RT Book, Section
A1 Erlandsen, Heidi
A1 Stevens, Raymond C.
A2 Valle, David L.
A2 Antonarakis, Stylianos
A2 Ballabio, Andrea
A2 Beaudet, Arthur L.
A2 Mitchell, Grant A.
SR Print(0)
ID 1181421745
T1 Structural Studies of Phenylalanine Hydroxylase Enzyme
T2 The Online Metabolic and Molecular Bases of Inherited Disease
YR 2019
FD 2019
PB McGraw-Hill Education
PP New York, NY
SN 9780071459969
LK ommbid.mhmedical.com/content.aspx?aid=1181421745
RD 2024/04/24
AB Recombinant  human  (liver)  phenylalanine  hydroxylase  (PheOH,  phenylalanine  4-monooxygenase,  EC  1.14.16.1)  is  reported  to  exist  in  solution  as  a  pH-dependent  equilibrium  between  homotetramers  and  homodimers  (Martinez  et  al,34).  The  molecular  weight  of  one  subunit  is  approximately  50  kDa  (between  50  and  53  kDa).  It  has  an  absolute  requirement  for  ferrous  iron  to  be  active,  and  uses  the  cofactors  BH4  and  O2  to  perform  the  hydroxylation  reaction.  PheOH,  like  the  two  other  aromatic  amino  acid  hydroxylases  tyrosine  hydroxylase  (TyrOH,  tyrosine  3-monooxygenase,  EC  1.14.16.2)  and  tryptophan  hydroxylase  (TrpOH,  tryptophan  5-monooxygenase,  EC  1.14.16.4),  consists  of  three  domains:  the  regulatory  domain  (residues  1-142),  the  catalytic  domain  (residues  143-410),  and  a  short  tetramerization  domain  (residues  411-452).