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Danshina, Pauline V

doi:10.1023/a:1023968028884

Cited by 9 publications

(3 citation statements)

References 14 publications

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“…The biological role of acylphosphatase is not fully understood. The enzyme hydrolyzes 1,3-bisphosphoglycerate to 3-phosphoglycerate and uncouples the ATP-generating reaction catalyzed by phosphoglycerate kinase (Harary, 1957;Ramponi et al, 1988;Raugei et al, 1996;Dan'shina et al, 2003). Its role in increasing the rate of glycolysis is further supported by the fact that the enzyme is overexpressed in tissues (e.g.…”

Section: Introductionmentioning

confidence: 99%

Crystallization and preliminary crystallographic analysis of human common-type acylphosphatase

2005

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Human acylphosphatase, an 11 kDa enzyme that catalyzes the hydrolysis of carboxyl phosphate bonds, has been studied extensively as a model system for amyloid-fibril formation. However, the structure is still not known of any isoform of human acylphosphatase. Here, the crystallization and preliminary X-ray diffraction data analysis of human common-type acylphosphatase are reported. Crystals of human common-type acylphosphatase have been grown by the sitting-drop vapour-diffusion method at 289 K using polyethylene glycol 4000 as precipitant. Diffraction data were collected to 1.45 A resolution at 100 K. The crystals belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 42.58, b = 47.23, c = 57.26 A.

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Section: Introductionmentioning

confidence: 99%

Crystallization and preliminary crystallographic analysis of human common-type acylphosphatase

2005

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“…The enzyme was shown to increase the rate of glycolysis. It hydrolyzes 1,3-bisphosphoglycerate to 3-phosphoglycerate and thereby uncouples the ATP-generating reaction catalyzed by phosphoglycerate kinase ( − ). This regulatory role of AcP on glycolysis is further supported by the fact that the enzyme is overexpressed in tissues that are very active in glycolysis (e.g., brain, heart, and skeletal muscle) ().…”

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confidence: 99%

Crystal Structure of a Hyperthermophilic Archaeal Acylphosphatase from Pyrococcus horikoshiiStructural Insights into Enzymatic Catalysis, Thermostability, and Dimerization^,

et al. 2005

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Acylphosphatases catalyze the hydrolysis of the carboxyl-phosphate bond in acyl phosphates. Although acylphosphatase-like sequences are found in all three domains of life, no structure of acylphosphatase has been reported for bacteria and archaea so far. Here, we report the characterization of enzymatic activities and crystal structure of an archaeal acylphosphatase. A putative acylphosphatase gene (PhAcP) was cloned from the genomic DNA of Pyrococcus horikoshii and was expressed in Escherichia coli. Enzymatic parameters of the recombinant PhAcP were measured using benzoyl phosphate as the substrate. Our data suggest that, while PhAcP is less efficient than other mammalian homologues at 25 degrees C, the thermophilic enzyme is fully active at the optimal growth temperature (98 degrees C) of P. horikoshii. PhAcP is extremely stable; its apparent melting temperature was 111.5 degrees C and free energy of unfolding at 25 degrees C was 54 kJ mol(-)(1). The 1.5 A crystal structure of PhAcP adopts an alpha/beta sandwich fold that is common to other acylphosphatases. PhAcP forms a dimer in the crystal structure via antiparallel association of strand 4. Structural comparison to mesophilic acylphosphatases reveals significant differences in the conformation of the L5 loop connecting strands 4 and 5. The extreme thermostability of PhAcP can be attributed to an extensive ion-pair network consisting of 13 charge residues on the beta sheet of the protein. The reduced catalytic efficiency of PhAcP at 25 degrees C may be due to a less flexible active-site residue, Arg20, which forms a salt bridge to the C-terminal carboxyl group. New insights into catalysis were gained by docking acetyl phosphate to the active site of PhAcP.

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“…The oxidative posttranslational modification of cysteine residues in the active center of GAPDH, which are very sensitive, might lead to inhibition of the enzyme. Their mild oxidation with hydrogen peroxide to sulfenic acid (-SOH) dampens GAPDH dehydrogenase activity while stimulating the acylphosphatase one [27].…”

Section: Glyceraldehyde-3-phosphate Dehydrogenasementioning

confidence: 99%

Carbonyl Stress in Red Blood Cells and Hemoglobin

2021

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The paper overviews the peculiarities of carbonyl stress in nucleus-free mammal red blood cells (RBCs). Some functional features of RBCs make them exceptionally susceptible to reactive carbonyl compounds (RCC) from both blood plasma and the intracellular environment. In the first case, these compounds arise from the increased concentrations of glucose or ketone bodies in blood plasma, and in the second—from a misbalance in the glycolysis regulation. RBCs are normally exposed to RCC—methylglyoxal (MG), triglycerides—in blood plasma of diabetes patients. MG modifies lipoproteins and membrane proteins of RBCs and endothelial cells both on its own and with reactive oxygen species (ROS). Together, these phenomena may lead to arterial hypertension, atherosclerosis, hemolytic anemia, vascular occlusion, local ischemia, and hypercoagulation phenotype formation. ROS, reactive nitrogen species (RNS), and RCC might also damage hemoglobin (Hb), the most common protein in the RBC cytoplasm. It was Hb with which non-enzymatic glycation was first shown in living systems under physiological conditions. Glycated HbA1c is used as a very reliable and useful diagnostic marker. Studying the impacts of MG, ROS, and RNS on the physiological state of RBCs and Hb is of undisputed importance for basic and applied science.

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Untitled

Cited by 9 publications

References 14 publications

Crystallization and preliminary crystallographic analysis of human common-type acylphosphatase

Crystallization and preliminary crystallographic analysis of human common-type acylphosphatase

Crystal Structure of a Hyperthermophilic Archaeal Acylphosphatase from Pyrococcus horikoshiiStructural Insights into Enzymatic Catalysis, Thermostability, and Dimerization^,

Carbonyl Stress in Red Blood Cells and Hemoglobin

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Untitled

Cited by 9 publications

References 14 publications

Crystallization and preliminary crystallographic analysis of human common-type acylphosphatase

Crystallization and preliminary crystallographic analysis of human common-type acylphosphatase

Crystal Structure of a Hyperthermophilic Archaeal Acylphosphatase from Pyrococcus horikoshiiStructural Insights into Enzymatic Catalysis, Thermostability, and Dimerization,

Carbonyl Stress in Red Blood Cells and Hemoglobin

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Crystal Structure of a Hyperthermophilic Archaeal Acylphosphatase from Pyrococcus horikoshiiStructural Insights into Enzymatic Catalysis, Thermostability, and Dimerization^,