Phosphoglycolate phosphatase

Last updated
Phosphoglycolate Phosphatase
Phosphoglycolate Phosphatase.png
Structure of the phosphoglycolate phosphatase dimer with attached Ca2+ (blue) and FMT (yellow), generated from 1L6R
Identifiers
EC no. 3.1.3.18
CAS no. 9025-76-7
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 / QuickGO
Search
PMC articles
PubMed articles
NCBI proteins

Phosphoglycolate phosphatase(EC 3.1.3.18; systematic name 2-phosphoglycolate phosphohydrolase), also commonly referred to as phosphoglycolate hydrolase, 2-phosphoglycolate phosphatase, P-glycolate phosphatase, and phosphoglycollate phosphatase, is an enzyme responsible for catalyzing the conversion of 2-phosphoglycolate into glycolate and phosphate:

Contents

2-phosphoglycolate + H2O = glycolate + phosphate

First studied and purified within plants, phosphoglycolate phosphatase plays a major role in photorespiratory 2-phosphoglycolate metabolism, an essential pathway for photosynthesis in plants. The occurrence of photorespiration in plants, due to the lack of substrate specificity of rubisco, leads to the formation of 2-phosphoglycolate and 3-phosphoglycerate. 3-phosphogylcerate is the normal product of carboxylation and will enter the Calvin cycle. Phosphoglycolate, which is a potent inhibitor of phosphofructokinase and triosephosphate isomerase, must be quickly metabolized and transformed into a useful substrate, and phosphoglycolate phosphatase catalyzes the first step in the regeneration of 3-phosphoglycerate from 2-phosphoglycolate at the expense of energy in the form of ATP.

Since the discovery of its activity in plants, it has been purified within human cells and implicated in 2,3-DPG regulation.

Structure

The structural characterization of phosphoglycolate phosphatase from Thermoplasma acidophilum (PDB 1L6R, pictured) revealed the monomer of the dimeric enzyme (indicated by the light blue and green coloring) includes two distinct domains, a smaller cap domain and a larger core domain. While the topology of the large domain is conserved, there is structural variation of the smaller domain. The active site of the protein is a continuous tunnel through the monomer and is lined with acidic residues, a feature consistent with other acid phosphatases. In addition, electrostatic surface analysis indicates a relatively acidic surface. [1]

Active site and

The crystallization of phosphoglycolate phosphatase from Thermoplasma acidophilum revealed 5 active sites indicated by the blue spheres in the image. The key residues of the active site are aspartate, lysine, and serine. [1]

Mechanism

This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds.

Reaction mechanism of phosphoglycolate phosphatase: 2-phosphoglycolate + H2O = glycolate + phosphate Phosphoglycolate Phosphatase Mechanism.png
Reaction mechanism of phosphoglycolate phosphatase:
     2-phosphoglycolate + H2O ⇌ glycolate + phosphate

The hydrolysis of phosphoglycolate begins with the nucleophilic attack by an aspartate residue on the electrophilic phosphorus of the phosphoglycolate. The susceptibility of the bond between phosphate and glycolate is heightened by two key interactions. An interaction with the cofactor, Mg2+, helps polarize the phosphate-oxygen bond and therefore increases the electrophilicity of the phosphorus atom. The other interaction of the phosphate with serine and lysine residues further increases the electrophilicity of the phosphorus atom. In addition, the Mg2+ also orients the nucleophilic aspartate. [1]

The loss of the phosphate glycolate bond causes the nucleophilic aspartate to be phosphorylated, producing the enzyme intermediate, [2] while glycolate is released from the active site. The interaction of the phosphorylated intermediate is stabilized by an interaction between the phosphate and a lysine residue. The Mg2+ located in the active site activates a water molecule to produce an hydroxide ion, which then hydrolyzes the phosphorylated aspartate and regenerates an active enzyme while releasing phosphate.

Function

Plants

It was previously believed that the evolution of the photorespiratory glycolate mechanism that involves phosphoglycolate phosphatase was essential for photosynthesis in more complex plants and unnecessary for cyanobacteria because of their ability to concentrate CO2 and therefore, avoid photorespiration, similar to C4 plants. However, the finding of three different phosphoglycolate metabolism pathways within the model cyanobacterium Synechocystis sp. strain PCC 6803 implicates that cyanobacteria were not only the evolutionary origin of oxygenic photosynthesis but also ancient photorespiratory phosphoglycolate metabolism, which might have been conveyed endosymbiotically to plants. [3] [4]

Drawing on earlier research that indicated the presence of phosphoglycolic acid in algae through labeling of C14O2 and P28-orthophosphate, Richardson & Tolbert were the first to find a phosphatase activity specific for phosphoglycolate in tobacco leaves. [5] The pH optimum of the enzyme is 6.3, and Mg2+ or Mn2+ ions as cofactors were necessary for activity. Mg2+ has been consistently noted to yield the maximum turnover rate. In other studies, Co2+ could also act as a divalent cofactor. In addition, Ca2+, despite being divalent, inhibits phosphoglycolate phosphatase on levels of greater than 90% of its enzymatic activity by acting as a competitive inhibitor to Mg2+. [6] Finally, Cl− can activate at low concentrations (up to 50mM), but at high concentrations, chloride ions will act as competitive inhibitors with respect to phosphoglycolate. [1] The enzyme localizes to the chloroplast, and plant studies, involving C14O2 fixation in the light, identified labeled glycolate outside of the chloroplast, suggesting that the activity of phosphoglycolate phosphatase allows the movement of glycolate out of the chloroplast. [7]

When a photorespiratory mutant of the eukaryotic green alga Chlamydomonas reinhardtii was studied, the mutant strain was identified with a conditional lethal growth phenotype that required elevated concentrations of CO2 for growth. The observation of large phosphoglycolate accumulation and the absence of glycolate accumulation ruled out the possible cause of the absence or mutation of the CO2-concentrating mechanism and indicated that phosphoglycolate phosphatase was most likely absent or deficient. The study concluded that the mutant phenotype arose from a phosphoglycolate phosphatase deficiency caused by a single-gene, nuclear mutation, which they subsequently named pgp1. [8] The deficiency inhibited the photorespiratory metabolic pathway, and the subsequent buildup of phosphoglycolate inhibited the Calvin Cycle. [9]

Since this initial study, three putative Phosphoglycolate phosphatase genes have been identified, PGP1, PGP2, and PGP3. Ensuing studies 20 years after the identification of the same mutant strain of Chlamydomonas reinhardtii found that the conditional lethal phenotype was no longer present despite the continued presence of the splice mutation of pgp1. Explanation of this occurrence concluded that the PGP2 gene was upregulated and most likely contributed to the phenotypic reversion in the pgp1 mutant. [10]

Arabidopsis thaliana is the only plant with a known set of well-defined photorespiratory mutants. [11] One of the is a knockout mutant that is devoid of 2PG phosphatase (PGLP). A high level of CO2 (1%), for example, is required for normal growth of those mutants. [11] In normal low CO2 conditions, growth is strongly impaired. [11]

Mammalian

Partial purification analysis has shown that human erythrocytes contain phosphoglycolate phosphatase as a cytoplasmic dimeric enzyme with molecular weight of 72,000. Approximately 5% of the enzyme's total activity is membrane-associated. It shows optimum pH of 6.7 and has a Michaelis constant of 1 mM for phosphoglycolate. The activity of the enzyme is Mg2+-dependent. Co2+, and to a smaller extent Mn2+, may substitute for Mg2+. [12] However, it has shown that though the enzyme requires both free Mg2+ and phosphoglycolate, the Mg2+-phosphoglycolate complex has inhibitory effects on enzymatic activity. [13]

In 1977, Badwey first demonstrated phosphoglycolate phosphatase activity in human erythrocytes and speculated that the enzyme's activity may function to protect red cells from inadvertently formed phosphoglycolate, which is synthesized by pyruvate kinase. [14] The implication of phosphoglycolate phosphatase's role in human red blood cells was discovered when its substrate, phosphoglycolate, was shown to be a potent activator of the enzyme 2,3-bisphosphoglycerate phosphatase(2,3-DPG), another hydrolase which catalyzes the metabolic reaction of 2,3-bisphosphoglycerate to 3-phosphoglycerate. In the presence of 0.02 mM phosphoglycolate, the phosphatase activity of 2,3-DPG is activated more than 1000-fold. [15]

The implication of phosphoglycolate phosphatase in the regulation of 2,3-PGA suggests the importance of having a functional version of the enzyme. In all animal tissues, 2,3-PGA is important as the cofactor of the glycolytic enzyme, phosphoglycerate mutase. [15] More important, the synthesis and breakdown of 2,3-PGA is critical to regulation of hemoglobin's binding affinity to oxygen, and an increase in its concentration leads to increased tissue oxygenation while a decrease may lead to tissue hypoxia. Therefore, the activation of the enzyme responsible for the metabolic breakdown of 2,3-PGA by phosphoglycolate could implicate phosphoglycolate phosphatase in the regulation of 2,3-PGA concentrations. [16]

Human

Phosphoglycolate phosphatase exhibits electrophoretically distinctive variant forms. Found in all human tissues, including red cells, lymphocytes, and cultured fibroblasts, the highest enzymatic activity was noted within skeletal and cardiac muscle. Research into the genetic polymorphism indicates that PGP is likely determined by three alleles at a single autosomal locus, which is expressed in all human tissues. Preliminary observations of fetal tissue suggest that the PGP locus is also fully expressed during intrauterine life. Initial research has also shown appreciable genetic variation indicated by the detection of 6 phenotypes within a small European population. [17]

Related Research Articles

<span class="mw-page-title-main">Glycolysis</span> Catabolic pathway

Glycolysis is the metabolic pathway that converts glucose into pyruvate, and in most organisms, occurs in the liquid part of cells, the cytosol. The free energy released in this process is used to form the high-energy molecules adenosine triphosphate (ATP) and reduced nicotinamide adenine dinucleotide (NADH). Glycolysis is a sequence of ten reactions catalyzed by enzymes.

<span class="mw-page-title-main">RuBisCO</span> Key enzyme of the photosynthesis involved in carbon fixation

Ribulose-1,5-bisphosphate carboxylase/oxygenase, commonly known by the abbreviations RuBisCo, rubisco, RuBPCase, or RuBPco, is an enzyme involved in light-independent part of photosynthesis, including the carbon fixation by which atmospheric carbon dioxide is converted by plants and other photosynthetic organisms to energy-rich molecules such as glucose. It emerged approximately four billion years ago in primordial metabolism prior to the presence of oxygen on earth. It is probably the most abundant enzyme on Earth. In chemical terms, it catalyzes the carboxylation of ribulose-1,5-bisphosphate.

<span class="mw-page-title-main">Pyrenoid</span> Organelle found within the chloroplasts of algae and hornworts

Pyrenoids are sub-cellular micro-compartments found in chloroplasts of many algae, and in a single group of land plants, the hornworts. Pyrenoids are associated with the operation of a carbon-concentrating mechanism (CCM). Their main function is to act as centres of carbon dioxide (CO2) fixation, by generating and maintaining a CO2 rich environment around the photosynthetic enzyme ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO). Pyrenoids therefore seem to have a role analogous to that of carboxysomes in cyanobacteria.

<span class="mw-page-title-main">Photorespiration</span> Process in plant metabolism

Photorespiration (also known as the oxidative photosynthetic carbon cycle or C2 cycle) refers to a process in plant metabolism where the enzyme RuBisCO oxygenates RuBP, wasting some of the energy produced by photosynthesis. The desired reaction is the addition of carbon dioxide to RuBP (carboxylation), a key step in the Calvin–Benson cycle, but approximately 25% of reactions by RuBisCO instead add oxygen to RuBP (oxygenation), creating a product that cannot be used within the Calvin–Benson cycle. This process lowers the efficiency of photosynthesis, potentially lowering photosynthetic output by 25% in C3 plants. Photorespiration involves a complex network of enzyme reactions that exchange metabolites between chloroplasts, leaf peroxisomes and mitochondria.

C<sub>3</sub> carbon fixation Most common pathway in photosynthesis

C3 carbon fixation is the most common of three metabolic pathways for carbon fixation in photosynthesis, the other two being C4 and CAM. This process converts carbon dioxide and ribulose bisphosphate (RuBP, a 5-carbon sugar) into two molecules of 3-phosphoglycerate through the following reaction:

<i>Chlamydomonas reinhardtii</i> Species of alga

Chlamydomonas reinhardtii is a single-cell green alga about 10 micrometres in diameter that swims with two flagella. It has a cell wall made of hydroxyproline-rich glycoproteins, a large cup-shaped chloroplast, a large pyrenoid, and an eyespot that senses light.

<span class="mw-page-title-main">Calvin cycle</span> Light-independent reactions in photosynthesis

The Calvin cycle,light-independent reactions, bio synthetic phase,dark reactions, or photosynthetic carbon reduction (PCR) cycle of photosynthesis is a series of chemical reactions that convert carbon dioxide and hydrogen-carrier compounds into glucose. The Calvin cycle is present in all photosynthetic eukaryotes and also many photosynthetic bacteria. In plants, these reactions occur in the stroma, the fluid-filled region of a chloroplast outside the thylakoid membranes. These reactions take the products of light-dependent reactions and perform further chemical processes on them. The Calvin cycle uses the chemical energy of ATP and reducing power of NADPH from the light dependent reactions to produce sugars for the plant to use. These substrates are used in a series of reduction-oxidation reactions to produce sugars in a step-wise process; there is no direct reaction that converts several molecules of CO2 to a sugar. There are three phases to the light-independent reactions, collectively called the Calvin cycle: carboxylation, reduction reactions, and ribulose 1,5-bisphosphate (RuBP) regeneration.

<span class="mw-page-title-main">2,3-Bisphosphoglyceric acid</span> Chemical compound

2,3-Bisphosphoglyceric acid (2,3-BPG), also known as 2,3-diphosphoglyceric acid (2,3-DPG), is a three-carbon isomer of the glycolytic intermediate 1,3-bisphosphoglyceric acid (1,3-BPG).

<span class="mw-page-title-main">Phosphoenolpyruvate carboxylase</span> Class of enzymes

Phosphoenolpyruvate carboxylase (also known as PEP carboxylase, PEPCase, or PEPC; EC 4.1.1.31, PDB ID: 3ZGE) is an enzyme in the family of carboxy-lyases found in plants and some bacteria that catalyzes the addition of bicarbonate (HCO3−) to phosphoenolpyruvate (PEP) to form the four-carbon compound oxaloacetate and inorganic phosphate:

<span class="mw-page-title-main">Bisphosphoglycerate mutase</span> Enzyme

Bisphosphoglycerate mutase is an enzyme expressed in erythrocytes and placental cells. It is responsible for the catalytic synthesis of 2,3-Bisphosphoglycerate (2,3-BPG) from 1,3-bisphosphoglycerate. BPGM also has a mutase and a phosphatase function, but these are much less active, in contrast to its glycolytic cousin, phosphoglycerate mutase (PGM), which favors these two functions, but can also catalyze the synthesis of 2,3-BPG to a lesser extent.

<span class="mw-page-title-main">Phosphoglycerate mutase</span> Class of enzymes

Phosphoglycerate mutase (PGM) is any enzyme that catalyzes step 8 of glycolysis - the internal transfer of a phosphate group from C-3 to C-2 which results in the conversion of 3-phosphoglycerate (3PG) to 2-phosphoglycerate (2PG) through a 2,3-bisphosphoglycerate intermediate. These enzymes are categorized into the two distinct classes of either cofactor-dependent (dPGM) or cofactor-independent (iPGM). The dPGM enzyme is composed of approximately 250 amino acids and is found in all vertebrates as well as in some invertebrates, fungi, and bacteria. The iPGM class is found in all plants and algae as well as in some invertebrate, fungi, and Gram-positive bacteria. This class of PGM enzyme shares the same superfamily as alkaline phosphatase.

<span class="mw-page-title-main">Biohydrogen</span>

Biohydrogen is H2 that is produced biologically. Interest is high in this technology because H2 is a clean fuel and can be readily produced from certain kinds of biomass, including biological waste. Furthermore some photosynthetic microorganisms are capable to produce H2 directly from water splitting using light as energy source.

<span class="mw-page-title-main">UTP—glucose-1-phosphate uridylyltransferase</span> Class of enzymes

UTP—glucose-1-phosphate uridylyltransferase also known as glucose-1-phosphate uridylyltransferase is an enzyme involved in carbohydrate metabolism. It synthesizes UDP-glucose from glucose-1-phosphate and UTP; i.e.,

Glucose-1,6-bisphosphate synthase is a type of enzyme called a phosphotransferase and is involved in mammalian starch and sucrose metabolism. It catalyzes the transfer of a phosphate group from 1,3-bisphosphoglycerate to glucose-1-phosphate, yielding 3-phosphoglycerate and glucose-1,6-bisphosphate.

<span class="mw-page-title-main">Glyoxylate reductase</span> Enzyme

Glyoxylate reductase, first isolated from spinach leaves, is an enzyme that catalyzes the reduction of glyoxylate to glycolate, using the cofactor NADH or NADPH.

<span class="mw-page-title-main">Phosphoribulokinase</span>

Phosphoribulokinase (PRK) (EC 2.7.1.19) is an essential photosynthetic enzyme that catalyzes the ATP-dependent phosphorylation of ribulose 5-phosphate (RuP) into ribulose 1,5-bisphosphate (RuBP), both intermediates in the Calvin Cycle. Its main function is to regenerate RuBP, which is the initial substrate and CO2-acceptor molecule of the Calvin Cycle. PRK belongs to the family of transferase enzymes, specifically those transferring phosphorus-containing groups (phosphotransferases) to an alcohol group acceptor. Along with ribulose 1,5-bisphosphate carboxylase/oxygenase (RuBisCo), phosphoribulokinase is unique to the Calvin Cycle. Therefore, PRK activity often determines the metabolic rate in organisms for which carbon fixation is key to survival. Much initial work on PRK was done with spinach leaf extracts in the 1950s; subsequent studies of PRK in other photosynthetic prokaryotic and eukaryotic organisms have followed. The possibility that PRK might exist was first recognized by Weissbach et al. in 1954; for example, the group noted that carbon dioxide fixation in crude spinach extracts was enhanced by the addition of ATP. The first purification of PRK was conducted by Hurwitz and colleagues in 1956.

ATP + Mg2+ - D-ribulose 5-phosphate  ADP + D-ribulose 1,5-bisphosphate
<span class="mw-page-title-main">Haloacid dehydrogenase superfamily</span>

The haloacid dehydrogenase superfamily is a superfamily of enzymes that include phosphatases, phosphonatases, P-type ATPases, beta-phosphoglucomutases, phosphomannomutases, and dehalogenases, and are involved in a variety of cellular processes ranging from amino acid biosynthesis to detoxification.

<span class="mw-page-title-main">PGAM2</span> Protein-coding gene in the species Homo sapiens

Phosphoglycerate mutase 2 (PGAM2), also known as muscle-specific phosphoglycerate mutase (PGAM-M), is a phosphoglycerate mutase that, in humans, is encoded by the PGAM2 gene on chromosome 7.

<span class="mw-page-title-main">Kinetic isotope effects of RuBisCO</span>

The kinetic isotope effect (KIE) of ribulose-1,5-bisphosphate carboxylase oxygenase (RuBisCO) is the isotopic fractionation associated solely with the step in the Calvin-Benson cycle where a molecule of carbon dioxide is attached to the 5-carbon sugar ribulose-1,5-bisphosphate (RuBP) to produce two 3-carbon sugars called 3-phosphoglycerate. This chemical reaction is catalyzed by the enzyme RuBisCO, and this enzyme-catalyzed reaction creates the primary kinetic isotope effect of photosynthesis. It is also largely responsible for the isotopic compositions of photosynthetic organisms and the heterotrophs that eat them. Understanding the intrinsic KIE of RuBisCO is of interest to earth scientists, botanists, and ecologists because this isotopic biosignature can be used to reconstruct the evolution of photosynthesis and the rise of oxygen in the geologic record, reconstruct past evolutionary relationships and environmental conditions, and infer plant relationships and productivity in modern environments.

<span class="mw-page-title-main">2-Phosphoglycolate</span> Chemical compound

2-Phosphoglycolate (chemical formula C2H2O6P3-; also known as phosphoglycolate, 2-PG, or PG) is a natural metabolic product of the oxygenase reaction mediated by the enzyme ribulose 1,5-bisphosphate carboxylase (RuBisCo).

References

  1. 1 2 3 4 Kim Y, Yakunin AF, Kuznetsova E, Xu X, Pennycooke M, Gu J, Cheung F, Proudfoot M, Arrowsmith CH, Joachimiak A, Edwards AM, Christendat D (January 2004). "Structure- and function-based characterization of a new phosphoglycolate phosphatase from Thermoplasma acidophilum". The Journal of Biological Chemistry. 279 (1): 517–26. doi: 10.1074/jbc.M306054200 . PMC   2795321 . PMID   14555659.
  2. ↑ Christeller JT, Tolbert NE (March 1978). "Mechanism of phosphoglycolate phosphatase. Studies of hydrolysis and transphosphorylation, substrate analogs, and sulfhydryl inhibition". The Journal of Biological Chemistry. 253 (6): 1791–8. doi: 10.1016/S0021-9258(19)62323-9 . PMID   204631.
  3. ↑ Eisenhut M, Ruth W, Haimovich M, Bauwe H, Kaplan A, Hagemann M (November 2008). "The photorespiratory glycolate metabolism is essential for cyanobacteria and might have been conveyed endosymbiontically to plants". Proceedings of the National Academy of Sciences of the United States of America. 105 (44): 17199–204. Bibcode:2008PNAS..10517199E. doi: 10.1073/pnas.0807043105 . PMC   2579401 . PMID   18957552.
  4. ↑ Hagemann M, Eisenhut M, Hackenberg C, Bauwe H (2010-01-01). "Pathway and Importance of Photorespiratory 2-Phosphoglycolate Metabolism in Cyanobacteria". Recent Advances in Phototrophic Prokaryotes. Advances in Experimental Medicine and Biology. Vol. 675. pp. 91–108. doi:10.1007/978-1-4419-1528-3_6. ISBN   978-1-4419-1527-6. PMID   20532737.
  5. ↑ Richardson KE, Tolbert NE (May 1961). "Phosphoglycolic acid phosphatase". The Journal of Biological Chemistry. 236 (5): 1285–90. doi: 10.1016/S0021-9258(18)64166-3 . PMID   13741300.
  6. ↑ Mamedov TG, Suzuki K, Miura K, Kucho Ki K, Fukuzawa H (December 2001). "Characteristics and sequence of phosphoglycolate phosphatase from a eukaryotic green alga Chlamydomonas reinhardtii". The Journal of Biological Chemistry. 276 (49): 45573–9. doi: 10.1074/jbc.M103882200 . PMID   11581250.
  7. ↑ Yu YL, Tolbert NE, Orth GM (July 1964). "Isolation and Distribution of Phosphoglycolate Phosphatase". Plant Physiology. 39 (4): 643–7. doi:10.1104/pp.39.4.643. PMC   550139 . PMID   16655977.
  8. ↑ Suzuki K, Marek LF, Spalding MH (May 1990). "A photorespiratory mutant of Chlamydomonas reinhardtii". Plant Physiology. 93 (1): 231–7. doi:10.1104/pp.93.1.231. PMC   1062493 . PMID   16667440.
  9. ↑ Anderson LE, Pacold I (March 1972). "Chloroplast and Cytoplasmic Enzymes: IV. Pea Leaf Fructose 1,6-Diphosphate Aldolases". Plant Physiology. 49 (3): 393–7. doi:10.1104/pp.49.3.393. PMC   365972 . PMID   16657968.
  10. ↑ Ma Y, Hartman MM, Moroney JV (January 2013). "Transcriptional Analysis of the Three Phosphoglycolate Phosphatase Genes in Wild Type and the pgp1 Mutant of Chlamydomonas Reinhardtii". Photosynthesis Research for Food, Fuel and the Future. Advanced Topics in Science and Technology in China. Berlin Heidelberg: Springer. pp. 315–318. doi:10.1007/978-3-642-32034-7_66. ISBN   978-3-642-32033-0.
  11. 1 2 3 Timm S, Mielewczik M, Florian A, Frankenbach S, Dreissen A, Hocken N, Fernie AR, Walter A, Bauwe H (17 August 2012). "High-to-low CO2 acclimation reveals plasticity of the photorespiratory pathway and indicates regulatory links to cellular metabolism of Arabidopsis". PLOS ONE. 7 (8): e42809. Bibcode:2012PLoSO...742809T. doi: 10.1371/journal.pone.0042809 . PMC   3422345 . PMID   22912743.
  12. ↑ Zecher R, Wolf HU (October 1980). "Partial purification and characterization of human erythrocyte phosphoglycollate phosphatase". The Biochemical Journal. 191 (1): 117–24. doi:10.1042/bj1910117. PMC   1162188 . PMID   6258579.
  13. ↑ Rose ZB (May 1981). "Phosphoglycolate phosphatase from human red blood cells". Archives of Biochemistry and Biophysics. 208 (2): 602–9. doi:10.1016/0003-9861(81)90549-x. PMID   6266352.
  14. ↑ Badwey JA (April 1977). "Phosphoglycolate phosphatase in human erythrocytes". The Journal of Biological Chemistry. 252 (7): 2441–3. doi: 10.1016/S0021-9258(17)40573-4 . PMID   14966.
  15. 1 2 Rose ZB, Liebowitz J (June 1970). "2,3-diphosphoglycerate phosphatase from human erythrocytes. General properties and activation by anions". The Journal of Biological Chemistry. 245 (12): 3232–41. doi: 10.1016/S0021-9258(18)63045-5 . PMID   4317427.
  16. ↑ MacDonald R (June 1977). "Red cell 2,3-diphosphoglycerate and oxygen affinity". Anaesthesia. 32 (6): 544–53. doi: 10.1111/j.1365-2044.1977.tb10002.x . PMID   327846. S2CID   35235969.
  17. ↑ Barker RF, Hopkinson DA (October 1978). "Genetic polymorphism of human phosphoglycolate phosphatase (PGP)". Annals of Human Genetics. 42 (2): 143–51. doi:10.1111/j.1469-1809.1978.tb00644.x. PMID   215071. S2CID   24895851.
This page is based on this Wikipedia article
Text is available under the CC BY-SA 4.0 license; additional terms may apply.
Images, videos and audio are available under their respective licenses.