An enzyme catalyzing the deamination of pyridoxaminephosphate to pyridoxal phosphate. It is a flavoprotein that also oxidizes pyridoxine-5-phosphate and pyridoxine. EC 1.4.3.5.
A flavoprotein enzyme that catalyzes the univalent reduction of OXYGEN using NADPH as an electron donor to create SUPEROXIDE ANION. The enzyme is dependent on a variety of CYTOCHROMES. Defects in the production of superoxide ions by enzymes such as NADPH oxidase result in GRANULOMATOUS DISEASE, CHRONIC.
An iron-molybdenum flavoprotein containing FLAVIN-ADENINE DINUCLEOTIDE that oxidizes hypoxanthine, some other purines and pterins, and aldehydes. Deficiency of the enzyme, an autosomal recessive trait, causes xanthinuria.
An enzyme that catalyzes the oxidative deamination of naturally occurring monoamines. It is a flavin-containing enzyme that is localized in mitochondrial membranes, whether in nerve terminals, the liver, or other organs. Monoamine oxidase is important in regulating the metabolic degradation of catecholamines and serotonin in neural or target tissues. Hepatic monoamine oxidase has a crucial defensive role in inactivating circulating monoamines or those, such as tyramine, that originate in the gut and are absorbed into the portal circulation. (From Goodman and Gilman's, The Pharmacological Basis of Therapeutics, 8th ed, p415) EC 1.4.3.4.

Update on interconversions of vitamin B-6 with its coenzyme. (1/43)

Biosynthesis of pyridoxal 5'-phosphate (PLP) depends upon the relatively specific action of two consecutive enzymes, viz. pyridoxal (pyridoxine, pyridoxamine) kinase and pyridoxine (pyridoxamine) phosphate oxidase. Less specific phosphatases catalyze hydrolyses of the 5'-phosphates of the vitamers pyridoxal, pyridoxamine, and pyridoxine. From the recognition a generation ago of these processes by which the three forms of vitamin B-6 and their 5'-phosphates are interconverted, more recent studies have provided a fairly sophisticated understanding of the molecular characteristics of the enzymes involved. The evolutionary retention of homologous portions of pyridoxal kinase in humans as well as bacteria and the most recent finding of a highly conserved region of the pyridoxine (pyridoxamine) phosphate oxidase, also from both prokaryotic and eukaryotic organisms, emphasize the importance of these catalysts in the formation of a coenzyme that is essential for most organisms. Both kinase and oxidase involved in B-6 metabolism are potential targets for pharmacologic agents.  (+info)

X-ray structure of Escherichia coli pyridoxine 5'-phosphate oxidase complexed with FMN at 1.8 A resolution. (2/43)

BACKGROUND: Escherichia coli pyridoxine 5'-phosphate oxidase (PNPOx) catalyzes the terminal step in the biosynthesis of pyridoxal 5'-phosphate (PLP), a cofactor used by many enzymes involved in amino acid metabolism. The enzyme oxidizes either the 4'-hydroxyl group of pyridoxine 5'-phosphate (PNP) or the 4'-primary amine of pyridoxamine 5'-phosphate (PMP) to an aldehyde. PNPOx is a homodimeric enzyme with one flavin mononucleotide (FMN) molecule non-covalently bound to each subunit. A high degree of sequence homology among the 15 known members of the PNPOx family suggests that all members of this group have similar three-dimensional folds. RESULTS: The crystal structure of PNPOx from E. coli has been determined to 1.8 A resolution. The monomeric subunit folds into an eight-stranded beta sheet surrounded by five alpha-helical structures. Two monomers related by a twofold axis interact extensively along one-half of each monomer to form the dimer. There are two clefts at the dimer interface that are symmetry-related and extend from the top to the bottom of the dimer. An FMN cofactor that makes interactions with both subunits is located in each of these two clefts. CONCLUSIONS: The structure is quite similar to the recently deposited 2.7 A structure of Saccharomyces cerevisiae PNPOx and also, remarkably, shares a common structural fold with the FMN-binding protein from Desulfovibrio vulgaris and a domain of chymotrypsin. This high-resolution E. coli PNPOx structure permits predictions to be made about residues involved in substrate binding and catalysis. These predictions provide testable hypotheses, which can be answered by making site-directed mutants.  (+info)

Structure and mechanism of Escherichia coli pyridoxine 5'-phosphate oxidase. (3/43)

Escherichia coli pyridoxine 5'-phosphate oxidase (PNPOx) catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP), forming pyridoxal 5'-phosphate (PLP). This reaction serves as the terminal step in the de novo biosynthesis of PLP in E. coli and as a part of the salvage pathway of this coenzyme in both E. coli and mammalian cells. Recent studies have shown that in addition to the active site, PNPOx contains a noncatalytic site that binds PLP tightly. The crystal structures of PNPOx with one and two molecules of PLP bound have been determined. In the active site, the PLP pyridine ring is stacked almost parallel against the re-face of the middle ring of flavin mononucleotide (FMN). A large protein conformational change occurs upon binding of PLP. When the protein is soaked with excess PLP an additional molecule of this cofactor is bound about 11 A from the active site. A possible tunnel exists between the two sites. Site mutants were made of all residues at the active site that make interactions with the substrate. Stereospecificity studies showed that the enzyme is specific for removal of the proR hydrogen atom from the prochiral C4' carbon of PMP. The crystal structure and the stereospecificity studies suggest that the pair of electrons on C4' of the substrate are transferred to FMN as a hydride ion.  (+info)

Structure and properties of recombinant human pyridoxine 5'-phosphate oxidase. (4/43)

Pyridoxine 5'-phosphate oxidase catalyzes the terminal step in the synthesis of pyridoxal 5'-phosphate. The cDNA for the human enzyme has been cloned and expressed in Escherichia coli. The purified human enzyme is a homodimer that exhibits a low catalytic rate constant of approximately 0.2 sec(-1) and K(m) values in the low micromolar range for both pyridoxine 5'phosphate and pyridoxamine 5'-phosphate. Pyridoxal 5'-phosphate is an effective product inhibitor. The three-dimensional fold of the human enzyme is very similar to those of the E. coli and yeast enzymes. The human and E. coli enzymes share 39% sequence identity, but the binding sites for the tightly bound FMN and substrate are highly conserved. As observed with the E. coli enzyme, the human enzyme binds one molecule of pyridoxal 5'-phosphate tightly on each subunit.  (+info)

Characterization of the complex pdxH-tyrS operon of Escherichia coli K-12 and pleiotropic phenotypes caused by pdxH insertion mutations. (5/43)

We report the first molecular genetic analysis of a pyridoxine 5'-phosphate oxidase, the PdxH gene product of Escherichia coli K-12. Chromosomal insertions in and around pdxH were generated with various transposons, and the resulting phenotypes were characterized. The DNA sequence of pdxH was determined, and the promoters of pdxH and the downstream gene tyrS, which encodes tyrosyl-tRNA synthetase, were mapped by RNase T2 protection assays of chromosomal transcripts. These combined approaches led to the following conclusions: (i) pdxH is transcribed from a sigma 70-type promoter and shares its transcript with tyrS; (ii) tyrS is additionally transcribed from a relatively strong, nonconventional internal promoter that may contain an upstream activating sequence but whose expression is unaffected by a fis mutation; (iii) PdxH oxidase is basic, has a molecular mass of 25,545 Da, and shares striking homology (greater than 40% identity) with the developmentally regulated FprA protein of Myxococcus xanthus; (iv) mild pyridoxal 5'-phosphate limitation of pdxH mutants inhibits cell division and leads to formation of unsegregated nucleoids; (v) E. coli PdxH oxidase is required aerobically and anaerobically, but second-site suppressors that replace pdxH function entirely can be isolated; and (vi) pdxH mutants excrete significant amounts of L-glutamate and a compound, probably alpha-ketoisovalerate, that triggers L-valine inhibition of E. coli K-12 strains. These findings extend earlier observations that pyridoxal 5'-phosphate biosynthetic and aminoacyl-tRNA synthetase genes are often members of complex, multifunctional operons. Our results also show that loss of pdxH function seriously disrupts cellular metabolism in unanticipated ways.  (+info)

Genomic organization, tissue distribution and deletion mutation of human pyridoxine 5'-phosphate oxidase. (6/43)

We used a combined computer and biochemical approach to characterize human pyridoxine 5'-phosphate oxidase (PNPO). The human PNPO gene is composed of seven exons and six introns, and spans approximately 8 kb. All exon/intron junctions contain the gt/ag consensus splicing site. The absence of TATA-like sequences, the presence of Sp1-binding sites and more importantly, the presence of CpG islands in the regulatory region of the PNPO gene are characteristic features of housekeeping genes. Northern blot analyses showed two species of poly(A)(+) RNA of approximately 2.4 and approximately 3.4 kb at identical intensity, whereas Western blot analysis showed that no protein isoform exists in any of the tissues examined. PCR-based analysis led to the idea that two messages are transcribed from a single copy gene, and that the size difference is due to differential usage of the polyadenylation signal. The major sites of PNPO expression are liver, skeletal muscle and kidneys while a very weak signal was detected in lung. The mRNA master dot-blot for multiple human tissues provided a complete map of the tissue distribution not only for PNPO but also for pyridoxal kinase and pyridoxal phosphatase. The data indicate that mRNA expression of all three enzymes essential for vitamin B(6) metabolism is ubiquitous but is highly regulated at the level of transcription in a tissue-specific manner. In addition, human brain PNPO cDNA was expressed in Escherichia coli, and the roles of both the N- and C-terminal regions were studied by creating sequential truncation mutants. Our results showed that deletion of the N-terminal 56 residues affects neither the binding of coenzyme nor catalytic activity.  (+info)

Neonatal epileptic encephalopathy caused by mutations in the PNPO gene encoding pyridox(am)ine 5'-phosphate oxidase. (7/43)

In the mouse, neurotransmitter metabolism can be regulated by modulation of the synthesis of pyridoxal 5'-phosphate and failure to maintain pyridoxal phosphate (PLP) levels results in epilepsy. This study of five patients with neonatal epileptic encephalopathy suggests that the same is true in man. Cerebrospinal fluid and urine analyses indicated reduced activity of aromatic L-amino acid decarboxylase and other PLP-dependent enzymes. Seizures ceased with the administration of PLP, having been resistant to treatment with pyridoxine, suggesting a defect of pyridox(am)ine 5'-phosphate oxidase (PNPO). Sequencing of the PNPO gene identified homozygous missense, splice site and stop codon mutations. Expression studies in Chinese hamster ovary cells showed that the splice site (IVS3-1g>a) and stop codon (X262Q) mutations were null activity mutations and that the missense mutation (R229W) markedly reduced pyridox(am)ine phosphate oxidase activity. Maintenance of optimal PLP levels in the brain may be important in many neurological disorders in which neurotransmitter metabolism is disturbed (either as a primary or as a secondary phenomenon).  (+info)

Tat-mediated protein transduction of human brain pyridoxine-5-P oxidase into PC12 cells. (8/43)

Pyridoxine-5-P oxidase catalyses the terminal step in the biosynthesis of pyridoxal-5-P, the biologically active form of vitamin B6 which acts as an essential cofactor. Here, a human brain pyridoxine-5-P oxidase gene was fused with a gene fragment encoding the HIV-1 Tat protein transduction domain (RKKRRQRRR) in a bacterial expression vector to produce a genetic in-frame Tat-pyridoxine-5-P oxidase fusion protein. Expressed and purified Tat-pyridoxine-5-P oxidase fusion protein transduced efficiently into PC12 cells in a time- and dose-dependent manner when added exogenously to culture media. Once inside the cells, the transduced Tat-pyridoxine-5-P oxidase protein showed catalytic activity and was stable for 48 h. Moreover, the formation of pyridoxal-5-P was increased by adding exogenous Tat-pyridoxine-5-P oxidase to media pre-treated with the vitamin B6 precursor pyridoxine. In addition, the intracellular concentration of pyridoxal-5-P was markedly increased when Tat-pyridoxal kinase was transduced together with Tat-pyridoxine-5-P oxidase into cells.These results suggest that the transduction of Tat-pyridoxine-5-P oxidase fusion protein presents a means of regulating the level of pyridoxal-5-P and of replenishing this enzyme in various neurological disorders related to vitamin B6.  (+info)

Pyridoxamine Phosphate Oxidase (PNPO) is an enzyme that is involved in the metabolism of the vitamin B6. The protein code for this enzyme is PNPO, and its systematic name is pyridoxamine 5'-phosphate:oxygen oxidoreductase (dephosphorylating).

The primary function of Pyridoxamine Phosphate Oxidase is to convert pyridoxamine phosphate (PMP) into pyridoxal 5'-phosphate (PLP), which is an active form of vitamin B6 and a cofactor for many enzymatic reactions in the body, particularly those involved in amino acid metabolism.

Deficiency or dysfunction of Pyridoxamine Phosphate Oxidase can lead to neurological disorders and seizures, as PLP is essential for the synthesis of neurotransmitters and other vital compounds in the brain.

NADPH oxidase is an enzyme complex that plays a crucial role in the production of reactive oxygen species (ROS) in various cell types. The primary function of NADPH oxidase is to catalyze the transfer of electrons from NADPH to molecular oxygen, resulting in the formation of superoxide radicals. This enzyme complex consists of several subunits, including two membrane-bound components (gp91phox and p22phox) and several cytosolic components (p47phox, p67phox, p40phox, and rac1 or rac2). Upon activation, these subunits assemble to form a functional enzyme complex that generates ROS, which serve as important signaling molecules in various cellular processes. However, excessive or uncontrolled production of ROS by NADPH oxidase has been implicated in the pathogenesis of several diseases, such as cardiovascular disorders, neurodegenerative diseases, and cancer.

Xanthine oxidase is an enzyme that catalyzes the oxidation of xanthine to uric acid, which is the last step in purine metabolism. It's a type of molybdenum-containing oxidoreductase that generates reactive oxygen species (ROS) during its reaction mechanism.

The enzyme exists in two interconvertible forms: an oxidized state and a reduced state. The oxidized form, called xanthine oxidase, reduces molecular oxygen to superoxide and hydrogen peroxide, while the reduced form, called xanthine dehydrogenase, reduces NAD+ to NADH.

Xanthine oxidase is found in various tissues, including the liver, intestines, and milk. An overproduction of uric acid due to increased activity of xanthine oxidase can lead to hyperuricemia, which may result in gout or kidney stones. Some medications and natural compounds are known to inhibit xanthine oxidase, such as allopurinol and febuxostat, which are used to treat gout and prevent the formation of uric acid stones in the kidneys.

Monoamine oxidase (MAO) is an enzyme found on the outer membrane of mitochondria in cells throughout the body, but primarily in the gastrointestinal tract, liver, and central nervous system. It plays a crucial role in the metabolism of neurotransmitters and dietary amines by catalyzing the oxidative deamination of monoamines. This enzyme exists in two forms: MAO-A and MAO-B, each with distinct substrate preferences and tissue distributions.

MAO-A preferentially metabolizes serotonin, norepinephrine, and dopamine, while MAO-B is mainly responsible for breaking down phenethylamines and benzylamines, as well as dopamine in some cases. Inhibition of these enzymes can lead to increased neurotransmitter levels in the synaptic cleft, which has implications for various psychiatric and neurological conditions, such as depression and Parkinson's disease. However, MAO inhibitors must be used with caution due to their potential to cause serious adverse effects, including hypertensive crises, when combined with certain foods or medications containing dietary amines or sympathomimetic agents.

... by the enzymes pyridoxamine-phosphate transaminase or pyridoxine 5'-phosphate oxidase, the latter of which also catalyzes the ... Pyridoxine 5'-phosphate oxidase is dependent on flavin mononucleotide (FMN) as a cofactor produced from riboflavin (vitamin B2 ... 4-Pyridoxic acid is formed by the action of aldehyde oxidase in the liver. Amounts excreted increase within 1-2 weeks with ... PLP is restored via a salvage pathway that requires three key enzymes, pyridoxal kinase, pyridoxine 5'-phosphate oxidase, and ...
... sarcosine oxidase MeSH D08.811.682.662.640 - proline oxidase MeSH D08.811.682.662.680 - pyridoxamine-phosphate oxidase MeSH ... d-amino-acid oxidase MeSH D08.811.682.664.500.261 - d-aspartate oxidase MeSH D08.811.682.664.500.398 - glutamate dehydrogenase ... proline oxidase MeSH D08.811.682.664.500.848 - protein-lysine 6-oxidase MeSH D08.811.682.664.500.924 - valine dehydrogenase ( ... galactose oxidase MeSH D08.811.682.047.239 - glucose oxidase MeSH D08.811.682.047.370 - homoserine dehydrogenase MeSH D08.811. ...
In these reactions, the PLP reacts with glutamate, which transfers its alpha-amino group to PLP to make pyridoxamine phosphate ... The final enzyme is PNP oxidase (pdxH), which catalyzes the oxidation of the 4' hydroxyl group to an aldehyde using dioxigen, ...
... by the enzymes pyridoxamine-phosphate transaminase or pyridoxine 5-phosphate oxidase, the latter of which also catalyzes the ... Pyridoxine 5-phosphate oxidase is dependent on flavin mononucleotide (FMN) as a cofactor produced from riboflavin (vitamin B2 ... 4-Pyridoxic acid is formed by the action of aldehyde oxidase in the liver. Amounts excreted increase within 1-2 weeks with ... PLP is restored via a salvage pathway that requires three key enzymes, pyridoxal kinase, pyridoxine 5-phosphate oxidase, and ...
Pyridoxaminephosphate Oxidase Preferred Term Term UI T034686. Date01/01/1999. LexicalTag NON. ThesaurusID NLM (1975). ... Pyridoxine-5-Phosphate Oxidase Narrower Concept UI. M0018245. Registry Number. 0. Terms. Pyridoxine-5-Phosphate Oxidase ... Pyridoxaminephosphate Oxidase Preferred Concept UI. M0018244. Registry Number. EC 1.4.3.5. Scope Note. An enzyme catalyzing the ... Pyridoxine-5-Phosphate Oxidase Pyridoxinephosphate Oxidase Registry Number. EC 1.4.3.5. CAS Type 1 Name. Pyridoxamine 5- ...
pyridoxamine-phosphate oxidase activity of 2xPNPO:2xFMN [cytosol] Physical Entity 2xPNPO:2xFMN [cytosol] (Homo sapiens) ... Pyridoxine-5-phosphate oxidase (PNPO) is able to oxidize pyridoxine phosphate (PDXP) to pyridoxal 5-phosphate (PXLP) (Kang et ... Genomic organization, tissue distribution and deletion mutation of human pyridoxine 5-phosphate oxidase Won, MH, Hong, ML, ...
GO:0004733; Molecular function: pyridoxamine-phosphate oxidase activity. GO:0010181; Molecular function: FMN binding. GO: ...
... pyridoxamine-phosphate oxidase MeSH ... d-amino-acid oxidase MeSH D08.811.682.664.500.261 - d-aspartate oxidase MeSH D08.811. ... Catechol Oxidase Entry term(s). Diphenol Oxidase Diphenol Oxidases Oxidase, Catechol Oxidase, Diphenol Oxidase, Polyphenol ... ... Catechol oxidase Entry term(s):. Diphenol Oxidase. Diphenol Oxidases. Oxidase, Catechol. Oxidase, Diphenol. Oxidase, Polyphenol ... Amine oxidase. [flavin-. containing] A. Amine oxidase. [flavin- ... oxidase. [copper-. containing]. Amine oxidase. [flavin-. ...
Piridoxaminafosfato Oxidase/classificação , Piridoxaminafosfato Oxidase/genética , Especificidade por Substrato ... Pyridoxal phosphate, pyridoxamine phosphate, and folic acid based on ceRNA regulatory network as potential biomarkers for the ... An LC-MS/MS-Based Method for the Quantification of Pyridox(am)ine 5-Phosphate Oxidase Activity in Dried Blood Spots from ... Here, we show that the PMP/PNP oxidase PDX3 is essential for balancing B6 vitamer levels in Arabidopsis thaliana. In the ...
Pyridoxaminephosphate Oxidase [D08.811.682.662.680] Pyridoxaminephosphate Oxidase * 1-Pyrroline-5-Carboxylate Dehydrogenase [ ...
Pyridoxaminephosphate Oxidase. *Pyrroline Carboxylate Reductases. *Saccharopine Dehydrogenases. *Tetrahydrofolate Dehydrogenase ...
Other name(s): pyridoxamine 5-phosphate oxidase; pyridoxamine phosphate oxidase; pyridoxine (pyridoxamine)phosphate oxidase; ... EC 1.4.3.1 D-aspartate oxidase. EC 1.4.3.2 L-amino-acid oxidase. EC 1.4.3.3 D-amino-acid oxidase. EC 1.4.3.4 amine oxidase. EC ... EC 1.4.3.19 glycine oxidase. EC 1.4.3.20 L-lysine 6-oxidase. EC 1.4.3.21 primary-amine oxidase. EC 1.4.3.22 diamine oxidase. EC ... Other name(s): adrenalin oxidase; adrenaline oxidase; amine oxidase (ambiguous); amine oxidase (flavin-containing); amine: ...
Pyridoxamine-phosphate oxidases and pyridoxamine-phosphate oxidase-related proteins catalyze the oxidation of 6-NAD(P)H to NAD( ... Pyridoxamine-phosphate oxidases and pyridoxamine-phosphate oxidase-related proteins catalyze the oxidation of 6-NAD(P)H to NAD( ... Remarkably, pyridoxamine-phosphate oxidase-related proteins (PNPO-RP) from Nostoc punctiforme, A. thaliana and the yeast S. ... The history of renalase from amine oxidase to a a-NAD(P)H-oxidase/anomerase]. Severina IS, Fedchenko VI, Veselovsky AV, ...
Pyridoxaminephosphate Oxidase / deficiency Actions. * Search in PubMed * Search in MeSH * Add to Search ... This includes pyridox(am)ine phosphate oxidase deficiency (a disorder affecting PLP synthesis and recycling), disorders ...
Pyridoxamine phosphate oxidase Entry term(s):. Oxidase, Pyridoxaminephosphate. Oxidase, Pyridoxine-5-Phosphate. Oxidase, ... Pyridoxaminephosphate Oxidase Entry term(s). Oxidase, Pyridoxaminephosphate Oxidase, Pyridoxinephosphate Pyridoxinephosphate ... Pyridoxine 5 Phosphate Oxidase. Pyridoxine-5-Phosphate Oxidase. Pyridoxinephosphate Oxidase. Tree number(s):. D08.811.682.662. ... Pyridoxaminephosphate Oxidase - Preferred Concept UI. M0018244. Scope note. An enzyme catalyzing the deamination of ...
Pyridoxaminephosphate Oxidase Preferred Term Term UI T034686. Date01/01/1999. LexicalTag NON. ThesaurusID NLM (1975). ... Pyridoxine-5-Phosphate Oxidase Narrower Concept UI. M0018245. Registry Number. 0. Terms. Pyridoxine-5-Phosphate Oxidase ... Pyridoxaminephosphate Oxidase Preferred Concept UI. M0018244. Registry Number. EC 1.4.3.5. Scope Note. An enzyme catalyzing the ... Pyridoxine-5-Phosphate Oxidase Pyridoxinephosphate Oxidase Registry Number. EC 1.4.3.5. CAS Type 1 Name. Pyridoxamine 5- ...
Pyridoxamine-phosphate oxidase (substance). Code System Preferred Concept Name. Pyridoxamine-phosphate oxidase (substance). ...
... pyridoxamine-phosphate oxidase). Links to other databases:. BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 131554-04- ...
N0000168225 Pyridoxal Kinase N0000007581 Pyridoxal Phosphate N0000167221 Pyridoxamine N0000167879 Pyridoxaminephosphate Oxidase ... ol-enkephalin N0000168380 D-Alanine Transaminase N0000167841 D-Amino-Acid Oxidase N0000167827 D-Aspartate Oxidase N0000170285 D ... N0000167826 L-Amino Acid Oxidase N0000167894 L-Aminoadipate-Semialdehyde Dehydrogenase N0000167967 L-Gulonolactone Oxidase ... Serpentine N0000167795 Ascorbate Oxidase N0000183527 Ascorbate Peroxidases N0000006439 Ascorbic Acid N0000169160 ...
Pyridones Pyridostigmine Bromide Pyridoxal Pyridoxal Kinase Pyridoxal Phosphate Pyridoxamine Pyridoxaminephosphate Oxidase ... ol-enkephalin D-Alanine Transaminase D-Amino-Acid Oxidase D-Aspartate Oxidase D-Aspartic Acid D-Xylulose Reductase Dacarbazine ... L Forms L-Amino Acid Oxidase L-Aminoadipate-Semialdehyde Dehydrogenase L-Gulonolactone Oxidase L-Iditol 2-Dehydrogenase L- ... Physiologic Monkey Diseases Monkeypox Monkeypox virus Monoacylglycerol Lipases Monoamine Oxidase Monoamine Oxidase Inhibitors ...
Pyridoxaminephosphate Oxidase. *Pyrroline Carboxylate Reductases. *Saccharopine Dehydrogenases. *Tetrahydrofolate Dehydrogenase ...
1. Pyridoxine-5-phosphate oxidase. General function:. Involved in pyridoxamine-phosphate oxidase activity. Specific function: ... In particular, pyridoxamine can be converted into pyridoxal; which is mediated by the enzyme pyridoxine-5-phosphate oxidase. ...
Their increase could be caused by a reduced monoamine oxidase activity or by an increased acylation in schizophrenic patients. ... A complete half-transamination of pyridoxal phosphate to pyridoxamine phosphate by aspartate or by cysteine sulfinate can be ...
A chemically competent derivative of pyridoxamine phosphate was incorporated into the C-peptide fragments of these non-covalent ... R2-like ligand-binding oxidase (R2lox). *Rabbit serum albumin (RSA). *Ribonuclease S ... The chimeric Pam residue integrates the heterocyclic functionality of pyridoxamine phosphate into the side chain of an alpha- ...
  • Molecular function: pyridoxamine-phosphate oxidase activity. (expasy.org)
  • Absorbed pyridoxine (PN) is converted to pyridoxamine 5'-phosphate (PMP) by the enzyme pyridoxal kinase, with PMP further converted to pyridoxal 5'-phosphate (PLP), the metabolically active form, by the enzymes pyridoxamine-phosphate transaminase or pyridoxine 5'-phosphate oxidase, the latter of which also catalyzes the conversion of pyridoxine 5′-phosphate (PNP) to PLP. (wikipedia.org)
  • An enzyme catalyzing the deamination of pyridoxaminephosphate to pyridoxal phosphate. (nih.gov)
  • Pyridoxine-5'-phosphate oxidase (PNPO) is able to oxidize pyridoxine phosphate (PDXP) to pyridoxal 5'-phosphate (PXLP) (Kang et al. (reactome.org)
  • We partially purified an enzyme oxidizing 6-NADPH from rat liver, and, surprisingly, identified it as pyridoxamine-phosphate oxidase (PNPO). (nih.gov)
  • Absorbed pyridoxine (PN) is converted to pyridoxamine 5'-phosphate (PMP) by the enzyme pyridoxal kinase, with PMP further converted to pyridoxal 5'-phosphate (PLP), the metabolically active form, by the enzymes pyridoxamine-phosphate transaminase or pyridoxine 5'-phosphate oxidase, the latter of which also catalyzes the conversion of pyridoxine 5′-phosphate (PNP) to PLP. (wikipedia.org)
  • An enzyme catalyzing the deamination of pyridoxaminephosphate to pyridoxal phosphate. (bvsalud.org)
  • which is mediated by the enzyme pyridoxine-5'-phosphate oxidase. (hmdb.ca)