Relevant bibliographies by topics / Pyridoxal-5′-phosphate (PLP)-dependent enzymes

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Academic literature on the topic 'Pyridoxal-5′-phosphate (PLP)-dependent enzymes'

Author: Grafiati
Published: 7 June 2025
Last updated: 2 August 2025

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Journal articles on the topic "Pyridoxal-5′-phosphate (PLP)-dependent enzymes"

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Zou, Lingling, Yang Song, Chengliang Wang, et al. "Crystal structure of maize serine racemase with pyridoxal 5′-phosphate." Acta Crystallographica Section F Structural Biology Communications 72, no. 3 (2016): 165–71. http://dx.doi.org/10.1107/s2053230x16000960.

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Serine racemase (SR) is a pyridoxal 5′-phosphate (PLP)-dependent enzyme that is responsible for D-serine biosynthesisin vivo. The first X-ray crystal structure of maize SR was determined to 2.1 Å resolution and PLP binding was confirmed in solution by UV–Vis absorption spectrometry. Maize SR belongs to the type II PLP-dependent enzymes and differs from the SR of a vancomycin-resistant bacterium. The PLP is bound to each monomer by forming a Schiff base with Lys67. Structural comparison with rat and fission yeast SRs reveals a similar arrangement of active-site residues but a different orientat
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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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AL Mughram, Mohammed H., Mohini S. Ghatge, Glen E. Kellogg, and Martin K. Safo. "Elucidating the Interaction between Pyridoxine 5′-Phosphate Oxidase and Dopa Decarboxylase: Activation of B6-Dependent Enzyme." International Journal of Molecular Sciences 24, no. 1 (2022): 642. http://dx.doi.org/10.3390/ijms24010642.

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Pyridoxal 5′-phosphate (PLP), the active form of vitamin B6, serves as a cofactor for scores of B6-dependent (PLP-dependent) enzymes involved in many cellular processes. One such B6 enzyme is dopa decarboxylase (DDC), which is required for the biosynthesis of key neurotransmitters, e.g., dopamine and serotonin. PLP-dependent enzymes are biosynthesized as apo-B6 enzymes and then converted to the catalytically active holo-B6 enzymes by Schiff base formation between the aldehyde of PLP and an active site lysine of the protein. In eukaryotes, PLP is made available to the B6 enzymes through the act
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Aleshin, Vasily A., and Victoria I. Bunik. "Protein–Protein Interfaces as Druggable Targets: A Common Motif of the Pyridoxal-5′-Phosphate-Dependent Enzymes to Receive the Coenzyme from Its Producers." Biochemistry (Moscow) 88, no. 7 (2023): 1022–33. http://dx.doi.org/10.1134/s0006297923070131.

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Abstract Pyridoxal-5′-phosphate (PLP), a phosphorylated form of vitamin B6, acts as a coenzyme for numerous reactions, including those changed in cancer and/or associated with the disease prognosis. Since highly reactive PLP can modify cellular proteins, it is hypothesized to be directly transferred from its donors to acceptors. Our goal is to validate the hypothesis by finding common motif(s) in the multitude of PLP-dependent enzymes for binding the limited number of PLP donors, namely pyridoxal kinase (PdxK), pyridox(am)in-5′-phosphate oxidase (PNPO), and PLP-binding protein (PLPBP). Experim
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Aleshin, V. A., and V. I. Bunik. "Protein-protein interfaces as druggable targets: a common motif of the pyridoxal-5′-phosphate-dependent enzymes to receive the coenzyme from its producer." Биохимия 88, no. 7 (2023): 1254–67. http://dx.doi.org/10.31857/s0320972523070138.

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Pyridoxal-5′-phosphate (PLP), a phosphorylated form of vitamin B6, acts as a coenzyme for numerous reactions, including those changed in cancer and/or associated with the disease prognosis. Since highly reactive PLP may modify cellular proteins, it is hypothesized to be directly transferred from its donors to acceptors. Our goal is to validate the hypothesis by finding common motif(s) in a multitude of the PLP-dependent enzymes for binding the limited number of the PLP donors, namely pyridoxal kinase (PdxK), pyridox(am)in-5′-phosphate oxidase (PNPO) and the PLP-binding protein (PLPBP). Experim
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Bisello, Giovanni, Carmen Longo, Giada Rossignoli, Robert S. Phillips, and Mariarita Bertoldi. "Oxygen reactivity with pyridoxal 5′-phosphate enzymes: biochemical implications and functional relevance." Amino Acids 52, no. 8 (2020): 1089–105. http://dx.doi.org/10.1007/s00726-020-02885-6.

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Abstract The versatility of reactions catalyzed by pyridoxal 5′-phosphate (PLP) enzymes is largely due to the chemistry of their extraordinary catalyst. PLP is necessary for many reactions involving amino acids. Reaction specificity is controlled by the orientation of the external aldimine intermediate that is formed upon addition of the amino acidic substrate to the coenzyme. The breakage of a specific bond of the external aldimine gives rise to a carbanionic intermediate. From this point, the different reaction pathways diverge leading to multiple activities: transamination, decarboxylation,
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Rajendran, Narayanan, Colby Smith, and Williard Mazhawidza. "Molecular and Phylogenetic Analysis of Pyridoxal Phosphate- Dependent Acyltransferase of Exiguobacterium acetylicum." Zeitschrift für Naturforschung C 64, no. 11-12 (2009): 891–98. http://dx.doi.org/10.1515/znc-2009-11-1222.

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The pyridoxal-5’-phosphate (PLP)-dependent family of enzymes is a very diverse group of proteins that metabolize small molecules like amino acids and sugars, and synthesize cofactors for other metabolic pathways through transamination, decarboxylation, racemization, and substitution reactions. In this study we employed degenerated primer-based PCR amplification, using genomic DNA isolated from the soil bacterium Exiguobacterium acetylicum strain SN as template. We revealed the presence of a PLP-dependent family of enzymes, such as PLP-dependent acyltransferase, and similarity to 8-amino-7-oxon
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Yoshikane, Yu, Nana Yokochi, Kouhei Ohnishi, Hideyuki Hayashi, and Toshiharu Yagi. "Molecular cloning, expression and characterization of pyridoxamine–pyruvate aminotransferase." Biochemical Journal 396, no. 3 (2006): 499–507. http://dx.doi.org/10.1042/bj20060078.

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Pyridoxamine–pyruvate aminotransferase is a PLP (pyridoxal 5′-phosphate) (a coenzyme form of vitamin B6)-independent aminotransferase which catalyses a reversible transamination reaction between pyridoxamine and pyruvate to form pyridoxal and L-alanine. The gene encoding the enzyme has been identified, cloned and overexpressed for the first time. The mlr6806 gene on the chromosome of a symbiotic nitrogen-fixing bacterium, Mesorhizobium loti, encoded the enzyme, which consists of 393 amino acid residues. The primary sequence was identical with those of archaeal aspartate aminotransferase and ra
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Lee, Dukwon, Hyojeong Lee, Kyumi Byun, Eun-Su Park, and Nam-Chul Ha. "Functional importance of Ser323 in cysteine desulfhydrase and cystathionine gamma-lyase MccB of Staphylococcus aureus." Journal of Microbiology 63, no. 2 (2025): e2411026. https://doi.org/10.71150/jm.2411026.

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Pyridoxal 5'-phosphate (PLP)-dependent enzymes participate in various reactions involved in methionine and cysteine metabolism. The representative foodborne pathogen Staphylococcus aureus expresses the PLP-dependent enzyme MccB, which exhibits both cystathionine gamma-lyase (CGL) and cysteine desulfhydrase activities. In this study, we investigated the role of Ser323 in MccB, a conserved residue in many PLP-dependent enzymes in the transsulfuration pathway. Our findings reveal that Ser323 forms a hydrogen bond with the catalytic lysine in the absence of PLP, and upon internal aldimine formatio
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Ngo, Ho-Phuong-Thuy, Nuno M. F. S. A. Cerqueira, Jin-Kwang Kim, et al. "PLP undergoes conformational changes during the course of an enzymatic reaction." Acta Crystallographica Section D Biological Crystallography 70, no. 2 (2014): 596–606. http://dx.doi.org/10.1107/s1399004713031283.

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Numerous enzymes, such as the pyridoxal 5′-phosphate (PLP)-dependent enzymes, require cofactors for their activities. Using X-ray crystallography, structural snapshots of the L-serine dehydratase catalytic reaction of a bacterial PLP-dependent enzyme were determined. In the structures, the dihedral angle between the pyridine ring and the Schiff-base linkage of PLP varied from 18° to 52°. It is proposed that the organic cofactor PLP directly catalyzes reactions by active conformational changes, and the novel catalytic mechanism involving the PLP cofactor was confirmed by high-level quantum-mech
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Dissertations / Theses on the topic "Pyridoxal-5′-phosphate (PLP)-dependent enzymes"

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Beattie, Ashley Emily. "Mechanistic studies of the pyridoxal 5'-phosphate-dependent enzyme serine palmitoyltransferase : substrates, cofactor and inhibitors." Thesis, University of Edinburgh, 2014. http://hdl.handle.net/1842/10059.

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Sphingolipids (SL) are essential structural components of membranes found in all eukaryotes and have also been identified in some bacteria. The first step of the SL biosynthetic pathway across all species is catalysed by serine palmitoyltransferase (SPT), a member of the alpha-oxoamine synthase (AOS) family of pyridoxal 5’- phosphate (PLP)-dependent enzymes. AOS enzymes are involved in the biosynthesis of a range of important natural products such as heme, vitamins and antibiotics where they catalyse the reaction between amino acid and acyl-thioester substrates. Substrate specificity across th
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Mykhaylyk, Bohdan. "Structural and mechanistic studies of the pyridoxal 5'-phosphate-dependent enzyme serine palmitoyltransferase." Thesis, University of Edinburgh, 2018. http://hdl.handle.net/1842/33195.

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Sphingolipids (SLs) are complex lipid-derived structures that are essential components of cell membranes in eukaryotes and some bacteria. SLs and their complex derivatives ceramides are known to be involved in multiple processes such as the formation of lipid rafts, cell signalling and membrane trafficking. The first step of SL biosynthesis is universal to all sphingolipid-producing organisms from bacteria to humans and is catalysed by the enzyme serine palmitoyltransferase (SPT). SPT is a member of the alpha-oxoamine synthase (AOS) family of pyridoxal- 5'-phosphate-dependent enzymes. All AOS
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Dajnowicz, Steven. "Electronic Modulation in Pyridoxal-5’-Phosphate-Dependent Enzymes." University of Toledo / OhioLINK, 2018. http://rave.ohiolink.edu/etdc/view?acc_num=toledo1542039760697676.

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Smith, David Martin. "Structural and mechanistic studies of pyridoxal-5'-phosphate dependent enzymes." Thesis, University of Southampton, 1990. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.357250.

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A model for the active-site of pyridoxal-5'-phosphate dependent carboxylases has been developed based on the known structural and mechanistic features of these enzymes. Comparison of the known structural and mechanistic features of aspartate aminotransferase with those of the model for pyridoxal-5'-phosphate dependent decarboxylases indicated that it might be feasible to convert aspartate aminotransferase into a decarboxylase using site-directed mutagenesis techniques. The possibility was investigated using computer graphics and molecular modelling techniques. The various AAT mutant structures
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Tilley, Kevin. "Structural and mechanistic studies of pyridoxal 5'-phosphate dependent enzymes." Thesis, University of Southampton, 1992. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.316085.

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The pyridoxal 5'-phosphate (PLP) analogue 4'-N-(2''-phosphoethyl) pyridoxamine 5'-phosphate (EAP-PMP) has been synthetized. The appenzymes of both E.coli L-glutamic acid decarboxylase (GAD) and cytosolic aspartate aminotransferase have been shown to cleave the pyridoxal analogue with the production of PLP, resulting in reactivation of the enzyme. Two other PLP apoenzymes have been purified and have been demonstrated to be inactive towards EAP-PMP. In order to determine the stereochemical course of the proton abstraction step of the reactivation reaction with E.coli GAD (2R)- and (2S)-[1''-2H1]
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Turbeville, Tracy D. "PLP-Dependent α-Oxoamine Synthases: Phylogenetic Analysis, Structural Plasticity, and Structure-Function Studies on 5-Aminolevulinate Synthase". Scholar Commons, 2009. https://scholarcommons.usf.edu/etd/57.

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5-Aminolevulinate synthase (ALAS) and 8-amino-7-oxononanoate synthase (AONS) are two of four homodimeric members of the alpha-oxoamine synthase family of pyridoxal 5'-phosphate (PLP)-dependent enzymes. The evolutionary relationships among α-oxoamine synthases representing a broad taxonomic and phylogenetic spectrum have been examined to help identify residues that may regulate substrate specificity. The structural plasticity of ALAS has been documented in studies of functional circularly permuted ALAS variants and the single polypeptide chain ALAS dimer (ALAS/ALAS) exhibiting a greater turnove
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Whyte, Sheena Malling. "Stereochemical aspects of the mechanism of inhibition of pyridoxal-5'-phosphate dependent enzymes." Thesis, University of Sussex, 1998. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.263214.

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Casasnovas, Perera Rodrigo. "Theoretical studies on pyridoxal 5’-phosphate-catalyzed reactions of biological relevance." Doctoral thesis, Universitat de les Illes Balears, 2014. http://hdl.handle.net/10803/133519.

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El piridoxal fosfato (PLP) es cofactor de más de un centenar de enzimas que catalizan reacciones sobre aminoácidos como racemizaciones, transaminaciones o descarboxilaciones entre otras. Todas las reacciones catalizadas por PLP implican al menos una etapa de protonacion/desprotonación del carbono C del aminoácido o C4’ del PLP. El estudio experimental de la acidez de estos carbonos presenta muchas dificultades. En este trabajo se han diseñado estrategias computacionales para la determinación de pKas, obteniendo una metodología que proporciona pKas con incertidumbres equivalentes a las experim
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Liu, Wenshe. "Kinetic and structural analysis of two pyridoxal 5'-phosphate-dependent enzymes : dialkylglycine decarboxylase and [gamma]-aminobutyrate aminotransferase /." For electronic version search Digital dissertations database. Restricted to UC campuses. Access is free to UC campus dissertations, 2005. http://uclibs.org/PID/11984.

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Thesis (Ph. D.)--University of California, Davis, 2005.<br>Degree granted in Chemistry. On title page "[gamma]" appears as lower-case Greek letter. Also available via the World Wide Web. (Restricted to UC campuses)
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Forde, Paul William. "An investigation into the mechanism of inhibition of Pyridoxal-5'-phosphate dependent enzymes and of D-amino acid oxidase." Thesis, University of Sussex, 2000. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.313969.

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Book chapters on the topic "Pyridoxal-5′-phosphate (PLP)-dependent enzymes"

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Christen, P., P. K. Mehta, and E. Sandmeier. "Molecular evolution of pyridoxal-5′-phosphate-dependent enzymes." In Biochemistry of Vitamin B6 and PQQ. Birkhäuser Basel, 1994. http://dx.doi.org/10.1007/978-3-0348-7393-2_2.

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Mehta, Perdeep K., and Philipp Christen. "The Molecular Evolution of Pyridoxal-5′-Phosphate-Dependent Enzymes." In Advances in Enzymology - and Related Areas of Molecular Biology. John Wiley & Sons, Inc., 2006. http://dx.doi.org/10.1002/9780470123201.ch4.

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Mozzarelli, Andrea, Barbara Campanini, Stefano Bettati, and Alessio Peracchi. "Functional properties of immobilized pyridoxal 5’-phosphate-dependent enzymes probed by absorption microspectrophotometry." In Biochemistry and Molecular Biology of Vitamin B6 and PQQ-dependent Proteins. Birkhäuser Basel, 2000. http://dx.doi.org/10.1007/978-3-0348-8397-9_57.

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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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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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DUINE, J. A. "PLP and/or PQQ?" In Enzymes Dependent on Pyridoxal Phosphate and Other Carbonyl Compounds As Cofactors. Elsevier, 1991. http://dx.doi.org/10.1016/b978-0-08-040820-0.50095-9.

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SODA, KENJI. "PLP-Dependent and Independent Amino Acid Racemases." In Enzymes Dependent on Pyridoxal Phosphate and Other Carbonyl Compounds As Cofactors. Elsevier, 1991. http://dx.doi.org/10.1016/b978-0-08-040820-0.50009-1.

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KONDO, H., Y. OHAMA, H. TANAMACHI, S. TANASE, and Y. MORINO. "15N NMR Studies on Aspartate Aminotransferase Reconstituted with [15N]PLP." In Enzymes Dependent on Pyridoxal Phosphate and Other Carbonyl Compounds As Cofactors. Elsevier, 1991. http://dx.doi.org/10.1016/b978-0-08-040820-0.50030-3.

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MARCEAU, M., and J. A. SHAFER. "Contribution of a Glycine-Rich Loop to PLP Active Sites." In Enzymes Dependent on Pyridoxal Phosphate and Other Carbonyl Compounds As Cofactors. Elsevier, 1991. http://dx.doi.org/10.1016/b978-0-08-040820-0.50066-2.

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MOROZOV, YU V., N. P. BAZHULINA, V. A. BOKOVOY, L. I. FIODOROVA, and V. O. CHEKHOV. "Peculiarities of Spectroscopicsl Behavior of PLP Aldimines with Amino Acids." In Enzymes Dependent on Pyridoxal Phosphate and Other Carbonyl Compounds As Cofactors. Elsevier, 1991. http://dx.doi.org/10.1016/b978-0-08-040820-0.50080-7.

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