Sequence of TYRB_PARDE
EC Number:2.6.1.57
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
an aromatic amino acid + 2-oxoglutarate = an aromatic oxo acid + L-glutamate
Other sequences found for EC No. 2.6.1.57
General information:
Sequence
0 MLGNLKPQAP DKILALMGEF RADPRQGKID LGVGVYKDAT GHTPIMRAVH AAEQRMLETE
60 TTKTYAGLSG EPEFQKAMGE LILGDGLKSE TTATLATVGG TGALRQALEL ARMANPDLRV
120 FVSDPTWPNH VSIMNFMGLP VQTYRYFDAE TRGVDFEGMK ADLAAAKKGD MVLLHGCCHN
180 PTGANLTLDQ WAEIASILEK TGALPLIDLA YQGFGDGLEE DAAGTRLIAS RIPEVLIAAS
240 CSKNFGIYRE RTGCLLALCA DAATRELAQG AMAFLNRQTY SFPPFHGAKI VSTVLTTPEL
300 RADWMAELEA VRSGMLRLRE QLAGELRDLS GSDRFGFVAE HRGMFSRLGA TPEQVKRIKE
360 EFGIYMVGDS RINIAGLNDN TIPILARAII EVGV
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
750618
Oue S.,Okamoto A.,Nakai Y.,Nakahira M.,Shibatani T.,Hayashi H.,Kagamiyama H.
Paracoccus denitrificans aromatic amino acid aminotransferase: a model enzyme for the study of dual substrate recognition mechanism.
J. Biochem.
121
161-171
1997
750619
Okamoto A.,Nakai Y.,Hayashi H.,Hirotsu K.,Kagamiyama H.
Crystal structures of Paracoccus denitrificans aromatic amino acid aminotransferase: a substrate recognition site constructed by rearrangement of hydrogen bond network.
J. Mol. Biol.
280
443-461
1998
750620
Okamoto A.,Ishii S.,Hirotsu K.,Kagamiyama H.
The active site of Paracoccus denitrificans aromatic amino acid aminotransferase has contrary properties: flexibility and rigidity.
Biochemistry
38
1176-1184
1999
