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Literature summary extracted from

  • Daubner, S.C.; Melendez, J.; Fitzpatrick, P.F.
    Reversing the substrate specificities of phenylalanine and tyrosine hydroxylase: aspartate 425 of tyrosine hydroxylase is essential for L-DOPA formation (2000), Biochemistry, 39, 9652-9661.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.16.1 expression of truncated enzyme containing the catalytic domain and various mutants in Escherichia coli Rattus norvegicus
1.14.16.2 expression of wild-type and mutant enzymes in Escherichia coli Rattus norvegicus

Protein Variants

EC Number Protein Variants Comment Organism
1.14.16.1 A322S/V379D truncated enzyme containing the catalytic domain, mutant shows tyrosine hydroxylation activity Rattus norvegicus
1.14.16.1 H264Q mutant of full length enzyme, no tyrosine hydroxylation activity Rattus norvegicus
1.14.16.1 H264Q/V379D truncated enzyme containing the catalytic domain, mutant shows tyrosine hydroxylation activity Rattus norvegicus
1.14.16.1 H264Q/V379D double mutant of full length enzyme, shows significant tyrosine hydroxylation activity Rattus norvegicus
1.14.16.1 H264Q/Y277H/V379D truncated enzyme containing the catalytic domain, mutant shows tyrosine hydroxylation activity Rattus norvegicus
1.14.16.1 H264Q/Y277H/V379D triple mutant of full length enzyme, shows significant tyrosine hydroxylation activity Rattus norvegicus
1.14.16.1 L293M truncated enzyme containing the catalytic domain, mutant shows tyrosine hydroxylation activity Rattus norvegicus
1.14.16.1 S251A truncated enzyme containing the catalytic domain, no tyrosine hydroxylation activity Rattus norvegicus
1.14.16.1 S251A/H264Q truncated enzyme containing the catalytic domain, no tyrosine hydroxylation activity Rattus norvegicus
1.14.16.1 S251A/H264Q/V379D truncated enzyme containing the catalytic domain, mutant shows tyrosine hydroxylation activity Rattus norvegicus
1.14.16.1 S251A/H264Q/Y277H truncated enzyme containing the catalytic domain, no tyrosine hydroxylation activity Rattus norvegicus
1.14.16.1 S251A/H264Q/Y277H/A322S truncated enzyme containing the catalytic domain, no tyrosine hydroxylation activity Rattus norvegicus
1.14.16.1 S251A/H264Q/Y277H/A322S/V379D truncated enzyme containing the catalytic domain, mutant shows tyrosine hydroxylation activity Rattus norvegicus
1.14.16.1 S251A/H264Q/Y277H/A322S/V379D/Y356H truncated enzyme containing the catalytic domain, mutant shows tyrosine hydroxylation activity Rattus norvegicus
1.14.16.1 S251A/H264Q/Y277H/A322S/V379D/Y356H/L293M truncated enzyme containing the catalytic domain, mutant shows tyrosine hydroxylation activity Rattus norvegicus
1.14.16.1 S251A/H264Q/Y277H/V379D truncated enzyme containing the catalytic domain, mutant shows tyrosine hydroxylation activity Rattus norvegicus
1.14.16.1 S251A/V379D truncated enzyme containing the catalytic domain, mutant shows tyrosine hydroxylation activity Rattus norvegicus
1.14.16.1 V379D truncated enzyme containing the catalytic domain, mutant shows tyrosine hydroxylation activity Rattus norvegicus
1.14.16.1 Y277H mutant of full length enzyme, no tyrosine hydroxylation activity Rattus norvegicus
1.14.16.1 Y277H/V379D truncated enzyme containing the catalytic domain, mutant shows tyrosine hydroxylation activity Rattus norvegicus
1.14.16.2 D425V 335fold reduced tyrosine hydroxylation/dopa formation activity, 120fold reduced reaction velocity with tyrosine, 3fold enhanced phenylalanine hydroxylation activity, active site mutant Rattus norvegicus
1.14.16.2 H323Y enhanced Km for tyrosine, 4.5fold enhanced phenylalanine hydroxylation activity, active site mutant Rattus norvegicus
1.14.16.2 additional information active site mutants of phenylalanine hydroxylase lead to highly increased tyrosine hydroxylation activity of the enzyme mutants Rattus norvegicus
1.14.16.2 Q310H 4fold reduced tyrosine hydroxylation/dopa formation activity, slightly enhanced phenylalanine hydroxylation activity, active site mutant Rattus norvegicus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.14.16.2 additional information
-
 additional information Km-values for tyrosine of mutant phenylalanine hydroxylase with tyrosine hydroxylation activity Rattus norvegicus
1.14.16.2 0.00125
-
 phenylalanine recombinant mutant D425V Rattus norvegicus
1.14.16.2 0.0077
-
 phenylalanine recombinant mutant H323Y Rattus norvegicus
1.14.16.2 0.0088
-
 phenylalanine recombinant mutant Q310H Rattus norvegicus
1.14.16.2 0.016
-
 tyrosine recombinant wild-type Rattus norvegicus
1.14.16.2 0.045
-
 tyrosine recombinant mutant D425V Rattus norvegicus
1.14.16.2 0.054
-
 tyrosine recombinant mutant Q310H Rattus norvegicus
1.14.16.2 0.092
-
 tyrosine recombinant mutant H323Y Rattus norvegicus
1.14.16.2 0.1
-
 phenylalanine recombinant wild-type Rattus norvegicus

Organism

EC Number Organism UniProt Comment Textmining
1.14.16.1 Rattus norvegicus
-
-
-
1.14.16.2 Rattus norvegicus P04177
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.14.16.2 recombinant wild-type and mutants from Escherichia coli Rattus norvegicus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.16.2 L-phenylalanine + tetrahydropteridine + 2 O2 wild-type and mutants Rattus norvegicus 3,4-dihydroxy-L-phenylalanine + dihydropteridine + 2 H2O
-
 ?
1.14.16.2 L-tyrosine + tetrahydrobiopterin + O2
-
 Rattus norvegicus 3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O 3,4-dihydroxy-L-phenylalanine is identical with dopa ?

Synonyms

EC Number Synonyms Comment Organism
1.14.16.2 TH
-
 Rattus norvegicus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.14.16.1 0.633
-
 phenylalanine V379D mutant enzyme Rattus norvegicus
1.14.16.1 2.08
-
 phenylalanine H264Q/Y277H/V379D mutant enzyme Rattus norvegicus
1.14.16.1 4.68
-
 phenylalanine H264Q/V379D mutant enzyme Rattus norvegicus
1.14.16.1 10.1
-
 phenylalanine Y277H mutant enzyme Rattus norvegicus
1.14.16.1 14
-
 phenylalanine H264Q mutant enzyme Rattus norvegicus
1.14.16.1 16
-
 phenylalanine recombinant wild-type enzyme Rattus norvegicus