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Literature summary for 1.14.16.1 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
Search for more literature for 1.14.16.1

Cloned(Commentary)

Cloned (Comment) Organism
expression of truncated enzyme containing the catalytic domain and various mutants in Escherichia coli Rattus norvegicus

Protein Variants

Protein Variants Comment Organism
A322S/V379D truncated enzyme containing the catalytic domain, mutant shows tyrosine hydroxylation activity Rattus norvegicus
H264Q mutant of full length enzyme, no tyrosine hydroxylation activity Rattus norvegicus
H264Q/V379D truncated enzyme containing the catalytic domain, mutant shows tyrosine hydroxylation activity Rattus norvegicus
H264Q/V379D double mutant of full length enzyme, shows significant tyrosine hydroxylation activity Rattus norvegicus
H264Q/Y277H/V379D truncated enzyme containing the catalytic domain, mutant shows tyrosine hydroxylation activity Rattus norvegicus
H264Q/Y277H/V379D triple mutant of full length enzyme, shows significant tyrosine hydroxylation activity Rattus norvegicus
L293M truncated enzyme containing the catalytic domain, mutant shows tyrosine hydroxylation activity Rattus norvegicus
S251A truncated enzyme containing the catalytic domain, no tyrosine hydroxylation activity Rattus norvegicus
S251A/H264Q truncated enzyme containing the catalytic domain, no tyrosine hydroxylation activity Rattus norvegicus
S251A/H264Q/V379D truncated enzyme containing the catalytic domain, mutant shows tyrosine hydroxylation activity Rattus norvegicus
S251A/H264Q/Y277H truncated enzyme containing the catalytic domain, no tyrosine hydroxylation activity Rattus norvegicus
S251A/H264Q/Y277H/A322S truncated enzyme containing the catalytic domain, no tyrosine hydroxylation activity Rattus norvegicus
S251A/H264Q/Y277H/A322S/V379D truncated enzyme containing the catalytic domain, mutant shows tyrosine hydroxylation activity Rattus norvegicus
S251A/H264Q/Y277H/A322S/V379D/Y356H truncated enzyme containing the catalytic domain, mutant shows tyrosine hydroxylation activity Rattus norvegicus
S251A/H264Q/Y277H/A322S/V379D/Y356H/L293M truncated enzyme containing the catalytic domain, mutant shows tyrosine hydroxylation activity Rattus norvegicus
S251A/H264Q/Y277H/V379D truncated enzyme containing the catalytic domain, mutant shows tyrosine hydroxylation activity Rattus norvegicus
S251A/V379D truncated enzyme containing the catalytic domain, mutant shows tyrosine hydroxylation activity Rattus norvegicus
V379D truncated enzyme containing the catalytic domain, mutant shows tyrosine hydroxylation activity Rattus norvegicus
Y277H mutant of full length enzyme, no tyrosine hydroxylation activity Rattus norvegicus
Y277H/V379D truncated enzyme containing the catalytic domain, mutant shows tyrosine hydroxylation activity Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Turnover Number [1/s]

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