Results 31 to 40 of about 39,888 (206)

PYRIDOXAL-5'-PHOSPHATE INHIBITION OF PLATELET FUNCTION.

open access: yes, 1979
PYRIDOXAL-5'-PHOSPHATE INHIBITION OF PLATELET ...
ELIZABETH HARRIET. KORNECKI (7959149)
core  

Catalytic Mechanism of Pyridoxal 5′-Phosphate-Dependent Aminodeoxychorismate Lyase: A Computational QM/MM Study

open access: yes, 2023
Aminodeoxychorismate lyase (ADCL) is a kind of pyridoxal-5′-phosphate (PLP)-dependent enzyme that catalyzes the conversion of 4-amino-4-deoxychorismate (ADC) to p-aminobenzoate (PABA), which is a key step for the biosynthesis of folate. To illuminate the
Lihua Dong   +3 more
core   +1 more source

Chemical Composition, Amino Acids, Phenolic Profiles and Bioavailability of Minerals in Livingstone Potato (Plectranthus esculentus) as Affected by Different Processing Techniques

open access: yesFood Chemistry International, EarlyView.
Boiling retained the nutrients and polyphenol compounds in Plectranthus esculentus tubers better than frying or roasting. A bioavailability study showed that the phytates and oxalates in the tuber may not affect the bioavailabilities of calcium, zinc, or iron in Plectranthus esculentus tubers when eaten.
Mercy Amarachi Iroaganachi   +4 more
wiley   +1 more source

Discovery and Characterization of Pyridoxal 5’-Phosphate-Dependent Cycloleucine Synthases

open access: yes
Pyridoxal 5’-phosphate (PLP)-dependent enzymes are the most versatile biocatalysts for synthesizing non proteinogenic amino acids. a,a-disubstituted quaternary amino acids, such as 1-amino-1-cyclopentanecarboxylic acid (cycloleucine), are useful building
David A., Delgadillo   +9 more
core   +1 more source

Biological Role of Carbamoyl pyridoxal 5'-phosphate

open access: yes, 1997
A new compound, carbamoyl-pyridoxal 5'-phosphate (C-PLP), was synthetized by condensation of pyridoxal 5'-phosphate (PLP) with KCNO. It may be obtained under certain physiological conditions of pH, temperature and concentration of reagents. Formation and
Marinello, Enrico   +6 more
core   +1 more source

Modification of Pepsinogen with Pyridoxal Phosphate

open access: yesJournal of Biological Chemistry, 1974
Pyridoxal-PO4 binds to pepsinogen in a reaction in which the stoichiometry is highly dependent on the conformation of the protein. When pepsinogen is in its native conformation, pyridoxal-PO4 forms Schiff bases with the α-NH2 group of Leu1 and the e-NH2 group of Lys358.
openaire   +2 more sources

Infused Tiger Nut and Almond Nut Crunchy Snacks Enhanced the Nutritional Value and Antioxidant Activity in High‐Fat Diet Fed Rat

open access: yesFood Chemistry International, EarlyView.
Crunches were produced from formulations of almond nuts and tiger nuts (AN–TN) for the plausible management of commodity disease of obese condition. The produced AN–TN crunches showed high consumers acceptability, phenolic, and amylopectin contents. In addition, formulated percentages of AN–TN crunches when fed to high‐fat diet (HFD) fed rats led to ...
Olufunke Florence Ajeigbe   +4 more
wiley   +1 more source

Reconstitution of the pyridoxal 5'-phosphate (PLP) dependent enzyme serine palmitoyltransferase (SPT) with pyridoxal reveals a crucial role for the phosphate during catalysis [PDF]

open access: yes, 2013
The pyridoxal 5'-phosphate (PLP)-dependent enzyme serine palmitoyltransferase (SPT) is required for de novo sphingolipid biosynthesis. A previous study revealed a novel and unexpected interaction between the hydroxyl group of the l-serine substrate and ...
Wadsworth, John M   +5 more
core   +1 more source

Effect of pyridoxal 5’-phosphate on human neutrophil aggregation in vitro

open access: yes, 1995
Pyridoxal 5′-phosphate inhibited polymorphonuclear leukocyte aggregation in vitro in a dose-dependent fashion at concentrations ranging from 0.5 to 0.001 mmol/l.
Schinella M   +3 more
core   +1 more source

Current Insight into Human Ornithine Aminotransferase: A Review

open access: yesProteins: Structure, Function, and Bioinformatics, EarlyView.
ABSTRACT Human ornithine aminotransferase (hOAT) is a mitochondrial matrix pyridoxal‐5′‐phosphate enzyme (PLP) that catalyzes the reversible transfer of the δ‐amino group of L‐ornithine (L‐Orn) to α‐ketoglutarate (α‐KG) yielding glutamate‐5‐semialdehyde (GSA) and glutamate. GSA is prone to cyclize to Δ1‐pyrroline‐5‐carboxylate.
Fulvio Floriani   +2 more
wiley   +1 more source

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