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5,10-methylenetetrahydrofolate
tetrahydrofolate derivatives
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requirement, if L-serine is substrate
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5,10-methylenetetrahydrofolate
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5,10-methylenetetrahydrofolate
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5,10-methylenetetrahydrofolate
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5,10-methylenetetrahydrofolate
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5,10-methylenetetrahydrofolate
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5,10-methylenetetrahydrofolate
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5,10-methylenetetrahydrofolate
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5,10-methylenetetrahydrofolate
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5,10-methylenetetrahydrofolate
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5,10-methylenetetrahydrofolate
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5,10-methylenetetrahydrofolate
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5,10-methylenetetrahydrofolate
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5,10-methylenetetrahydrofolate
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5,10-methylenetetrahydrofolate
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5,10-methylenetetrahydrofolate
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5,10-methylenetetrahydrofolate
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5,10-methylenetetrahydrofolate
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5,10-methylenetetrahydrofolate
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5,10-methylenetetrahydrofolate
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pyridoxal 5'-phosphate
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pyridoxal 5'-phosphate
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pyridoxal 5'-phosphate
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pyridoxal 5'-phosphate
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pyridoxal 5'-phosphate
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pyridoxal 5'-phosphate
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pyridoxal 5'-phosphate
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pyridoxal 5'-phosphate
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pyridoxal 5'-phosphate
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pyridoxal 5'-phosphate
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pyridoxal 5'-phosphate
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pyridoxal 5'-phosphate
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pyridoxal 5'-phosphate
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pyridoxal 5'-phosphate
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pyridoxal 5'-phosphate
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pyridoxal 5'-phosphate
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pyridoxal 5'-phosphate
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pyridoxal 5'-phosphate
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pyridoxal 5'-phosphate
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pyridoxal 5'-phosphate
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pyridoxal 5'-phosphate
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pyridoxal 5'-phosphate
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pyridoxal 5'-phosphate
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pyridoxal 5'-phosphate
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dependent on
pyridoxal 5'-phosphate
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dependent on
pyridoxal 5'-phosphate
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dependent on
pyridoxal 5'-phosphate
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dependent on
pyridoxal 5'-phosphate
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dependent on
pyridoxal 5'-phosphate
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dependent on
pyridoxal 5'-phosphate
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dependent on
pyridoxal 5'-phosphate
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dependent on
pyridoxal 5'-phosphate
-
dependent on
pyridoxal 5'-phosphate
dependent on
pyridoxal 5'-phosphate
dependent on
pyridoxal 5'-phosphate
dependent on
pyridoxal 5'-phosphate
dependent on
pyridoxal 5'-phosphate
dependent on
pyridoxal 5'-phosphate
dependent on
pyridoxal 5'-phosphate
dependent on
pyridoxal 5'-phosphate
dependent on
pyridoxal 5'-phosphate
dependent on
pyridoxal 5'-phosphate
dependent on
pyridoxal 5'-phosphate
dependent on
pyridoxal 5'-phosphate
dependent on
pyridoxal 5'-phosphate
dependent on
pyridoxal 5'-phosphate
dependent on
pyridoxal 5'-phosphate
dependent on
pyridoxal 5'-phosphate
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2 mol per mol enzyme
pyridoxal 5'-phosphate
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2 mol per mol enzyme
pyridoxal 5'-phosphate
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stimulates activity
pyridoxal 5'-phosphate
stimulates activity
pyridoxal 5'-phosphate
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requirement, 4 mol per mol enzyme
pyridoxal 5'-phosphate
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requirement, 4 mol per mol enzyme
pyridoxal 5'-phosphate
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requirement, 4 mol per mol enzyme
pyridoxal 5'-phosphate
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requirement, 4 mol per mol enzyme
pyridoxal 5'-phosphate
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requirement, 4 mol per mol enzyme
pyridoxal 5'-phosphate
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requirement, 4 mol per mol enzyme
pyridoxal 5'-phosphate
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not essential
pyridoxal 5'-phosphate
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one mol/subunit bound to the epsilon-amino group of lysine
pyridoxal 5'-phosphate
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one mol/subunit bound to the epsilon-amino group of lysine
pyridoxal 5'-phosphate
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one mol/subunit bound to the epsilon-amino group of lysine
pyridoxal 5'-phosphate
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one mol/subunit bound to the epsilon-amino group of lysine
pyridoxal 5'-phosphate
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one mol/subunit bound to the epsilon-amino group of lysine
pyridoxal 5'-phosphate
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one mol/subunit bound to the epsilon-amino group of lysine
pyridoxal 5'-phosphate
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one mol per subunit
pyridoxal 5'-phosphate
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mechanism, active-site structure
pyridoxal 5'-phosphate
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mechanism, active-site structure
pyridoxal 5'-phosphate
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mechanism, active-site structure
pyridoxal 5'-phosphate
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mechanism, active-site structure
pyridoxal 5'-phosphate
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important role in maintaining the structural integrity of the enzyme by preventing the dissociation of the enzyme into subunits, in addition to its function in catalysis
pyridoxal 5'-phosphate
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important role in maintaining the structural integrity of the enzyme by preventing the dissociation of the enzyme into subunits, in addition to its function in catalysis
pyridoxal 5'-phosphate
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important role in maintaining the structural integrity of the enzyme by preventing the dissociation of the enzyme into subunits, in addition to its function in catalysis
pyridoxal 5'-phosphate
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important role in maintaining the structural integrity of the enzyme by preventing the dissociation of the enzyme into subunits, in addition to its function in catalysis
pyridoxal 5'-phosphate
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important role in maintaining the structural integrity of the enzyme by preventing the dissociation of the enzyme into subunits, in addition to its function in catalysis
pyridoxal 5'-phosphate
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important role in maintaining the structural integrity of the enzyme by preventing the dissociation of the enzyme into subunits, in addition to its function in catalysis
pyridoxal 5'-phosphate
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dimeric form of some mutant enzymes contains no pyridoxal 5'-phosphate
pyridoxal 5'-phosphate
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mutant enzymes K226M and K226Q contain 1 mol of pyridoxal 5'-phosphate per mol of subunit. Pyridoxal 5'-phosphate is bound at the active site in an orientation different from that of the wild-type enzyme. K226 is responsible for flipping of pyridoxal 5'-phosphate from one orientation to another which is crucial for tetrahydropteroylglutamate-dependent Calpha-Cbeta bond cleavage of L-Ser
pyridoxal 5'-phosphate
SHM1 contains 1 mol per mol of enzyme dimer
pyridoxal 5'-phosphate
SHM2 contains 2 mol per mol of enzyme dimer
pyridoxal 5'-phosphate
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dependent on, the apo enzyme has some enzyme activity in the absence of pyridoxal 5'-phosphate but this activity is only slightly above background and can be due to incomplete removal of pyridoxal 5'-phosphate
pyridoxal 5'-phosphate
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the Kd for binding of the enzyme and pyridoxal 5'-phosphate is 0.00014 mM
pyridoxal 5'-phosphate
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wild type enzyme contains 1 mol per mole of subunit
pyridoxal 5'-phosphate
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dependent on, stabilizes the dimeric form of the enzyme
pyridoxal 5'-phosphate
dependent on, cofactor binding triggers a rearrangement of the small domain that moves toward the large domain and screens the pyridoxal 5'-phosphate binding site at the solvent side
pyridoxal 5'-phosphate
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dependent on. The binding environment of PLP in human and Plasmodium enzymes is significantly different
pyridoxal 5'-phosphate
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dependent on. The binding environment of PLP in human and Plasmodium enzymes is significantly different
pyridoxal 5'-phosphate
dependent on. The binding environment of PLP in human and Plasmodium enzymes is significantly different
tetrahydrofolate
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tetrahydrofolate
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requirement with L-serine or L-2-methylserine as substrate
tetrahydrofolate
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requirement with L-serine or L-2-methylserine as substrate
tetrahydrofolate
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requirement with L-serine or L-2-methylserine as substrate
tetrahydrofolate
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requirement with L-serine or L-2-methylserine as substrate
tetrahydrofolate
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requirement with L-serine or L-2-methylserine as substrate
tetrahydrofolate
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requirement with L-serine or L-2-methylserine as substrate
tetrahydrofolate
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requirement with L-serine or L-2-methylserine as substrate
tetrahydrofolate
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requirement with L-serine or L-2-methylserine as substrate
tetrahydrofolate
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requirement with L-serine or L-2-methylserine as substrate
tetrahydrofolate
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requirement with L-serine or L-2-methylserine as substrate
tetrahydrofolate
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allosteric regulation
tetrahydrofolate
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mechanism
tetrahydrofolate
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mechanism
tetrahydrofolate
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mechanism
tetrahydrofolate
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mechanism
tetrahydrofolate
binding structure analysis