Sequence of TPL_CITFR
EC Number:4.1.99.2
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
L-tyrosine + H2O = phenol + pyruvate + NH3
Other sequences found for EC No. 4.1.99.2
General information:
Sequence
0 MNYPAEPFRI KSVETVSMIP RDERLKKMQE AGYNTFLLNS KDIYIDLLTD SGTNAMSDKQ
60 WAGMMMGDEA YAGSENFYHL ERTVQELFGF KHIVPTHQGR GAENLLSQLA IKPGQYVAGN
120 MYFTTTRYHQ EKNGAVFVDI VRDEAHDAGL NIAFKGDIDL KKLQKLIDEK GAENIAYICL
180 AVTVNLAGGQ PVSMANMRAV RELTEAHGIK VFYDATRCVE NAYFIKEQEQ GFENKSIAEI
240 VHEMFSYADG CTMSGKKDCL VNIGGFLCMN DDEMFSSAKE LVVVYEGMPS YGGLAGRDME
300 AMAIGLREAM QYEYIEHRVK QVRYLGDKLK AAGVPIVEPV GGHAVFLDAR RFCEHLTQDE
360 FPAQSLAASI YVETGVRSME RGIISAGRNN VTGEHHRPKL ETVRLTIPRR VYTYAHMDVV
420 ADGIIKLYQH KEDIRGLKFI YEPKQLRFFT ARFDYI
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Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
110873
Antson A.A.,Demidkina T.V.,Gollnick P.,Dauter Z.,Vontersch R.,Long J.,Berezhnoy S.N.,Phillips R.S.,Harutyunyan D.,Wilson K.S.
Three-dimensional structure of tyrosine phenol-lyase.
Biochemistry
32
4195-4206
1993
110874
Antson A.A.,Strokopytov B.V.,Murshudov G.N.,Isupov M.N.,Harutyunyan E.H.,Demidkina T.V.,Vassylyev D.G.,Dauter Z.,Terry H.,Wilson K.S.
The polypeptide chain fold in tyrosine phenol-lyase, a pyridoxal-5'-phosphate-dependent enzyme.
FEBS Lett.
302
256-260
1992
110875
Sundararaju B.,Antson A.A.,Phillips R.S.,Demidkina T.V.,Barbolina M.V.,Gollnick P.,Dodson G.G.,Wilson K.S.
The crystal structure of Citrobacter freundii tyrosine phenol-lyase complexed with 3-(4'-hydroxyphenyl)propionic acid, together with site-directed mutagenesis and kinetic analysis, demonstrates that arginine 381 is required for substrate specificity.
Biochemistry
36
6502-6510
1997