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pyridoxal phosphate
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- Author:
- Riccardo Montioli; Ilaria Bellezza; Maria Andrea Desbats; Carla Borri Voltattorni; Leonardo Salviati; Barbara Cellini
- Source:
- Biochimica et biophysica acta 2021 v.1869 no.1 pp. 140555
- ISSN:
- 1570-9639
- Subject:
- atrophy; blindness; catabolism; diet; genes; humans; ornithine; ornithine-oxo-acid transaminase; phenotype; pyridoxal phosphate; pyridoxine; retina
- Abstract:
- ... Gyrate Atrophy (GA) of the choroid and retina (MIM# 258870) is an autosomal recessive disorder due to mutations of the OAT gene encoding ornithine-delta-aminotransferase (OAT), associated with progressive retinal deterioration and blindness. The disease has a theoretical global incidence of approximately 1:1,500,000. OAT is mainly involved in ornithine catabolism in adults, thus explaining the hyp ...
- DOI:
- 10.1016/j.bbapap.2020.140555
- https://doi.org/10.1016/j.bbapap.2020.140555
- Author:
- Annalisa Michielon; Francesco Marchesani; Serena Faggiano; Roberta Giaccari; Barbara Campanini; Stefano Bettati; Andrea Mozzarelli; Stefano Bruno
- Source:
- Biochimica et biophysica acta 2021 v.1869 no.1 pp. 140544
- ISSN:
- 1570-9639
- Subject:
- aldehydes; biosynthesis; enantiomers; glyceraldehyde 3-phosphate; glyceraldehyde-3-phosphate dehydrogenase; humans; ligands; mice; pyridoxal phosphate; serine; serine racemase
- Abstract:
- ... Murine serine racemase (SR), the enzyme responsible for the biosynthesis of the neuromodulator d-serine, was reported to form a complex with glyceraldehyde 3-phosphate dehydrogenase (GAPDH), resulting in SR inhibition. In this work, we investigated the interaction between the two human orthologues. We were not able to observe neither the inhibition nor the formation of the SR-GAPDH complex. Rather ...
- DOI:
- 10.1016/j.bbapap.2020.140544
- https://doi.org/10.1016/j.bbapap.2020.140544
- Author:
- Rúben J. Ramos; Monique Albersen; Esmee Vringer; Marjolein Bosma; Susan Zwakenberg; Fried Zwartkruis; Judith J.M. Jans; Nanda M. Verhoeven-Duif
- Source:
- Biochimica et biophysica acta 2019 v.1863 no.6 pp. 1088-1097
- ISSN:
- 0304-4165
- Subject:
- cell lines; dose response; enzyme activity; enzymes; humans; in vitro studies; metabolism; patients; phosphates; potassium channels; protective effect; pyridoxal; pyridoxal phosphate; pyridoxine; yeasts
- Abstract:
- ... Pyridoxal 5′-phosphate (PLP) is the active form of vitamin B6. Mammals cannot synthesize vitamin B6, so they rely on dietary uptake of the different B6 forms, and via the B6 salvage pathway they interconvert them into PLP. Humans possess three enzymes in this pathway: pyridoxal kinase, pyridox(am)ine phosphate oxidase and pyridoxal phosphatase. Besides these, a fourth enzyme has been described in ...
- DOI:
- 10.1016/j.bbagen.2019.03.019
- https://doi.org/10.1016/j.bbagen.2019.03.019
- Author:
- Yulia S. Zeifman; Konstantin M. Boyko; Alena Yu. Nikolaeva; Vladimir I. Timofeev; Tatiana V. Rakitina; Vladimir O. Popov; Ekaterina Yu. Bezsudnova
- Source:
- Biochimica et biophysica acta 2019 v.1867 no.6 pp. 575-585
- ISSN:
- 1570-9639
- Subject:
- active sites; alpha-ketoglutaric acid; amination; amino acids; pH; pyridoxal phosphate; sodium chloride; stereoselectivity; substrate specificity; transaminases
- Abstract:
- ... Pyridoxal-5′-phosphate (PLP)-dependent transaminases are industrially important enzymes catalyzing the stereoselective amination of ketones and keto acids. Transaminases of PLP fold type IV are characterized by (R)- or (S)-stereoselective transfer of amino groups, depending on the substrate profile of the enzyme. PLP fold type IV transaminases include branched-chain amino acid transaminases (BCATs ...
- DOI:
- 10.1016/j.bbapap.2019.03.005
- https://doi.org/10.1016/j.bbapap.2019.03.005
- Author:
- Robert S. Phillips; Mori Crocker; Richard Lin; O. Elijah Idowu; David K. McCannon; Santiago Lima
- Source:
- Biochimica et biophysica acta 2019 v.1867 no.7-8 pp. 722-731
- ISSN:
- 1570-9639
- Subject:
- Pseudomonas fluorescens; alanine; benzaldehyde; catalytic activity; cleavage (chemistry); glutamic acid; hydrogen bonding; hydrolases; mutants; mutation; nuclear magnetic resonance spectroscopy; oxyanions; oxygen; pyridoxal phosphate; quinones
- Abstract:
- ... Kynureninase from Pseudomonas fluorescens (Pfkynase) catalyzes the pyridoxal-5′-phosphate (PLP) dependent hydrolytic cleavage of L-kynurenine to give anthranilate and L-alanine. Asp-132 and Asp-201 are located in the structure near the pyridine NH of the PLP, with Asp-201 forming a hydrogen bond. Mutation of Asp-132 to alanine and glutamate and Asp-201 to glutamate results in reduced catalytic act ...
- DOI:
- 10.1016/j.bbapap.2019.05.005
- https://doi.org/10.1016/j.bbapap.2019.05.005
- Author:
- Stefano Bruno; Marilena Margiotta; Francesco Marchesani; Gianluca Paredi; Valentina Orlandi; Serena Faggiano; Luca Ronda; Barbara Campanini; Andrea Mozzarelli
- Source:
- Biochimica et biophysica acta 2017 v.1865 no.4 pp. 381-387
- ISSN:
- 1570-9639
- Subject:
- adenosine triphosphate; binding sites; calcium; enzymes; glutamate receptors; humans; ions; ligands; magnesium; median effective concentration; metabolism; pyridoxal; pyridoxal phosphate; serine; threonine
- Abstract:
- ... Serine racemase is the pyridoxal 5′-phosphate dependent enzyme that catalyzes both production and catabolism of d-serine, a co-agonist of the NMDA glutamate receptors. Mg²⁺, or, alternatively, Ca²⁺, activate human serine racemase by binding both at a specific site and – as ATP-metal complexes – at a distinct ATP binding site. We show that Mg²⁺ and Ca²⁺ bind at the metal binding site with a 4.5-fol ...
- DOI:
- 10.1016/j.bbapap.2017.01.001
- https://doi.org/10.1016/j.bbapap.2017.01.001
- Author:
- Caitlyn Makins; Douglas A. Whitelaw; Michael McGregor; Alix Petit; Robert G. Mothersole; Kathleen E. Prosser; Kirsten R. Wolthers
- Source:
- Biochimica et biophysica acta 2017 v.1865 no.8 pp. 1077-1084
- ISSN:
- 1570-9639
- Subject:
- Clostridium sticklandii; active sites; catalytic activity; electron paramagnetic resonance spectroscopy; electrostatic interactions; homolytic cleavage; hydrogen; isomerization; isotopes; ornithine; pyridoxal; pyridoxal phosphate
- Abstract:
- ... Ornithine 4,5-aminomutase (OAM) from Clostridium sticklandii is an adenosylcobalamin (AdoCbl) and pyridoxal 5′-phosphate (PLP)-dependent enzyme that catalyzes a 1,2-amino shift, interconverting d-ornithine and 2S, 4R-diaminopentanoate. The reaction occurs via a radical-based mechanism whereby a PLP-bound substrate radical undergoes intramolecular isomerization via an azacyclopropylcarbinyl radical ...
- DOI:
- 10.1016/j.bbapap.2017.05.011
- https://doi.org/10.1016/j.bbapap.2017.05.011
- Author:
- Davide Amidani; Angela Tramonti; Andrea Valeria Canosa; Barbara Campanini; Stefano Maggi; Teresa Milano; Martino L. di Salvo; Stefano Pascarella; Roberto Contestabile; Stefano Bettati; Claudio Rivetti
- Source:
- Biochimica et biophysica acta 2017 v.1861 no.1 pp. 3474-3489
- ISSN:
- 0304-4165
- Subject:
- Bacillus subtilis; DNA; DNA-binding domains; atomic force microscopy; electrophoresis; gamma-aminobutyric acid; genes; in vitro studies; mechanism of action; models; mutants; nitroprusside; oligomerization; pyridoxal; pyridoxal phosphate; stoichiometry; transaminases; transcription factors
- Abstract:
- ... GabR is a transcriptional regulator belonging to the MocR/GabR family, characterized by a N-terminal wHTH DNA-binding domain and a C-terminal effector binding and/or oligomerization domain, structurally homologous to aminotransferases (ATs). In the presence of γ-aminobutyrate (GABA) and pyridoxal 5′-phosphate (PLP), GabR activates the transcription of gabT and gabD genes involved in GABA metabolis ...
- DOI:
- 10.1016/j.bbagen.2016.09.013
- https://doi.org/10.1016/j.bbagen.2016.09.013
- Author:
- Bosko M. Stojanovski; Leonid Breydo; Vladimir N. Uversky; Gloria C. Ferreira
- Source:
- Biochimica et biophysica acta 2016 v.1864 no.5 pp. 441-452
- ISSN:
- 1570-9639
- Subject:
- 5-aminolevulinate synthase; algorithms; biosynthesis; blood; catalytic activity; cytosol; denaturation; eukaryotic cells; heme; mice; molecular weight; physiological transport; proteolysis; pyridoxal; pyridoxal phosphate; thermal stability; topology
- Abstract:
- ... 5-Aminolevulinate synthase (ALAS), a pyridoxal 5′-phosphate (PLP)-dependent homodimeric enzyme, catalyzes the initial step of heme biosynthesis in non-plant eukaryotes. The precursor form of the enzyme is translated in the cytosol, and upon mitochondrial import, the N-terminal targeting presequence is proteolytically cleaved to generate mature ALAS. In bone marrow-derived erythroid cells, a mitoch ...
- DOI:
- 10.1016/j.bbapap.2016.02.002
- https://doi.org/10.1016/j.bbapap.2016.02.002
- Author:
- Davide Schiroli; Alessio Peracchi
- Source:
- Biochimica et biophysica acta 2015 v.1854 no.9 pp. 1200-1211
- ISSN:
- 1570-9639
- Subject:
- amines; catalysts; proteins; pyridoxal phosphate; transaminases; variance
- Abstract:
- ... The present review focuses on a subfamily of pyridoxal phosphate (PLP)-dependent enzymes, belonging to the broader fold-type I structural group and whose archetypes can be considered ornithine δ-transaminase and γ-aminobutyrate transaminase. These proteins were originally christened “subgroup-II aminotransferases” (AT-II) but are very often referred to as “class-III aminotransferases”. As names su ...
- DOI:
- 10.1016/j.bbapap.2015.02.023
- https://doi.org/10.1016/j.bbapap.2015.02.023
- Author:
- Robert S. Phillips
- Source:
- Biochimica et biophysica acta 2015 v.1854 no.9 pp. 1167-1174
- ISSN:
- 1570-9639
- Subject:
- alanine; catalytic activity; decarboxylation; enzymes; kynurenine; phenol; phosphates; proteins; pyridoxal phosphate; reaction mechanisms; transamination; tyrosine
- Abstract:
- ... Pyridoxal-5′-phosphate (PLP) is a versatile cofactor that enzymes use to catalyze a wide variety of reactions of amino acids, including transamination, decarboxylation, racemization, β- and γ-eliminations and substitutions, retro-aldol and Claisen reactions. These reactions depend on the ability of PLP to stabilize, to a varying degree, α-carbanionic intermediates. Furthermore, oxidative decarboxy ...
- DOI:
- 10.1016/j.bbapap.2014.12.028
- https://doi.org/10.1016/j.bbapap.2014.12.028
- Author:
- Magnus Monné; Daniela Valeria Miniero; Toshihiro Obata; Lucia Daddabbo; Luigi Palmieri; Angelo Vozza; M. Cristina Nicolardi; Alisdair R. Fernie; Ferdinando Palmieri
- Source:
- Biochimica et biophysica acta 2015 v.1847 no.10 pp. 1220-1230
- ISSN:
- 0005-2728
- Subject:
- Arabidopsis thaliana; EDTA (chelating agent); adenosine; adenosine diphosphate; adenosine monophosphate; adenosine triphosphate; calcium; ethylene glycol tetraacetic acid; flowers; gene expression; genes; humans; leaves; membrane proteins; mitochondria; mitochondrial membrane; phosphates; pyridoxal phosphate; seedlings; sulfates; thiosulfates; transcription (genetics)
- Abstract:
- ... The Arabidopsis thaliana genome contains 58 membrane proteins belonging to the mitochondrial carrier family. Three members of this family, here named AtAPC1, AtAPC2, and AtAPC3, exhibit high structural similarities to the human mitochondrial ATP–Mg2+/phosphate carriers. Under normal physiological conditions the AtAPC1 gene was expressed at least five times more than the other two AtAPC genes in fl ...
- DOI:
- 10.1016/j.bbabio.2015.06.015
- https://doi.org/10.1016/j.bbabio.2015.06.015
- Author:
- Alessandra Astegno; Guido Capitani; Paola Dominici
- Source:
- Biochimica et biophysica acta 2015 v.1854 no.9 pp. 1229-1237
- ISSN:
- 1570-9639
- Subject:
- Arabidopsis thaliana; calcium; calmodulin; crystal structure; dissociation; glutamate decarboxylase; glutamic acid; mutants; oligomerization; pH; pyridoxal; pyridoxal phosphate; site-directed mutagenesis
- Abstract:
- ... Glutamate decarboxylase (GAD) is a pyridoxal 5′-phosphate (PLP)-dependent enzyme that catalyzes the α-decarboxylation of glutamate to γ-aminobutyrate. A unique feature of plant GAD is the presence of a calmodulin (CaM)-binding domain at its C-terminus. In plants, transient elevation of cytosolic Ca²⁺ in response to different types of stress is responsible for GAD activation via CaM. The crystal st ...
- DOI:
- 10.1016/j.bbapap.2015.01.001
- https://doi.org/10.1016/j.bbapap.2015.01.001
- Author:
- Riccardo Montioli; Elisa Oppici; Mirco Dindo; Alessandro Roncador; Giovanni Gotte; Barbara Cellini; Carla Borri Voltattorni
- Source:
- Biochimica et biophysica acta 2015 v.1854 no.10 pp. 1280-1289
- ISSN:
- 1570-9639
- Subject:
- Escherichia coli; alleles; binding capacity; denaturation; dissociation; dose response; haplotypes; liver; mammals; missense mutation; mitochondria; patients; peroxisomes; proteolysis; pyridoxal; pyridoxal phosphate; pyridoxine; therapeutics
- Abstract:
- ... Liver peroxisomal alanine:glyoxylate aminotransferase (AGT), a pyridoxal 5′-phosphate (PLP) enzyme, exists as two polymorphic forms, the major (AGT-Ma) and the minor (AGT-Mi) haplotype. Deficit of AGT causes Primary Hyperoxaluria Type 1 (PH1), an autosomal recessive rare disease. Although ~one-third of the 79 disease-causing missense mutations segregates on AGT-Mi, only few of them are well charac ...
- DOI:
- 10.1016/j.bbapap.2015.07.002
- https://doi.org/10.1016/j.bbapap.2015.07.002
- Author:
- Martino Luigi di Salvo; Isabel Nogués; Alessia Parroni; Angela Tramonti; Teresa Milano; Stefano Pascarella; Roberto Contestabile
- Source:
- Biochimica et biophysica acta 2015 v.1854 no.9 pp. 1160-1166
- ISSN:
- 1570-9639
- Subject:
- Escherichia coli; adenosine triphosphate; metabolism; nutrients; phosphates; phosphotransferases (kinases); pyridoxal; pyridoxal phosphate; pyridoxine; schiff bases; solvents
- Abstract:
- ... Pyridoxal 5′-phosphate (PLP), the catalytically active form of vitamin B6, plays a crucial role in several cellular processes. In most organisms, PLP is recycled from nutrients and degraded B6-enzymes in a salvage pathway that involves pyridoxal kinase (PLK), pyridoxine phosphate oxidase and phosphatase activities. Regulation of the salvage pathway is poorly understood. Escherichia coli possesses ...
- DOI:
- 10.1016/j.bbapap.2015.01.013
- https://doi.org/10.1016/j.bbapap.2015.01.013
- Author:
- Robert Schnell; Dharmarajan Sriram; Gunter Schneider
- Source:
- Biochimica et biophysica acta 2015 v.1854 no.9 pp. 1175-1183
- ISSN:
- 1570-9639
- Subject:
- Bacilli; Mycobacterium tuberculosis; antibiotics; biosynthesis; cysteine; cysteine synthase; drug resistance; drug therapy; drugs; free radicals; homeostasis; lungs; nitrogen; oxygen; pathogen survival; proteins; pyridoxal phosphate; relapse; sulfur; tuberculosis
- Abstract:
- ... The alarming increase of drug resistance in Mycobacterium tuberculosis strains poses a severe threat to human health. Chemotherapy is particularly challenging because M. tuberculosis can persist in the lungs of infected individuals; estimates of the WHO indicate that about 1/3 of the world population is infected with latent tuberculosis providing a large reservoir for relapse and subsequent spread ...
- DOI:
- 10.1016/j.bbapap.2014.11.010
- https://doi.org/10.1016/j.bbapap.2014.11.010
- Author:
- Natalya V. Anufrieva; Nicolai G. Faleev; Elena A. Morozova; Natalia P. Bazhulina; Svetlana V. Revtovich; Vladimir P. Timofeev; Yaroslav V. Tkachev; Alexei D. Nikulin; Tatyana V. Demidkina
- Source:
- Biochimica et biophysica acta 2015 v.1854 no.9 pp. 1220-1228
- ISSN:
- 1570-9639
- Subject:
- Citrobacter freundii; X-radiation; absorption; active sites; deuterium oxide; hydrogen bonding; mutants; oxygen; phenylalanine; phosphates; proteins; protons; pyridoxal; pyridoxal phosphate; site-directed mutagenesis; spectral analysis; tyrosine
- Abstract:
- ... In the spatial structure of methionine γ-lyase (MGL, EC 4.4.1.11) from Citrobacter freundii, Tyr58 is located at H-bonding distance to the oxygen atom of the phosphate “handle” of pyridoxal 5′-phosphate (PLP). It was replaced for phenylalanine by site-directed mutagenesis. The X-ray structure of the mutant enzyme was determined at 1.96Å resolution. Comparison of spatial structures and absorption s ...
- DOI:
- 10.1016/j.bbapap.2014.12.027
- https://doi.org/10.1016/j.bbapap.2014.12.027
- Author:
- Hans-Heinrich Limbach; Monique Chan-Huot; Shasad Sharif; Peter M. Tolstoy; Ilya G. Shenderovich; Gleb S. Denisov; Michael D. Toney
- Source:
- Biochimica et biophysica acta 2011 v.1814 no.11 pp. 1426-1437
- ISSN:
- 1878-1454
- Subject:
- aqueous solutions; aspartate transaminase; aspartic acid; correlation; enzymatic reactions; enzymology; histidine; hydrogen bonding; models; nitrogen; nuclear magnetic resonance spectroscopy; proteins; pyridoxal; pyridoxal phosphate; schiff bases; solvents; stable isotopes; zwitterions
- Abstract:
- ... In this contribution we review recent NMR studies of protonation and hydrogen bond states of pyridoxal 5′-phosphate (PLP) and PLP model Schiff bases in different environments, starting from aqueous solution, the organic solid state to polar organic solution and finally to enzyme environments. We have established hydrogen bond correlations that allow one to estimate hydrogen bond geometries from ¹⁵ ...
- DOI:
- 10.1016/j.bbapap.2011.06.004
- https://doi.org/10.1016/j.bbapap.2011.06.004
- Author:
- Hiroko Ikushiro; Hideyuki Hayashi
- Source:
- Biochimica et biophysica acta 2011 v.1814 no.11 pp. 1474-1480
- ISSN:
- 1878-1454
- Subject:
- biosynthesis; pyridoxal phosphate; sphingolipids; spectroscopy; enzymology; serine C-palmitoyltransferase
- Abstract:
- ... Serine palmitoyltransferase, which is one of the α-oxamine synthase family enzymes, catalyzes the condensation reaction of L-serine and palmitoyl-CoA to form 3-ketodihydrosphingosine, the first and rate-determining step of the sphingolipid biosynthesis. As with other α-oxamine synthase family enzymes, the catalytic reaction is composed of multiple elementary steps, and the mechanism to control the ...
- DOI:
- 10.1016/j.bbapap.2011.02.005
- https://doi.org/10.1016/j.bbapap.2011.02.005
- Author:
- Barbara Kappes; Ivo Tews; Alexandra Binter; Peter Macheroux
- Source:
- Biochimica et biophysica acta 2011 v.1814 no.11 pp. 1567-1576
- ISSN:
- 1878-1454
- Subject:
- Protozoa; drugs; enzymatic reactions; enzymes; enzymology; parasites; physicochemical properties; pyridoxal phosphate; pyridoxine
- Abstract:
- ... The chemical properties of the B₆ vitamers are uniquely suited for wide use as cofactors in essential reactions, such as decarboxylations and transaminations. This review addresses current efforts to explore vitamin B₆ dependent enzymatic reactions as drug targets. Several current targets are described that are found amongst these enzymes. The focus is set on diseases caused by protozoan parasites ...
- DOI:
- 10.1016/j.bbapap.2011.07.018
- https://doi.org/10.1016/j.bbapap.2011.07.018
- Author:
- Tathagata Mukherjee; Jeremiah Hanes; Ivo Tews; Steven E. Ealick; Tadhg P. Begley
- Source:
- Biochimica et biophysica acta 2011 v.1814 no.11 pp. 1585-1596
- ISSN:
- 1878-1454
- Subject:
- biosynthesis; chemical reactions; enzymes; enzymology; fungi; oxidative stress; protective effect; pyridoxal phosphate; pyridoxine; singlet oxygen
- Abstract:
- ... Vitamin B₆ is an essential cofactor that participates in a large number of biochemical reactions. Pyridoxal phosphate is biosynthesized de novo by two different pathways (the DXP dependent pathway and the R5P pathway) and can also be salvaged from the environment. It is one of the few cofactors whose catabolic pathway has been comprehensively characterized. It is also known to function as a single ...
- DOI:
- 10.1016/j.bbapap.2011.06.018
- https://doi.org/10.1016/j.bbapap.2011.06.018
- Author:
- Rita Florio; Martino Luigi di Salvo; Mirella Vivoli; Roberto Contestabile
- Source:
- Biochimica et biophysica acta 2011 v.1814 no.11 pp. 1489-1496
- ISSN:
- 1878-1454
- Subject:
- enzymology; glycine hydroxymethyltransferase; metabolism; mutants; pyridoxal; pyridoxal phosphate; serine
- Abstract:
- ... Serine hydroxymethyltransferase is a ubiquitous representative of the family of fold type I, pyridoxal 5′-phosphate-dependent enzymes. The reaction catalyzed by this enzyme, the reversible transfer of the Cβ of serine to tetrahydropteroylglutamate, represents a link between amino acid and folates metabolism and operates as a major source of one-carbon units for several essential biosynthetic proce ...
- DOI:
- 10.1016/j.bbapap.2010.10.010
- https://doi.org/10.1016/j.bbapap.2010.10.010
- Author:
- Susan M. Aitken; Pratik H. Lodha; Dominique J.K. Morneau
- Source:
- Biochimica et biophysica acta 2011 v.1814 no.11 pp. 1511-1517
- ISSN:
- 1878-1454
- Subject:
- active sites; animals; anti-infective agents; bacteria; cystathionine; cystathionine beta-synthase; cystathionine gamma-lyase; cysteine; engineering; enzymology; pyridoxal; pyridoxal phosphate; therapeutics; yeasts
- Abstract:
- ... The diversity of reactions catalyzed by enzymes reliant on pyridoxal 5′-phosphate (PLP) demonstrates the catalytic versatility of this cofactor and the plasticity of the protein scaffolds of the major fold types of PLP-dependent enzymes. The enzymes of the transsulfuration (cystathionine γ-synthase and cystathionine β-lyase) and reverse transsulfuration (cystathionine β-synthase and cystathionine ...
- DOI:
- 10.1016/j.bbapap.2011.03.006
- https://doi.org/10.1016/j.bbapap.2011.03.006
- Author:
- Martino Luigi di Salvo; Roberto Contestabile; Martin K. Safo
- Source:
- Biochimica et biophysica acta 2011 v.1814 no.11 pp. 1597-1608
- ISSN:
- 1570-9639
- Subject:
- animals; enzymatic reactions; enzymes; enzymology; homeostasis; metabolism; pyridoxal; pyridoxal phosphate; pyridoxamine; pyridoxine
- Abstract:
- ... Vitamin B₆ is a generic term referring to pyridoxine, pyridoxamine, pyridoxal and their related phosphorylated forms. Pyridoxal 5′-phosphate is the catalytically active form of vitamin B₆, and acts as cofactor in more than 140 different enzyme reactions. In animals, pyridoxal 5′-phosphate is recycled from food and from degraded B₆-enzymes in a “salvage pathway”, which essentially involves two ubiq ...
- DOI:
- 10.1016/j.bbapap.2010.12.006
- https://doi.org/10.1016/j.bbapap.2010.12.006