pyridoxamine phosphate
pyridoxamine phosphate structure
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Common Name | pyridoxamine phosphate | ||
|---|---|---|---|---|
| CAS Number | 529-96-4 | Molecular Weight | 248.17300 | |
| Density | 1.559g/cm3 | Boiling Point | 607.3ºC at 760 mmHg | |
| Molecular Formula | C8H13N2O5P | Melting Point | N/A | |
| MSDS | USA | Flash Point | 321.1ºC | |
| Symbol |
GHS07 |
Signal Word | Warning | |
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Fungal recognition enhances mannose receptor shedding through dectin-1 engagement.
J. Biol. Chem. 286(10) , 7822-9, (2011) The mannose receptor (MR) is an endocytic type I membrane molecule with a broad ligand specificity that is involved in both hemostasis and pathogen recognition. Membrane-anchored MR is cleaved by a metalloproteinase into functional soluble MR (sMR) composed o... |
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The intestine plays a substantial role in human vitamin B6 metabolism: a Caco-2 cell model.
PLoS ONE 8(1) , e54113, (2013) Vitamin B6 is present in various forms (vitamers) in the diet that need to be metabolized to pyridoxal phosphate (PLP), the active cofactor form of vitamin B6. In literature, the liver has been reported to be the major site for this conversion, whereas the ex... |
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Interaction between glutamate dehydrogenase (GDH) and L-leucine catabolic enzymes: intersecting metabolic pathways.
Neurochem. Int. 59 , 518-524, (2011) Branched-chain amino acids (BCAAs) catabolism follows sequential reactions and their metabolites intersect with other metabolic pathways. The initial enzymes in BCAA metabolism, the mitochondrial branched-chain aminotransferase (BCATm), which deaminates the B... |
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Crystal structures of the PLP- and PMP-bound forms of BtrR, a dual functional aminotransferase involved in butirosin biosynthesis.
Proteins 65(1) , 220-30, (2006) The aminotransferase (BtrR), which is involved in the biosynthesis of butirosin, a 2-deoxystreptamine (2-DOS)-containing aminoglycoside antibiotic produced by Bacillus circulans, catalyses the pyridoxal phosphate (PLP)-dependent transamination reaction both o... |
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Cofactor-directed reversible denaturation pathways: the cofactor-stabilized Escherichia coli aspartate aminotransferase homodimer unfolds through a pathway that differs from that of the apoenzyme.
Biochemistry 46(19) , 5819-29, (2007) While the urea-mediated unfolding pathway of the Escherichia coli aspartate aminotransferase (eAATase) homodimer proceeds through a reversible three-state process with a partially folded dimeric intermediate, D D* 2U (E. Deu and J. F. Kirsch, accompanying pap... |
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Insights into the mechanism of oxidative deamination catalyzed by DOPA decarboxylase.
Biochemistry 47(27) , 7187-95, (2008) The unusual oxygen-consuming oxidative deamination reaction catalyzed by the pyridoxal 5'-phosphate (PLP) enzyme DOPA decarboxylase (DDC) was here investigated. Either wild-type or Y332F DDC variant is able to perform such oxidation toward aromatic amines or ... |
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The structure of NtdA, a sugar aminotransferase involved in the kanosamine biosynthetic pathway in Bacillus subtilis, reveals a new subclass of aminotransferases.
J. Biol. Chem. 288(47) , 34121-30, (2013) NtdA from Bacillus subtilis is a sugar aminotransferase that catalyzes the pyridoxal phosphate-dependent equatorial transamination of 3-oxo-α-D-glucose 6-phosphate to form α-D-kanosamine 6-phosphate. The crystal structure of NtdA shows that NtdA shares the co... |
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Spectral and kinetic characterization of 7,8-diaminopelargonic acid synthase from Mycobacterium tuberculosis.
IUBMB Life 58(4) , 225-33, (2006) The indispensability of biotin for crucial processes like lipid biosynthesis coupled to the absence of the biotin biosynthesis pathway in humans make the enzymes of this pathway, attractive targets for development of novel drugs against numerous pathogens inc... |
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Purification and characterization of pyridoxine 5'-phosphate phosphatase from Sinorhizobium meliloti.
Biosci. Biotechnol. Biochem. 69(12) , 2277-84, (2005) Here we report the purification and biochemical characterization of a pyridoxine 5'-phosphate phosphatase involved in the biosynthesis of pyridoxine in Sinorhizobium meliloti. The phosphatase was localized in the cytoplasm and purified to electrophoretic homo... |
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Crystal structure of glutamate-1-semialdehyde aminotransferase from Bacillus subtilis with bound pyridoxamine-5'-phosphate.
Biochem. Biophys. Res. Commun. 402(2) , 356-60, (2010) Glutamate-1-semialdehyde aminotransferase (GSA-AT), also named glutamate-1-semialdehyde aminomutase (GSAM), a pyridoxamine-5'-phosphate (PMP)/pyridoxal-5'-phosphate (PLP) dependent enzyme, catalyses the transamination of the substrate glutamate-1-semialdehyde... |