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This role is performed by the active form, pyridoxal phosphate.
For example, R138W is known to disrupt to pyridoxal phosphate binding site.
Pyridoxal phosphate is involved in the metabolism of histamine.
Pyridoxal phosphate has been implicated in increasing or decreasing the expression of certain genes.
Pyridoxal phosphate is a prosthetic group of this enzyme.
The enzyme uses pyridoxal phosphate, the active form of vitamin B6, as a cofactor.
Pyridoxal phosphate is involved in almost all amino acid metabolism, from synthesis to breakdown.
Inadequate levels of pyridoxal phosphate in the brain can cause neurological dysfunction, particularly epilepsy.
In this configuration, the radical is stablizied by the pi-system of pyridoxal phosphate.
Pyridoxal phosphate is required as a coenzyme.
It has 2 cofactors: pyridoxal phosphate, and Potassium.
Vitamin B6 (pyridoxal phosphate) is needed for the metabolism of several amines, which act as important messengers within the brain.
Pyridoxal phosphate is needed as a cofactor for the enzymes that allow selenium to be used from the dietary form.
The trapped pyridoxine and pyridoxamine are oxidized to pyridoxal phosphate in the tissue.
It employs one cofactor, pyridoxal phosphate.
The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor.
This enzyme requires pyridoxal phosphate.
Pyridoxal phosphate de-activation by pyrroline-5-carboxylic acid.
They are natural toxins that cause slow binding inhibition by interfering with the coenzyme pyridoxal phosphate.
Transamination: Transaminase enzymes needed to break down amino acids are dependent on the presence of pyridoxal phosphate.
When plasma pyridoxal phosphate is less than 10nmol/L, it is indicative of vitamin B deficiency.
Pyridoxal phosphate links with basic residues (in this case Lys680) and covalently forms a Schiff base.
The pyridoxal phosphate cofactor binds lysine 69 at the C-terminus end of the barrel domain.
Lys-680 is involved in binding the pyridoxal phosphate, which is the active form of vitamin B, a cofactor required by myophosphorylase.
They react in the presence of a synthase complex consisting of Pdx1 and Pdx2, and form pyridoxal phosphate.