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Liver Diseases
Published in George Feuer, Felix A. de la Iglesia, Molecular Biochemistry of Human Disease, 2020
George Feuer, Felix A. de la Iglesia
Diagnosis of primary liver cancer is mainly based on clinical observations, X-ray, or liver scan. Hepatoma cells frequently contain bilirubin, possibly because they lose the ability to conjugate and excrete this pigment. Bilirubin is retained in the tumor cells since there is no connection with bile ducts to allow for normal flow. Cholangiocarcinomas do not show bile pigment. In the serum of many hepatoma patients α-fetoglobulin is found.7,130 Hepatitis and cirrhosis patients do not have this protein. The finding of a positive test for α-fetoglobulin is of great diagnostic value. In some cases, severe metabolic abnormalities are found, including serious reductions of blood glucose, which are difficult to treat,376 and large quantities of glucose are necessary to maintain the concentration near normal. In primary human liver tumor, enzyme changes can be detected. These include glutathione S-transferase and UDP-glucuronyltransferase,489 glucose 6-phosphatase,400 intestinal-type alkaline phosphatase,609 ATP-ase,179 thymidine phosphorylase,318 prolyl hydroxylase,51 and galactosyltransferase.46 Aberrant porphyrin metabolism560 and calcitonin93 are also observed in hepatocellular carcinoma. Changes in aldolase isoenzyme pattern are found in human cancer.16 Alterations in sex steroid receptor protein are connected with malignancy of liver tissue.50,268
Biocatalysts: The Different Classes and Applications for Synthesis of APIs
Published in Peter Grunwald, Pharmaceutical Biocatalysis, 2019
These enzymes belonging to the class of lyase enzymes catalyze the formation of C–C bonds known from Organic Chemistry as the aldol-reaction. The aldolase-catalyzed reaction represents a reversible stereoselective addition of a nucleophile to an electrophile. In living cells, aldolases play a key role in degradation as well as in synthesis of carbohydrates and keto acids. Natural donors (see scheme below) of aldolases are dihydroxyacetone phosphate (DHAP), pyruvate and phosphoenol pyruvate (PEP), acetaldehyde and glycine. Several aldolases, among them KDPG and KDPGal aldolase, or N-acetyl neuraminic acid lyase (Walters and Toone, 2017; Stockwell et al., 2016) accept fluoropyruvate as an alternative donor substrate to pyruvate, a property used by Windle et al. (2017), to investigate the stereoselective synthesis of fluorinated compounds such as α-fluoro β-hydroxy carboxyl derivatives.
Human Erythroenzymopathies Of The Anaerobic Embden-Meyerhof Glycolytic And Associated Pathways
Published in Ronald L. Nagel, Genetically Abnormal Red Cells, 2019
Ernst R. Jaffé, William N. Valentine
Aldolase exists in the tissues as three isozymes,22 A, B, and C, possesses four subunits, and has a molecular weight of 58,000. It catalyzes the reversible interconversion of F-1,6-P2 and the two trioses, DHAP and G-3-P.
Pyomyositis presenting as myonecrosis secondary to methicillin-resistant Staphylococcus aureus bacteremia in chronic lymphocytic leukemia
Published in Baylor University Medical Center Proceedings, 2022
Shannon Coombs, Albert Bui, Haares S. Mirzan, Kimberly Robelin, Hillary W. Garner, Murli Krishna, Jennifer B. Cowart
Throughout the hospitalization, disseminated bacteremia with multiorgan involvement was suspected and treated accordingly. The patient’s RUE pain worsened as he developed progressive edema and weakness. There were no sensory deficits. Magnetic resonance imaging (MRI) of the right shoulder demonstrated loss of normal muscle fiber architecture and generalized edema of multiple muscles as well as large areas of nonenhancement consistent with myonecrosis (Figure 1). The patient also had an elevated aldolase at 11.5 U/L (reference range <7.7 U/L) and creatine kinase at 475 U/L (reference range 39–308 U/L). Computed tomography–guided core needle biopsy of the right posterior deltoid muscle revealed focal necrotizing inflammation in the muscle. Culture of the biopsy sample was positive for MRSA, which confirmed the diagnosis of MRSA pyomyositis (Figure 2).
Clinical guide to eosinophilic fasciitis: straddling dermatology and rheumatology
Published in Expert Review of Clinical Immunology, 2022
There are no generally accepted diagnostic criteria for EF. Pinal-Fernandez et al. [7] proposed the criteria for diagnosis and classification of EF. Two major criteria are: a. swelling, induration, and thickening of the skin and subcutaneous tissue that is symmetrical or nonsymmetrical, diffuse (involving extremities, the trunk, and abdomen), or localized (involving the extremities), b. fascial thickening with accumulation of lymphocytes and macrophages with or without eosinophilic infiltration (determined by full-thickness wedge biopsy of clinically affected skin). Five minor criteria are: a. eosinophilia >0.5 × 10 9 /L, b. hypergammaglobulinemia >1.5 g/L. c. muscle weakness and/or elevated aldolase levels, d. groove sign and/or peau d’orange, e. hyperintense fascia on MR T2-weighted images. Accordingly, two major or one major and two minor criteria are consistent with EF diagnosis.
8-Mercaptoguanine-based inhibitors of Mycobacterium tuberculosis dihydroneopterin aldolase: synthesis, in vitro inhibition and docking studies
Published in Journal of Enzyme Inhibition and Medicinal Chemistry, 2021
Alexia de Matos Czeczot, Candida Deves Roth, Rodrigo Gay Ducati, Kenia Pissinate, Raoní Scheibler Rambo, Luís Fernando Saraiva Macedo Timmers, Bruno Lopes Abbadi, Fernanda Souza Macchi, Víctor Zajaczkowski Pestana, Luiz Augusto Basso, Pablo Machado, Cristiano Valim Bizarro
The synthesised compounds 2a-h, 3a-c, and 4a-h were evaluated as inhibitors of MtFolB aldolase activity using a continuous fluorescence assay. The Michaelis–Menten constant (KM) was determined at varying concentrations of DHNP until enzyme saturation (Figure S1, Supplementary Material). KM and kcat values of 1.42 ± 0.13 µM and 0.011 ± 0.0003s−1 were obtained, respectively. The values determined here differ from the values previously reported for this enzyme (KM = 0.165 ± 0.026 µM and kcat = 0.0054 ± 0.0002s−1)9. This should be attributed to differences in the method of enzyme purification and the buffer and pH of the enzyme activity assay; changes in solution conditions can affect the apparent value of KM, influencing the ability of the enzyme to combine with substrate16.