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Journal Abstract Search


183 related items for PubMed ID: 6350283

  • 1. The large subunit of the fatty acid oxidation complex from Escherichia coli is a multifunctional polypeptide. Evidence for the existence of a fatty acid oxidation operon (fad AB) in Escherichia coli.
    Yang SY, Schulz H.
    J Biol Chem; 1983 Aug 25; 258(16):9780-5. PubMed ID: 6350283
    [Abstract] [Full Text] [Related]

  • 2. Evidence that the fadB gene of the fadAB operon of Escherichia coli encodes 3-hydroxyacyl-coenzyme A (CoA) epimerase, delta 3-cis-delta 2-trans-enoyl-CoA isomerase, and enoyl-CoA hydratase in addition to 3-hydroxyacyl-CoA dehydrogenase.
    Yang SY, Li JM, He XY, Cosloy SD, Schulz H.
    J Bacteriol; 1988 Jun 25; 170(6):2543-8. PubMed ID: 3286611
    [Abstract] [Full Text] [Related]

  • 3. Glutamate 139 of the large alpha-subunit is the catalytic base in the dehydration of both D- and L-3-hydroxyacyl-coenzyme A but not in the isomerization of delta 3, delta 2-enoyl-coenzyme A catalyzed by the multienzyme complex of fatty acid oxidation from Escherichia coli.
    Yang SY, He XY, Schulz H.
    Biochemistry; 1995 May 16; 34(19):6441-7. PubMed ID: 7756275
    [Abstract] [Full Text] [Related]

  • 4. Molecular cloning of the cDNAs for the subunits of rat mitochondrial fatty acid beta-oxidation multienzyme complex. Structural and functional relationships to other mitochondrial and peroxisomal beta-oxidation enzymes.
    Kamijo T, Aoyama T, Miyazaki J, Hashimoto T.
    J Biol Chem; 1993 Dec 15; 268(35):26452-60. PubMed ID: 8253773
    [Abstract] [Full Text] [Related]

  • 5. Histidine-450 is the catalytic residue of L-3-hydroxyacyl coenzyme A dehydrogenase associated with the large alpha-subunit of the multienzyme complex of fatty acid oxidation from Escherichia coli.
    He XY, Yang SY.
    Biochemistry; 1996 Jul 23; 35(29):9625-30. PubMed ID: 8755745
    [Abstract] [Full Text] [Related]

  • 6. Nucleotide sequence of the promoter and fadB gene of the fadBA operon and primary structure of the multifunctional fatty acid oxidation protein from Escherichia coli.
    Yang XY, Schulz H, Elzinga M, Yang SY.
    Biochemistry; 1991 Jul 09; 30(27):6788-95. PubMed ID: 1712230
    [Abstract] [Full Text] [Related]

  • 7. Association of both enoyl coenzyme A hydratase and 3-hydroxyacyl coenzyme A epimerase with an active site in the amino-terminal domain of the multifunctional fatty acid oxidation protein from Escherichia coli.
    Yang SY, Elzinga M.
    J Biol Chem; 1993 Mar 25; 268(9):6588-92. PubMed ID: 8454629
    [Abstract] [Full Text] [Related]

  • 8. The structure of the multienzyme complex of fatty acid oxidation from Escherichia coli.
    Pawar S, Schulz H.
    J Biol Chem; 1981 Apr 25; 256(8):3894-9. PubMed ID: 7012144
    [No Abstract] [Full Text] [Related]

  • 9. Fatty acid oxidation complex from Escherichia coli.
    Binstock JF, Schulz H.
    Methods Enzymol; 1981 Apr 25; 71 Pt C():403-11. PubMed ID: 7024730
    [No Abstract] [Full Text] [Related]

  • 10. Multienzyme complexes of fatty acid oxidation from Escherichia coli K12 and from a mutant with a defective L-3-hydroxyacyl coenzyme A dehydrogenase.
    Pramanik A, Schulz H.
    Biochim Biophys Acta; 1983 Jan 07; 750(1):41-6. PubMed ID: 6402028
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  • 12. Five different enzymatic activities are associated with the multienzyme complex of fatty acid oxidation from Escherichia coli.
    Pramanik A, Pawar S, Antonian E, Schulz H.
    J Bacteriol; 1979 Jan 07; 137(1):469-73. PubMed ID: 368024
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  • 15. Amino acid sequence similarities of the mitochondrial short chain delta 3, delta 2-enoyl-CoA isomerase and peroxisomal multifunctional delta 3, delta 2-enoyl-CoA isomerase, 2-enoyl-CoA hydratase, 3-hydroxyacyl-CoA dehydrogenase enzyme in rat liver. The proposed occurrence of isomerization and hydration in the same catalytic domain of the multifunctional enzyme.
    Palosaari PM, Vihinen M, Mäntsälä PI, Alexson SE, Pihlajaniemi T, Hiltunen JK.
    J Biol Chem; 1991 Jun 15; 266(17):10750-3. PubMed ID: 2040594
    [Abstract] [Full Text] [Related]

  • 16. Glutamate-119 of the large alpha-subunit is the catalytic base in the hydration of 2-trans-enoyl-coenzyme A catalyzed by the multienzyme complex of fatty acid oxidation from Escherichia coli.
    He XY, Yang SY.
    Biochemistry; 1997 Sep 09; 36(36):11044-9. PubMed ID: 9283097
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  • 18. Importance of the gamma-carboxyl group of glutamate-462 of the large alpha-subunit for the catalytic function and the stability of the multienzyme complex of fatty acid oxidation from Escherichia coli.
    He XY, Deng H, Yang SY.
    Biochemistry; 1997 Jan 07; 36(1):261-8. PubMed ID: 8993342
    [Abstract] [Full Text] [Related]

  • 19. Purification of the multienzyme complex for fatty acid oxidation from Pseudomonas fragi and reconstitution of the fatty acid oxidation system.
    Imamura S, Ueda S, Mizugaki M, Kawaguchi A.
    J Biochem; 1990 Feb 07; 107(2):184-9. PubMed ID: 2361950
    [Abstract] [Full Text] [Related]

  • 20. Evidence for a complex of three beta-oxidation enzymes in Escherichia coli: induction and localization.
    O'Brien WJ, Frerman FE.
    J Bacteriol; 1977 Nov 07; 132(2):532-40. PubMed ID: 334745
    [Abstract] [Full Text] [Related]


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