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3,4-dimethoxycinnamic acid
3-deoxy-D-arabino-heptulosonate-7-phosphate synthase
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arabinose
expression can be induced by arabinose under the control of the araBAD promoter
3,4-dimethoxycinnamic acid
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activates enzyme form CM3
3,4-dimethoxycinnamic acid
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enzyme form CM1 is unaffected
3,4-dimethoxycinnamic acid
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enzyme form CM1 is unaffected
3,4-dimethoxycinnamic acid
Penicillium duponti
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enzyme form CM2 is unaffected
3,4-dimethoxycinnamic acid
Penicillium duponti
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activates enzyme form CM3
3,4-dimethoxycinnamic acid
Penicillium duponti
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enzyme form CM1 is unaffected
3-deoxy-D-arabino-heptulosonate-7-phosphate synthase
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3-deoxy-D-arabino-heptulosonate-7-phosphate synthase
the catalytic efficiency of chorismate mutase increases 140fold on addition of 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase, chorismate mutase forms a complex with 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase and that complex formation both increases the CM activity by more than two orders of magnitude and endows chorismate mutase with regulatory features
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caffeic acid
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enzyme form CM3 is activated
caffeic acid
Penicillium duponti
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enzyme form CM3 is activated
cysteine
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histidine
is a positive effector for the enzyme
histidine
is a positive effector for the enzyme
L-Trp
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plastidic isoenzyme is activated, cytosolic isoenzyme is inactive
L-Trp
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activates enzyme forms CM1 and CM3
L-Trp
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enzyme form CM1 is activated
L-Trp
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enzyme form CM1 is activated
L-Trp
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enzyme form CM3 is activated
L-Trp
Penicillium duponti
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enzyme form CM1 is activated
L-Trp
Penicillium duponti
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enzyme form CM3 is activated
L-Trp
Penicillium duponti
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enzyme form CM2 is unaffected
L-Trp
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enzyme form CM1 is activated
L-Trp
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enzyme form CM2 is unaffected
L-Trp
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wild-type enzyme, mutant enzyme Ile225Thr/Thr226Ile and enzymes with mutations at Tyr234 are activated. No activation of mutant enzyme Thr226Ile
L-Trp
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enzyme form CM2 is unaffected
tryptophan
is a positive effector for the enzyme
tryptophan
activates about 3fold
tryptophan
Q9Y7B2
0.005 mM, heterotrophic activator
tryptophan
heterotrophic positive effector
tryptophan
is a positive effector for the enzyme
tryptophan
is a positive effector for the enzyme, identification of the allosteric effector site and the structural differences between the R- (more active) and T-state (less active) forms of plant chorismate mutase
tryptophan
heterotrophic positive effector
tryptophan
is a positive effector for the enzyme
additional information
although AtCM2 contains the putative regulatory effector binding domain, phenylalanine, tyrosine, and tryptophan do not affect its activity
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additional information
although AtCM2 contains the putative regulatory effector binding domain, phenylalanine, tyrosine, and tryptophan do not affect its activity
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additional information
although AtCM2 contains the putative regulatory effector binding domain, phenylalanine, tyrosine, and tryptophan do not affect its activity
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additional information
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although AtCM2 contains the putative regulatory effector binding domain, phenylalanine, tyrosine, and tryptophan do not affect its activity
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additional information
isozyme AtCM3 is unaltered by either phenylalanine or tyrosine but is activated by tryptophan, histidine, and cysteine
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additional information
isozyme AtCM3 is unaltered by either phenylalanine or tyrosine but is activated by tryptophan, histidine, and cysteine
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additional information
isozyme AtCM3 is unaltered by either phenylalanine or tyrosine but is activated by tryptophan, histidine, and cysteine
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additional information
Most essential residue in BsCM is Arg90, the lack of Arg90 leads to a charge loss of catalytic activity. Two important catalytic roles of Arg90: one is to control the relative stability of the substrate through the collective hydrogen-bonding network in the Glu78-Arg90-substrate, and the other is to polarize the substrate at the appropriate location on the reaction path to gain the maximum electrostatic stabilisation factor for TSS
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additional information
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Most essential residue in BsCM is Arg90, the lack of Arg90 leads to a charge loss of catalytic activity. Two important catalytic roles of Arg90: one is to control the relative stability of the substrate through the collective hydrogen-bonding network in the Glu78-Arg90-substrate, and the other is to polarize the substrate at the appropriate location on the reaction path to gain the maximum electrostatic stabilisation factor for TSS
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additional information
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the CM0819 activity is not affected by L-Phe, L-Tyr or L-Trp (0.01-10 mM), EDTA at concentrations of 0.1-2 mM does not affect CM0819 activity
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additional information
neither pH variation between 5.9 and 8.7, nor provision of 0.1 mg/ml bovine serum albumin, 2 mM Ca2+, 10 mM Mg2+, 1 mM EDTA, 1 mM EGTA, 1 mM 1,10-phenanthroline, 1 mM L-phenylalanine, 1 mM L-tyrosine, 1 mM L-tryptophan, or 0.6 mM salicylate affect catalytic activity by more than a factor of 2
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additional information
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neither pH variation between 5.9 and 8.7, nor provision of 0.1 mg/ml bovine serum albumin, 2 mM Ca2+, 10 mM Mg2+, 1 mM EDTA, 1 mM EGTA, 1 mM 1,10-phenanthroline, 1 mM L-phenylalanine, 1 mM L-tyrosine, 1 mM L-tryptophan, or 0.6 mM salicylate affect catalytic activity by more than a factor of 2
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additional information
CM1 is allosterically regulated by L-tryptophan but not L-phenylalanine or L-tyrosine
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additional information
CM1 is allosterically regulated by L-tryptophan but not L-phenylalanine or L-tyrosine
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additional information
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CM1 is allosterically regulated by L-tryptophan but not L-phenylalanine or L-tyrosine
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additional information
CM2 is not allosterically regulated by L-tryptophan, L-phenylalanine, or L-tyrosine
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additional information
CM2 is not allosterically regulated by L-tryptophan, L-phenylalanine, or L-tyrosine
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additional information
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CM2 is not allosterically regulated by L-tryptophan, L-phenylalanine, or L-tyrosine
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additional information
neither tyrosine nor phenylalanine alters the activity of enzyme SmCM
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