andrea; Palmai, Zoltan; Gugolya, Zoltán; Gráczer, Éva; Vonderviszt, Ferenc; Závodszky, Péter; Balog, Erika; Vas, Mária (21 December 2012). "Importance of Aspartate Residues in Balancing the Flexibility and Fine-Tuning the Catalysis of Human 3-Phosphoglycerate Kinase". Biochemistry 51 (51): 10197–10207. doi:10.1021/bi301194t. |accessdate= requires |url= (help)

[11] Cliff, MJ; Bowler MW; Varga A; Marston JP et al. (12 May 2010). "Transition state analogue structures of human phosphoglycerate kinase establish the importance of charge balance in catalysis". J Am Chem Soc 132 (18): 6507–6516. doi:10.1021/ja100974t. PMID 20397725. Retrieved 6 March 2013.

[12] Banks, R. D.; Blake, C. C. F.; Evans, P. R.; Haser, R.; Rice, D. W.; Hardy, G. W.; Merrett, M.; Phillips, A. W. (28 June 1979). "Sequence, structure and activity of phosphoglycerate kinase: a possible hinge-bending enzyme". Nature 279 (5716): 773–777. doi:10.1038/279773a0.

[13] "Phosphoglycerate kinase". Mechanism, Annotation and Classification In Enzymes (MACiE). Retrieved 4 March 2013.

[14] Bernstein, Bradley E; Wim G; Hol J (17 March 1998). "Crystal structures of substrates and products bound to the phosphoglycerate kinase active site reveal the catalytic mechanism". Biochemistry 37 (13): 4429–4436. doi:10.1021/bi9724117. |accessdate= requires |url= (help)

[LarssonR-1967-15] Larsson-Raźnikiewicz M (January 1967). "Kinetic studies on the reaction catalyzed by phosphoglycerate kinase. II. The kinetic relationships between 3-phosphoglycerate, MgATP2-and activating metal ion". Biochim. Biophys. Acta 132 (1): 33–40. doi:10.1016/0005-2744(67)90189-1. PMID 6030358.

[Varga_nuc-16] Varga, A; Chaloin K; Sagi G; Sendula R et al. (20 April 2011). "Nucleotide promiscuity of 3-phosphoglycerate kinase is in focus: implications for the design of better anti-HIV analogues". Mol Biosyst 7 (6): 1863–73. doi:10.1039/c1mb05051f. PMID 21505655. |accessdate= requires |url= (help)

[17] Larsson-Raźnikiewicz, Märtha; Wiksell, Eva (1 March 1978). "Inhibition of phosphoglycerate kinase by salicylates". Biochimica et Biophysica Acta (BBA) - Enzymology 523 (1): 94–100. doi:10.1016/0005-2744(78)90012-8. |accessdate= requires |url= (help)

[pmid6689547-18] Yoshida A, Tani K (1983). "Phosphoglycerate kinase abnormalities: functional, structural and genomic aspects". Biomed. Biochim. Acta 42 (11-12): S263–7. PMID 6689547.

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[Rhodes_bone_marrow-20] Rhodes, Melissa; Ashford, Linda; Manes, Becky; Calder, Cassie; Domm, Jennifer; Frangoul, Haydar (1 February 2011). "Bone marrow transplantation in phosphoglycerate kinase (PGK) deficiency". British Journal of Haematology 152 (4): 500–502. doi:10.1111/j.1365-2141.2010.08474.x.

[21] Zieker, Derek; Königsrainer, Ingmar; Tritschler, Isabel; Löffler, Markus; Beckert, Stefan; Traub, Frank; Nieselt, Kay; Bühler, Sarah; Weller, Michael; Gaedcke, Jochen; Taichman, Russell S.; Northoff, Hinnak; Brücher BL; Königsrainer, Alfred (1 January 2010). "Phosphoglycerate kinase 1 a promoting enzyme for peritoneal dissemination in gastric cancer". International Journal of Cancer: NA–NA. doi:10.1002/ijc.24835. |accessdate= requires |url= (help)

[22] Gallois-Mantbrun, Sarah; Faraj A; Seclaman E; Sommadossi JP et al. (1 November 2004). "Broad specificity of human phosphoglycerate kinase for antiviral nucleoside analogs". Biochemical Pharmacology 68 (9): 1749–1756. doi:10.1016/j.bcp.2004.06.012. PMID 15450940.

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phosphoglycerate kinase deficiency