Tags

Type your tag names separated by a space and hit enter

Flavin-containing monooxygenase (FMO)-dependent metabolism of methionine and evidence for FMO3 being the major FMO involved in methionine sulfoxidation in rabbit liver and kidney microsomes.
J Biol Chem. 1994 Jul 01; 269(26):17525-30.JB

Abstract

Methionine was a substrate for cDNA-expressed rabbit flavin-containing monooxygenase (FMO) 1, FMO2, and FMO3, while incubations with membrane fractions containing cDNA-expressed FMO5 did not lead to the detection of methionine sulfoxide; Km values with FMO1, FMO2, and FMO3 were about 48.0, 30.0, and 6.5 mM, respectively. With FMO3 methionine d-sulfoxide was formed in nearly 8-fold higher concentrations than the l-diastereomer, whereas with FMO1 and FMO2, the d:l diastereomeric ratios were approximately 1.5:1 and 0.7:1, respectively. These results provide evidence for methionine being the first identified endogenous compound metabolized to diastereomeric sulfoxides by flavin-containing monooxygenases. The Km values for methionine sulfoxidation in rabbit liver and kidney microsomes (3.7 and 6.0 mM, respectively) were more comparable to the Km value obtained with FMO3 than FMO1 or FMO2. This result provides evidence that FMO3 is the major FMO isoform involved in methionine sulfoxidation in rabbit liver and kidney microsomes. Further evidence for this hypothesis is provided by the finding that methionine d-sulfoxide was also the preferred product in rabbit liver and kidney microsomes by nearly 8:1 and 6:1 over the l-diastereomer, respectively.

Authors+Show Affiliations

Department of Comparative Biosciences, University of Wisconsin, Madison 53706.No affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, U.S. Gov't, P.H.S.

Language

eng

PubMed ID

8021260

Citation

Duescher, R J., et al. "Flavin-containing Monooxygenase (FMO)-dependent Metabolism of Methionine and Evidence for FMO3 Being the Major FMO Involved in Methionine Sulfoxidation in Rabbit Liver and Kidney Microsomes." The Journal of Biological Chemistry, vol. 269, no. 26, 1994, pp. 17525-30.
Duescher RJ, Lawton MP, Philpot RM, et al. Flavin-containing monooxygenase (FMO)-dependent metabolism of methionine and evidence for FMO3 being the major FMO involved in methionine sulfoxidation in rabbit liver and kidney microsomes. J Biol Chem. 1994;269(26):17525-30.
Duescher, R. J., Lawton, M. P., Philpot, R. M., & Elfarra, A. A. (1994). Flavin-containing monooxygenase (FMO)-dependent metabolism of methionine and evidence for FMO3 being the major FMO involved in methionine sulfoxidation in rabbit liver and kidney microsomes. The Journal of Biological Chemistry, 269(26), 17525-30.
Duescher RJ, et al. Flavin-containing Monooxygenase (FMO)-dependent Metabolism of Methionine and Evidence for FMO3 Being the Major FMO Involved in Methionine Sulfoxidation in Rabbit Liver and Kidney Microsomes. J Biol Chem. 1994 Jul 1;269(26):17525-30. PubMed PMID: 8021260.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Flavin-containing monooxygenase (FMO)-dependent metabolism of methionine and evidence for FMO3 being the major FMO involved in methionine sulfoxidation in rabbit liver and kidney microsomes. AU - Duescher,R J, AU - Lawton,M P, AU - Philpot,R M, AU - Elfarra,A A, PY - 1994/7/1/pubmed PY - 1994/7/1/medline PY - 1994/7/1/entrez SP - 17525 EP - 30 JF - The Journal of biological chemistry JO - J Biol Chem VL - 269 IS - 26 N2 - Methionine was a substrate for cDNA-expressed rabbit flavin-containing monooxygenase (FMO) 1, FMO2, and FMO3, while incubations with membrane fractions containing cDNA-expressed FMO5 did not lead to the detection of methionine sulfoxide; Km values with FMO1, FMO2, and FMO3 were about 48.0, 30.0, and 6.5 mM, respectively. With FMO3 methionine d-sulfoxide was formed in nearly 8-fold higher concentrations than the l-diastereomer, whereas with FMO1 and FMO2, the d:l diastereomeric ratios were approximately 1.5:1 and 0.7:1, respectively. These results provide evidence for methionine being the first identified endogenous compound metabolized to diastereomeric sulfoxides by flavin-containing monooxygenases. The Km values for methionine sulfoxidation in rabbit liver and kidney microsomes (3.7 and 6.0 mM, respectively) were more comparable to the Km value obtained with FMO3 than FMO1 or FMO2. This result provides evidence that FMO3 is the major FMO isoform involved in methionine sulfoxidation in rabbit liver and kidney microsomes. Further evidence for this hypothesis is provided by the finding that methionine d-sulfoxide was also the preferred product in rabbit liver and kidney microsomes by nearly 8:1 and 6:1 over the l-diastereomer, respectively. SN - 0021-9258 UR - https://www.unboundmedicine.com/medline/citation/8021260/Flavin_containing_monooxygenase__FMO__dependent_metabolism_of_methionine_and_evidence_for_FMO3_being_the_major_FMO_involved_in_methionine_sulfoxidation_in_rabbit_liver_and_kidney_microsomes_ DB - PRIME DP - Unbound Medicine ER -