1.3.1.12: prephenate dehydrogenase
This is an abbreviated version!
For detailed information about prephenate dehydrogenase, go to the full flat file.
Word Map on EC 1.3.1.12
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1.3.1.12
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l-tyrosine
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h-protein
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arogenate
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hyperglycinemia
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nonketotic
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4-hydroxyphenylpyruvate
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aminomethyltransferase
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dahp
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3-deoxy-d-arabino-heptulosonate
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cyclohexadienyl
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7-phosphate
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dimethylglycine
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tetrahydrofolate-dependent
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glycine-cleavage
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aminomethyl
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folate-binding
- 1.3.1.12
- l-tyrosine
- h-protein
- arogenate
- hyperglycinemia
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nonketotic
- 4-hydroxyphenylpyruvate
- aminomethyltransferase
- dahp
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3-deoxy-d-arabino-heptulosonate
-
cyclohexadienyl
- 7-phosphate
- dimethylglycine
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tetrahydrofolate-dependent
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glycine-cleavage
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aminomethyl
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folate-binding
Reaction
Synonyms
AceF, AroQ, bifunctional T-protein, chorismate mutase-prephenate dehydratase, chorismate mutase-prephenate dehydrogenase bifunctional enzyme, chorismate mutase-T:prephenate dehydrogenase bifunctional enzyme, Chorismate mutase/prephenate dehydratase, CM-PD, CM-TyrAp, CM/PDT/PDHG, CMPD, dehydrogenase, prephenate, hydroxyphenylpyruvate synthase, PD, PDH, pdhE-1, PDHG, T-protein, TYR1, tyrA, TyrA dehydrogenase, TyrAp
ECTree
1.3.1.12 prephenate dehydrogenaseAdvanced search results
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results (Engineering
Engineering on EC 1.3.1.12 - prephenate dehydrogenase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
DELTA1-19
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delta19PD, more sensitive to temperature effects yielding a half-life of 55 min at 95°C versus 2 h for PD
H147N
inactive, binds prephenate with apparent affinity similar to wild-type
H217A
40fold increase in Km for prephenate, no inhibition by tyrosine
H217N
30fold increase in Km for prephenate, no inhibition by tyrosine
R250Q
10fold increase in the Km for prephenate and a 20fold increase in Ki for tyrosine
S126A
15fold reduction in kcat, a 10fold increase in the Km value for prephenate, and a 2-fold increase in Ki for tyrosine
H131A
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chorismate mutase-prephenate dehydrogenase bifunctional enzyme, mutant enzyme retains 10% of dehydrogenase activity and 30% mutase activity compared to the wild-type enzyme, His131 is not an essential residue whose protonation state is critical for catalysis or substrate binding
H189N
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chorismate mutase-prephenate dehydrogenase bifunctional enzyme, mutant enzyme shows less than 0.01% the activity of wild-type mutase and dehydrogenase
H197N
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chorismate mutase-prephenate dehydrogenase bifunctional enzyme, mutant enzyme exhibits no significant dehydrogenase activity, retains nearly wild-type mutase activity and unaltered Michaelis constants for chorismate, prephenate and NAD+
K37A
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chorismate mutase-prephenate dehydrogenase bifunctional enzyme, mutant protein poorly expressed, no detectable mutase or dehydrogenase activity, structural changes may result in its inactivity and instability
K37Q
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chorismate mutase-prephenate dehydrogenase bifunctional enzyme, mutant enzyme exhibits no mutase activity while retaining wild-type dehydrogenase activity
R294Q
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chorismate mutase-prephenate dehydrogenase bifunctional enzyme, R294Q substitution reduces the affinity of the enzyme for prephenate, Arg294 interacts electrostatically with the ring carboxylate at C1 of prephenate
N234D
additional information
N234D
the prephenate dehydrogenase activity of the mutant enzyme is 5fold increased compared to the wild type enzyme. L-tyrosine sensitivity is not altered compared to the wild type enzyme. The mutant does not have arognate dehydrogenase activity
N234D
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the prephenate dehydrogenase activity of the mutant enzyme is slightly reduced compared to the wild type enzyme. L-tyrosine sensitivity is not altered compared to the wild type enzyme. The mutant does not have arognate dehydrogenase activity
additional information
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delta19-PDH, delta25-PDH, and delta28-PDH, which produce stable and soluble proteins, delta36-PDH, delta52-PDH, and delta55-PDH are unstable
additional information
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feedback-inhibition-resistant mutants toward L-tyrosine, chorismate mutase activities similar to those of the wild-type, amino acid substitutions either at Tyr263 or at residues 354 to 357
additional information
mutation of a prominent surface loop that links the first and second beta-strands in all lipoyl domains, of E2p dihydrolipoyl acetyltransferase. Deletion of the loop (four residues) renders the domain incapable of reductive acetylation by pyruvate dehydrogenase complex subunit E1p in the presence of pyruvate. Additional exchange of the two residues on the C-terminal side of the loop (V14A, E15T) has no effect. Exchanging the residue on the N-terminal side of the lipoyl-lysine beta-turn in the E2p and E2o domains (G39T), both singly and in conjunction with the loop exchange, has no effect on the ability of the E2p domain to be reductively acetylated but does confer a slight increase in susceptibility to reductive succinylation. All mutant E2p domains, apart from that with the loop deletion, are readily lipoylated in vitro by lipoate protein ligase A
additional information
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feedback-inhibition-resistant mutants toward L-tyrosine, chorismate mutase activities similar to those of the wild-type, amino acid substitutions either at Tyr263 or at residues 354 to 357
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