pyridoxal phosphate has been researched along with Oxaluria, Primary in 6 studies
Pyridoxal Phosphate: This is the active form of VITAMIN B 6 serving as a coenzyme for synthesis of amino acids, neurotransmitters (serotonin, norepinephrine), sphingolipids, aminolevulinic acid. During transamination of amino acids, pyridoxal phosphate is transiently converted into pyridoxamine phosphate (PYRIDOXAMINE).
pyridoxal 5'-phosphate : The monophosphate ester obtained by condensation of phosphoric acid with the primary hydroxy group of pyridoxal.
| Excerpt | Relevance | Reference |
|---|---|---|
| "The autosomal recessive disorder primary hyperoxaluria type 1 (PH1) is caused by a deficiency of the liver-specific pyridoxal-phosphate-dependent enzyme alanine:glyoxylate aminotransferase (AGT)." | 1.31 | Functional synergism between the most common polymorphism in human alanine:glyoxylate aminotransferase and four of the most common disease-causing mutations. ( Danpure, CJ; Lumb, MJ, 2000) |
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 3 (50.00) | 29.6817 |
| 2010's | 2 (33.33) | 24.3611 |
| 2020's | 1 (16.67) | 2.80 |
| Authors | Studies |
|---|---|
| Gatticchi, L | 1 |
| Dindo, M | 1 |
| Pampalone, G | 1 |
| Conter, C | 1 |
| Cellini, B | 3 |
| Takayama, T | 1 |
| Oppici, E | 2 |
| Fodor, K | 1 |
| Paiardini, A | 1 |
| Williams, C | 1 |
| Voltattorni, CB | 1 |
| Wilmanns, M | 1 |
| Hopper, ED | 1 |
| Pittman, AM | 1 |
| Fitzgerald, MC | 1 |
| Tucker, CL | 1 |
| Montioli, R | 1 |
| Lorenzetto, A | 1 |
| Bianconi, S | 1 |
| Borri Voltattorni, C | 1 |
| Coulter-Mackie, MB | 1 |
| Lian, Q | 1 |
| Wong, SG | 1 |
| Lumb, MJ | 1 |
| Danpure, CJ | 1 |
| Trial | Phase | Enrollment | Study Type | Start Date | Status | ||
|---|---|---|---|---|---|---|---|
| Efficacy of Betaine for Reduction of Urine Oxalate in Patients With Type 1 Primary Hyperoxaluria[NCT00283387] | Phase 2 | 15 participants (Actual) | Interventional | 2007-02-28 | Completed | ||
| [information is prepared from clinicaltrials.gov, extracted Sep-2024] | |||||||
"The patients were randomly assigned oral betaine or placebo for 2 months, followed by a 2 month washout. Each patient then received the alternate study medication for 2 months.~Urinary Oxalate Excretion was measured by oxalate oxidase. Two 24 hour urine collections were obtained at baseline, and during the eighth week of each study period." (NCT00283387)
Timeframe: baseline, 2 months, 6 months
| Intervention | umol/mg (Mean) |
|---|---|
| Betaine | 1.43 |
| Placebo | 1.04 |
6 other studies available for pyridoxal phosphate and Oxaluria, Primary
| Article | Year |
|---|---|
Biochemical and cellular effects of a novel missense mutation of the AGXT gene associated with Primary Hyperoxaluria Type 1.
Topics: Glyoxylates; Humans; Hyperoxaluria, Primary; Mutation; Mutation, Missense; Pyridoxal Phosphate; Tran | 2023 |
Crystal structure of the S187F variant of human liver alanine: glyoxylate [corrected] aminotransferase associated with primary hyperoxaluria type I and its functional implications.
Topics: Alanine; Catalytic Domain; Crystallography, X-Ray; Humans; Hyperoxaluria, Primary; Liver; Models, Mo | 2013 |
In vivo and in vitro examination of stability of primary hyperoxaluria-associated human alanine:glyoxylate aminotransferase.
Topics: Alleles; Enzyme Stability; Genetic Complementation Test; Humans; Hyperoxaluria, Primary; Ligands; Mu | 2008 |
Biochemical analyses are instrumental in identifying the impact of mutations on holo and/or apo-forms and on the region(s) of alanine:glyoxylate aminotransferase variants associated with primary hyperoxaluria type I.
Topics: Animals; Apoproteins; Circular Dichroism; Computational Biology; Enzyme Stability; Escherichia coli; | 2012 |
Overexpression of human alanine:glyoxylate aminotransferase in Escherichia coli: renaturation from guanidine-HCl and affinity for pyridoxal phosphate co-factor.
Topics: Base Sequence; DNA, Complementary; Escherichia coli; Gene Expression; Guanidine; Humans; Hyperoxalur | 2005 |
Functional synergism between the most common polymorphism in human alanine:glyoxylate aminotransferase and four of the most common disease-causing mutations.
Topics: Amino Acid Substitution; Catalysis; Dimerization; Enzyme Stability; Escherichia coli; Humans; Hydrog | 2000 |