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Relevant bibliographies by topics / Pyridoxamine 5 Phosphate (PMP)

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Academic literature on the topic 'Pyridoxamine 5 Phosphate (PMP)'

Author: Grafiati

Published: 7 June 2025

Last updated: 2 August 2025

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Journal articles on the topic "Pyridoxamine 5 Phosphate (PMP)"

1

Yang, Yong, Genshi Zhao, Tsz-Kwong Man, and Malcolm E. Winkler. "Involvement of the gapA- and epd(gapB)-Encoded Dehydrogenases in Pyridoxal 5′-Phosphate Coenzyme Biosynthesis in Escherichia coli K-12." Journal of Bacteriology 180, no. 16 (1998): 4294–99. http://dx.doi.org/10.1128/jb.180.16.4294-4299.1998.

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ABSTRACT We show that epd (gapB) mutants lacking an erythrose 4-phosphate (E4P) dehydrogenase are impaired for growth on some media and contain less pyridoxal 5′-phosphate (PLP) and pyridoxamine 5′-phosphate (PMP) than their epd +parent. In contrast to a previous report, we found that gapA epd double mutants lacking the glyceraldehyde 3-phosphate and E4P dehydrogenases are auxotrophic for pyridoxine. These results implicate the GapA and Epd dehydrogenases in de novo PLP and PMP coenzyme biosynthesis.

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Campanini, Barbara, Stefano Bettati, Martino Luigi di Salvo, Andrea Mozzarelli, and Roberto Contestabile. "Asymmetry of the Active Site Loop Conformation between Subunits of Glutamate-1-semialdehyde Aminomutase in Solution." BioMed Research International 2013 (2013): 1–10. http://dx.doi.org/10.1155/2013/353270.

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Glutamate-1-semialdehyde aminomutase (GSAM) is a dimeric, pyridoxal 5′-phosphate (PLP)- dependent enzyme catalysing in plants and some bacteria the isomerization of L-glutamate-1-semialdehyde to 5-aminolevulinate, a common precursor of chlorophyll, haem, coenzyme B12, and other tetrapyrrolic compounds. During the catalytic cycle, the coenzyme undergoes conversion from pyridoxamine 5′-phosphate (PMP) to PLP. The entrance of the catalytic site is protected by a loop that is believed to switch from an open to a closed conformation during catalysis. Crystallographic studies indicated that the stru

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Bakunova, A. K., I. O. Matyuta, A. Yu Nikolaeva, K. M. Boyko, V. O. Popov, and E. Yu Bezsudnova. "Mechanism of D-cycloserine inhibition of D-amino acid transaminase from <i>Haliscomenobacter hydrossis</i>." Биохимия 88, no. 5 (2023): 841–53. http://dx.doi.org/10.31857/s0320972523050111.

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D-cycloserine inhibits pyridoxal-5′-phosphate (PLP)-dependent enzymes. The inhibition efficiency depends on the organization of their active center and the mechanism of the catalyzed reaction. D-cycloserine interacts with the PLP form of enzyme similarly to substrate amino donor, and the interaction is predominantly reversible. Inhibition products include hydroxyisoxazole-pyridoxamine-5′-phosphate, oxime between PLP and β-aminooxy-D-alanine, ketimine between pyridoxamine-5′-phosphate and cyclic or open forms of D-cycloserine, pyridoxamine-5′-phosphate, etc. For some enzymes the formation of a

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Yanee, Trongpanich, Phimwapi Suphaporn, Niamsanit Suwanna, Wangsomnuk P. Preeya, Boonmee Mallika, and Siri Sineenart. "Isolation and characterization of bacteria capable of producing pyridoxamine (PM) and pyridoxamine 5′-phosphate (PMP), vitamin B6 compounds." Journal of General and Applied Microbiology 53, no. 5 (2007): 295–99. http://dx.doi.org/10.2323/jgam.53.295.

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Cellini, Barbara, Mariarita Bertoldi, Riccardo Montioli, Alessandro Paiardini, and Carla Borri Voltattorni. "Human wild-type alanine:glyoxylate aminotransferase and its naturally occurring G82E variant: functional properties and physiological implications." Biochemical Journal 408, no. 1 (2007): 39–50. http://dx.doi.org/10.1042/bj20070637.

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Human hepatic peroxisomal AGT (alanine:glyoxylate aminotransferase) is a PLP (pyridoxal 5′-phosphate)-dependent enzyme whose deficiency causes primary hyperoxaluria Type I, a rare autosomal recessive disorder. To acquire experimental evidence for the physiological function of AGT, the Keq,overall of the reaction, the steady-state kinetic parameters of the forward and reverse reactions, and the pre-steady-state kinetics of the half-reactions of the PLP form of AGT with L-alanine or glycine and the PMP (pyridoxamine 5′-phosphate) form with pyruvate or glyoxylate have been measured. The results i

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BERTOLDI, Mariarita, Barbara CELLINI, Alessandro PAIARDINI, Martino Di SALVO, and Carla BORRIVOLTATTORNI. "Treponema denticola cystalysin exhibits significant alanine racemase activity accompanied by transamination: mechanistic implications1." Biochemical Journal 371, no. 2 (2003): 473–83. http://dx.doi.org/10.1042/bj20020875.

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To obtain information on the reaction specificity of cystalysin from the spirochaete bacterium Treponema denticola, the interaction with l- and d-alanine has been investigated. Binding of both alanine enantiomers leads to the appearance of an external aldimine absorbing at 429nm and of a band absorbing at 498nm, indicative of a quinonoid species. Racemization and transamination reactions were observed to occur with both alanine isomers as substrates. The steady-state kinetic parameters for racemization, kcat and Km, for l-alanine are 1.05±0.03s−1 and 10±1mM respectively, whereas those for d-al

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Abbas, Sk Jahir, P. V. R. K. Ramacharyulu, and Shyue-Chu Ke. "MnO2/TiO2 catalyzed synthesis of coenzyme pyridoxamine-5′-phosphate analogues: 3-deoxypyridoxamine-5′-phosphate." RSC Advances 6, no. 13 (2016): 10242–48. http://dx.doi.org/10.1039/c5ra25779d.

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The highly efficient-selective synthetic route of the pyridoxal-5′-phosphate (vitamin B<sub>6</sub>, PLP) analogues: C3 substituted deoxy derivatives were developed via reduction and followed by selective oxidation in one pot using solid supported nanoparticles.

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PALMIERI, Gianna, Michela DI PALO, Andrea SCALONI, Stefania ORRÙ, Gennaro MARINO, and Giovanni SANNIA. "Glutamate-1-semialdehyde aminotransferase from Sulfolobus solfataricus*." Biochemical Journal 320, no. 2 (1996): 541–45. http://dx.doi.org/10.1042/bj3200541.

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Glutamate-1-semialdehyde aminotransferase (GSA-AT) from the extremely thermophilic bacterium Sulfolobus solfataricus has been purified to homogeneity and characterized. GSA-AT is the last enzyme in the C5 pathway for the conversion of glutamate into the tetrapyrrole precursor Δ-aminolaevulinate (ALA) in plants, algae and several bacteria. The active form of GSA-AT from S. solfataricus seems to be a homodimer with a molecular mass of 87 kDa. The absorption spectrum of the purified aminotransferase is indicative of the presence of pyridoxamine 5´-phosphate (PMP) cofactor, and the catalytic activ

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Dudipala, Sai C., Sagar Potharajula, Srikanth R. Pabbathi, and Krishna Chaithanya Battu. "A treatable early onset epileptic encephalopathy: pyridoxamine 5'-phosphate oxidase deficiency." International Journal of Contemporary Pediatrics 11, no. 7 (2024): 979–81. http://dx.doi.org/10.18203/2349-3291.ijcp20241688.

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Pyridox (am) ine 5'-phosphate oxidase (PNPO) deficiency is a rare epileptic encephalopathy condition due to mutations in PNPO gene. It is one of treatable metabolic epilepsies. It is unresponsive to antiseizure medications, but respond to pyridoxal-5-phosphate (PLP), active form of vitamin B6. It is characterized by refractory seizures from newborn or in utero, developmental delay. Based on refractory seizures, age of onset, negative biochemical profile and response to PLP, suspect PNPO deficiency. Next generation sequencing will help in the diagnosis. Early diagnosis and early initiation of P

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Rivero, Maribel, Nerea Novo, and Milagros Medina. "Pyridoxal 5′-Phosphate Biosynthesis by Pyridox-(am)-ine 5′-Phosphate Oxidase: Species-Specific Features." International Journal of Molecular Sciences 25, no. 6 (2024): 3174. http://dx.doi.org/10.3390/ijms25063174.

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Enzymes reliant on pyridoxal 5′-phosphate (PLP), the metabolically active form of vitamin B6, hold significant importance in both biology and medicine. They facilitate various biochemical reactions, particularly in amino acid and neurotransmitter metabolisms. Vitamin B6 is absorbed by organisms in its non-phosphorylated form and phosphorylated within cells via pyridoxal kinase (PLK) and pyridox-(am)-ine 5′-phosphate oxidase (PNPOx). The flavin mononucleotide-dependent PNPOx enzyme converts pyridoxine 5′-phosphate and pyridoxamine 5′-phosphate into PLP. PNPOx is vital for both biosynthesis and

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Dissertations / Theses on the topic "Pyridoxamine 5 Phosphate (PMP)"

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Yuen, Lao-Duien. "Part I. Studies involving the formation of pyridoxamine-5'-phosphate Schiff bases and their zinc(II) complexes ; Part II. Activity of partly metallated polymer in the decarboxylation of oxalacetic acid /." The Ohio State University, 1985. http://rave.ohiolink.edu/etdc/view?acc_num=osu1487262825075348.

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Alouane, Hamiroufou Loubna. "Préconditionnement myocardique et diabéte : effets aigus des AGEs sur le préconditionnement induit par la stimulation des récepteurs β1-adrénergiques et purinergiques. Rôle de la vitamine B6 (Pyridoxal-5- phosphate et pyridoxamine)". Thesis, Reims, 2012. http://www.theses.fr/2012REIMM202/document.

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Le diabète prédispose à des complications affectant divers organes comme le systémecardiovasculaire. La cardiopathie ischémique chez les patients diabétiques pourrait être liée àl'accumulation de produits avancés de glycation (AGEs). Dans les coeurs de rats ischémiques,l'expression des récepteurs aux AGEs et de ses ligands est considérablement augmentée etimpliquée dans les lésions de l'ischémie / reperfusion (I / R), même en absence de diabète. Ila été récemment rapporté que le myocarde humain diabétique ne peut pas être protégé par lepréconditionnement. Dans ce contexte, notre hypothèse étai

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Caldés, Melis Catalina. "Formación de bases de Schiff de análogos de aminofosfolípidos con compuestos glicantes y efecto competitivo de vitámeros B6." Doctoral thesis, Universitat de les Illes Balears, 2012. http://hdl.handle.net/10803/97354.

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La glicació no enzimàtica de biomolècules consisteix en la modificació irreversible dels seus grups amina per sucres reductors, i s’ha relacionat amb les complicacions patològiques de la diabetis. Una de les dianes de la glicació són els aminofosfolípids, encara que s’han realitzat pocs treballs sobre les seves reaccions. Aquesta tesi es centra en l’estudi de la primera etapa de la glicació (formació d’una base de Schiff) de composts anàlegs d’aminofosfolípids naturals amb composts carbonílics glicants i amb el 5’-fosfat de piridoxal (vitàmer B6 que actua com a inhibidor de la glicació). S’han

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Book chapters on the topic "Pyridoxamine 5 Phosphate (PMP)"

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Sudarsanam, Annapurna, Harry Singh, Bridget Wilcken, et al. "Cirrhosis Associated with Pyridoxal 5′-Phosphate Treatment of Pyridoxamine 5′-Phosphate Oxidase Deficiency." In JIMD Reports. Springer Berlin Heidelberg, 2014. http://dx.doi.org/10.1007/8904_2014_338.

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H. Al-Shekaili, Hilal, Clara van Karnebeek, and Blair R. Leavitt. "Vitamin B6 and Related Inborn Errors of Metabolism." In B-Complex Vitamins - Sources, Intakes and Novel Applications [Working Title]. IntechOpen, 2021. http://dx.doi.org/10.5772/intechopen.99751.

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Vitamin B6 (vitB6) is a generic term that comprises six interconvertible pyridine compounds. These vitB6 compounds (also called vitamers) are pyridoxine (PN), pyridoxamine (PM), pyridoxal (PL) and their 5′-phosphorylated forms pyridoxine 5′-phosphate (PNP), pyridoxamine 5′-phosphate (PMP) and pyridoxal 5′-phosphate (PLP). VitB6 is an essential nutrient for all living organisms, but only microorganisms and plants can carry out de novo synthesis of this vitamin. Other organisms obtain vitB6 from dietary sources and interconvert its different forms according to their needs via a biochemical pathw

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Frey, Perry A., and Adrian D. Hegeman. "Nitrogen and Sulfur Transferases." In Enzymatic Reaction Mechanisms. Oxford University Press, 2007. http://dx.doi.org/10.1093/oso/9780195122589.003.0017.

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Unlike other group transfer reactions in biochemistry, the actions of nitrogen transferring enzymes do not follow a single unifying chemical principle. Nitrogen-transferring enzymes catalyze aminotransfer, amidotransfer, and amidinotransfer. An aminotransferase catalyzes the transfer of the NH2 group from a primary amine to a ketone or aldehyde. An amidotransferase catalyzes the transfer of the anide-NH2 group from glutamine to another group. These reactions proceed by polar reaction mechanisms. Aminomutases catalyze 1,2-intramolecular aminotransfer, in which an amino group is inserted into an

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KWON, OH-SHIN, and JORGE E. CHURCHICH. "Reaction of Pyridoxamine with Carboxylic Residues of Protein." In Enzymes Dependent on Pyridoxal Phosphate and Other Carbonyl Compounds As Cofactors. Elsevier, 1991. http://dx.doi.org/10.1016/b978-0-08-040820-0.50134-5.

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Bowers-Komro, Delores M., Tory M. Hagen, and Donald B. McCormick. "[19] Modified purification of pyridoxamine (pyridoxine) 5′-phosphate oxidase from rabbit liver by 5′-phosphopyridoxyl affinity chromatography." In Methods in Enzymology. Elsevier, 1986. http://dx.doi.org/10.1016/0076-6879(86)22157-6.

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