PMID- 29458006
OWN - NLM
STAT- MEDLINE
DCOM- 20190422
LR  - 20190422
IS  - 1096-0384 (Electronic)
IS  - 0003-9861 (Linking)
VI  - 643
DP  - 2018 Apr 2
TI  - Mechanistic studies of formate oxidase from Aspergillus oryzae: A novel member of 
      the glucose-Methanol-choline oxidoreductase enzyme superfamily that oxidizes 
      carbon acids.
PG  - 24-31
LID - S0003-9861(17)30803-2 [pii]
LID - 10.1016/j.abb.2018.02.007 [doi]
AB  - Formate oxidase (FOX) from Aspergillus oryzae is the only GMC member that 
      oxidizes a carbon acid rather than alcohols; thus, its catalytic mechanism may be 
      different from that of other GMC members. We have used pH, solvent viscosity, and 
      deuterium kinetic isotope effects, to investigate the catalytic mechanism of FOX. 
      The enzyme followed a Bi-Bi sequential steady-state kinetic mechanism. The k(cat) 
      value was pH-independent between pH 2.8 and 6.8, suggesting a lack of ionizable 
      groups in kinetic step(s) that limit the overall turnover of the enzyme. The 
      k(cat)/K(formate) value decreased from a value of 10,000 M(-1)s(-1) at low pH 
      with a pK(a) value of 4.4, consistent with the requirement of a protonated group 
      for substrate binding. An inverse viscosity dependence on the k(cat)/K(formate) 
      value indicated an isomerization of the Michaelis complex. The k(cat)/K(oxygen) 
      value was 340,000 M(-1)s(-1) and pH independent up to pH 6.0. The (D)k(cat) and 
      (D)(k(cat)/K(formate)) values were 2.5 and 1.9, respectively, indicating that 
      substrate CH bond cleavage is rate-limiting for FOX catalysis. Analytical 
      ultracentrifugation indicated a concentration dependence of the oligomeric state 
      of FOX. The (app)k(red,H) value was  approximately 75% that of k(cat,H), indicating that the 
      anaerobic reduction of FOX was dependent on the oligomeric state of FOX.
CI  - Copyright (c) 2018 Elsevier Inc. All rights reserved.
FAU - Robbins, John M
AU  - Robbins JM
AD  - School of Chemical and Biomolecular Engineering, Georgia Institute of Technology, 
      Atlanta, GA, 30332-0100, United States; Krone Engineered Biosystems Building, 
      Georgia Institute of Technology, Atlanta, GA, 30332-2000, United States.
FAU - Bommarius, Andreas S
AU  - Bommarius AS
AD  - School of Chemical and Biomolecular Engineering, Georgia Institute of Technology, 
      Atlanta, GA, 30332-0100, United States; Krone Engineered Biosystems Building, 
      Georgia Institute of Technology, Atlanta, GA, 30332-2000, United States; School 
      of Chemistry and Biochemistry, Georgia Institute of Technology, Atlanta, GA, 
      30332-0100, United States. Electronic address: andreas.bommarius@chbe.gatech.edu.
FAU - Gadda, Giovanni
AU  - Gadda G
AD  - Department of Chemistry, Georgia State University, Atlanta, GA, 30302-3965, 
      United States; Department of Biology, Georgia State University, Atlanta, GA, 
      30302-4010, United States; Center for Biotechnology and Drug Design, Georgia 
      State University, Atlanta, GA, 30302-3965, United States; Center for Diagnostics 
      and Therapeutics, Georgia State University, Atlanta, GA, 30302-3965, United 
      States. Electronic address: ggadda@gsu.edu.
LA  - eng
PT  - Journal Article
PT  - Research Support, U.S. Gov't, Non-P.H.S.
DEP - 20180216
PL  - United States
TA  - Arch Biochem Biophys
JT  - Archives of biochemistry and biophysics
JID - 0372430
RN  - 0 (Formates)
RN  - 0 (Solvents)
RN  - 0YIW783RG1 (formic acid)
RN  - EC 1.- (Oxidoreductases)
RN  - IY9XDZ35W2 (Glucose)
RN  - N91BDP6H0X (Choline)
RN  - Y4S76JWI15 (Methanol)
SB  - IM
MH  - Aspergillus oryzae/*enzymology
MH  - Choline/*metabolism
MH  - Formates/*metabolism
MH  - Glucose/metabolism
MH  - Kinetics
MH  - Methanol/*metabolism
MH  - Oxidation-Reduction
MH  - Oxidoreductases/chemistry/*metabolism
MH  - Solvents/chemistry
MH  - Viscosity
OTO - NOTNLM
OT  - 8-formyl FAD
OT  - Analytical ultracentrifugation
OT  - Formate oxidation
OT  - Isotope effects
OT  - Viscosity effects
OT  - pH effects
EDAT- 2018/02/20 06:00
MHDA- 2019/04/23 06:00
CRDT- 2018/02/20 06:00
PHST- 2017/11/25 00:00 [received]
PHST- 2018/01/18 00:00 [revised]
PHST- 2018/02/13 00:00 [accepted]
PHST- 2018/02/20 06:00 [pubmed]
PHST- 2019/04/23 06:00 [medline]
PHST- 2018/02/20 06:00 [entrez]
AID - S0003-9861(17)30803-2 [pii]
AID - 10.1016/j.abb.2018.02.007 [doi]
PST - ppublish
SO  - Arch Biochem Biophys. 2018 Apr 2;643:24-31. doi: 10.1016/j.abb.2018.02.007. Epub 
      2018 Feb 16.