PMID- 10504734
OWN - NLM
STAT- MEDLINE
DCOM- 19991027
LR  - 20131121
IS  - 1072-8368 (Print)
IS  - 1072-8368 (Linking)
VI  - 6
IP  - 10
DP  - 1999 Oct
TI  - Substrate-mediated electron transfer in peptidylglycine alpha-hydroxylating
      monooxygenase.
PG  - 976-83
AB  - Peptide amidation is a ubiquitous posttranslational modification of bioactive
      peptides. Peptidylglycine alpha-hydroxylating monooxygenase (PHM; EC 1.14.17.3), 
      the enzyme that catalyzes the first step of this reaction, is composed of two
      domains, each of which binds one copper atom. The coppers are held 11 A apart on 
      either side of a solvent-filled interdomain cleft, and the PHM reaction requires 
      electron transfer between these sites. A plausible mechanism for electron
      transfer might involve interdomain motion to decrease the distance between the
      copper atoms. Our experiments show that PHM catalytic core (PHMcc) is
      enzymatically active in the crystal phase, where interdomain motion is not
      possible. Instead, structures of two states relevant to catalysis indicate that
      water, substrate and active site residues may provide an electron transfer
      pathway that exists only during the PHM catalytic cycle.
FAU - Prigge, S T
AU  - Prigge ST
AD  - Department of Biophysics and Biophysical Chemistry, Johns Hopkins School of
      Medicine, Baltimore, Maryland 21205, USA.
FAU - Kolhekar, A S
AU  - Kolhekar AS
FAU - Eipper, B A
AU  - Eipper BA
FAU - Mains, R E
AU  - Mains RE
FAU - Amzel, L M
AU  - Amzel LM
LA  - eng
SI  - PDB/1OPM
SI  - PDB/3PHM
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Nat Struct Biol
JT  - Nature structural biology
JID - 9421566
RN  - 0 (Ligands)
RN  - 0 (Multienzyme Complexes)
RN  - 0 (Peptide Fragments)
RN  - 0 (Solvents)
RN  - 789U1901C5 (Copper)
RN  - EC 1.- (Mixed Function Oxygenases)
RN  - EC 1.14.17.3 (peptidylglycine monooxygenase)
RN  - S88TT14065 (Oxygen)
SB  - IM
MH  - Animals
MH  - Binding Sites
MH  - Catalysis
MH  - Catalytic Domain
MH  - Copper/chemistry/metabolism
MH  - Crystallization
MH  - Crystallography, X-Ray
MH  - *Electrons
MH  - Hydrogen-Ion Concentration
MH  - Kinetics
MH  - Ligands
MH  - Mixed Function Oxygenases/*chemistry/*metabolism
MH  - Models, Chemical
MH  - Models, Molecular
MH  - Molecular Sequence Data
MH  - *Multienzyme Complexes
MH  - Oxidation-Reduction
MH  - Oxygen/metabolism
MH  - Peptide Fragments/chemistry/metabolism
MH  - Protein Conformation
MH  - Rats
MH  - Solvents
MH  - Structure-Activity Relationship
EDAT- 1999/10/03 09:00
MHDA- 2001/03/23 10:01
CRDT- 1999/10/03 09:00
PHST- 1999/10/03 09:00 [pubmed]
PHST- 2001/03/23 10:01 [medline]
PHST- 1999/10/03 09:00 [entrez]
AID - 10.1038/13351 [doi]
PST - ppublish
SO  - Nat Struct Biol. 1999 Oct;6(10):976-83. doi: 10.1038/13351.