187 related articles for article (PubMed ID: 22961985)
1. Protein-protein interactions in the β-oxidation part of the phenylacetate utilization pathway: crystal structure of the PaaF-PaaG hydratase-isomerase complex.
Grishin AM; Ajamian E; Zhang L; Rouiller I; Bostina M; Cygler M
J Biol Chem; 2012 Nov; 287(45):37986-96. PubMed ID: 22961985
[TBL] [Abstract][Full Text] [Related]
2. Functional genomics by NMR spectroscopy. Phenylacetate catabolism in Escherichia coli.
Ismail W; El-Said Mohamed M; Wanner BL; Datsenko KA; Eisenreich W; Rohdich F; Bacher A; Fuchs G
Eur J Biochem; 2003 Jul; 270(14):3047-54. PubMed ID: 12846838
[TBL] [Abstract][Full Text] [Related]
3. The isomerase and hydratase reaction mechanism of the crotonase active site of the multifunctional enzyme (type-1), as deduced from structures of complexes with 3S-hydroxy-acyl-CoA.
Kasaragod P; Schmitz W; Hiltunen JK; Wierenga RK
FEBS J; 2013 Jul; 280(13):3160-75. PubMed ID: 23351063
[TBL] [Abstract][Full Text] [Related]
4. 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; 170(6):2543-8. PubMed ID: 3286611
[TBL] [Abstract][Full Text] [Related]
5. 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; 258(16):9780-5. PubMed ID: 6350283
[TBL] [Abstract][Full Text] [Related]
6. Enoyl-CoA hydratase and isomerase form a superfamily with a common active-site glutamate residue.
Müller-Newen G; Janssen U; Stoffel W
Eur J Biochem; 1995 Feb; 228(1):68-73. PubMed ID: 7883013
[TBL] [Abstract][Full Text] [Related]
7. Crystal structure of phenylacetic acid degradation protein PaaG from Thermus thermophilus HB8.
Kichise T; Hisano T; Takeda K; Miki K
Proteins; 2009 Sep; 76(4):779-86. PubMed ID: 19452559
[TBL] [Abstract][Full Text] [Related]
8. 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; 30(27):6788-95. PubMed ID: 1712230
[TBL] [Abstract][Full Text] [Related]
9. Site-directed mutagenesis of putative active-site amino acid residues of 3,2-trans-enoyl-CoA isomerase, conserved within the low-homology isomerase/hydratase enzyme family.
Müller-Newen G; Stoffel W
Biochemistry; 1993 Oct; 32(42):11405-12. PubMed ID: 8218206
[TBL] [Abstract][Full Text] [Related]
10. 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; 268(9):6588-92. PubMed ID: 8454629
[TBL] [Abstract][Full Text] [Related]
11. 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; 34(19):6441-7. PubMed ID: 7756275
[TBL] [Abstract][Full Text] [Related]
12. Structural basis for channelling mechanism of a fatty acid beta-oxidation multienzyme complex.
Ishikawa M; Tsuchiya D; Oyama T; Tsunaka Y; Morikawa K
EMBO J; 2004 Jul; 23(14):2745-54. PubMed ID: 15229654
[TBL] [Abstract][Full Text] [Related]
13. 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; 35(29):9625-30. PubMed ID: 8755745
[TBL] [Abstract][Full Text] [Related]
14. Peroxisomes and beta-oxidation of long-chain unsaturated carboxylic acids.
Hiltunen JK
Scand J Clin Lab Invest Suppl; 1991; 204():33-46. PubMed ID: 2042025
[TBL] [Abstract][Full Text] [Related]
15. Structure of mycobacterial β-oxidation trifunctional enzyme reveals its altered assembly and putative substrate channeling pathway.
Venkatesan R; Wierenga RK
ACS Chem Biol; 2013 May; 8(5):1063-73. PubMed ID: 23496842
[TBL] [Abstract][Full Text] [Related]
16. Domains of the tetrafunctional protein acting in glyoxysomal fatty acid beta-oxidation. Demonstration of epimerase and isomerase activities on a peptide lacking hydratase activity.
Preisig-Müller R; Gühnemann-Schäfer K; Kindl H
J Biol Chem; 1994 Aug; 269(32):20475-81. PubMed ID: 8051146
[TBL] [Abstract][Full Text] [Related]
17. Crystallization and X-ray diffraction analysis of peroxisomal Delta3-Delta2-enoyl-CoA isomerase from Saccharomyces cerevisiae.
Mursula AM; van Aalten DM; Modis Y; Hiltunen JK; Wierenga RK
Acta Crystallogr D Biol Crystallogr; 2000 Aug; 56(Pt 8):1020-3. PubMed ID: 10944342
[TBL] [Abstract][Full Text] [Related]
18. Domain swapping in the low-similarity isomerase/hydratase superfamily: the crystal structure of rat mitochondrial Delta3, Delta2-enoyl-CoA isomerase.
Hubbard PA; Yu W; Schulz H; Kim JJ
Protein Sci; 2005 Jun; 14(6):1545-55. PubMed ID: 15883186
[TBL] [Abstract][Full Text] [Related]
19. Human Δ³,Δ²-enoyl-CoA isomerase, type 2: a structural enzymology study on the catalytic role of its ACBP domain and helix-10.
Onwukwe GU; Kursula P; Koski MK; Schmitz W; Wierenga RK
FEBS J; 2015 Feb; 282(4):746-68. PubMed ID: 25515061
[TBL] [Abstract][Full Text] [Related]
20. Structural and sequence comparisons of bacterial enoyl-CoA isomerase and enoyl-CoA hydratase.
Hwang J; Jeong CS; Lee CW; Shin SC; Kim HW; Lee SG; Youn UJ; Lee CS; Oh TJ; Kim HJ; Park H; Park HH; Lee JH
J Microbiol; 2020 Jul; 58(7):606-613. PubMed ID: 32323197
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
