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3mog
From Proteopedia
m (Protected "3mog" [edit=sysop:move=sysop]) |
Revision as of 21:07, 17 April 2013
Contents |
Crystal structure of 3-hydroxybutyryl-CoA dehydrogenase from Escherichia coli K12 substr. MG1655
Function
[PAAH_ECOLI] Catalyzes the oxidation of 3-hydroxyadipyl-CoA to yield 3-oxoadipyl-CoA.[1] [2]
About this Structure
3mog is a 3 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
- ↑ Ferrandez A, Minambres B, Garcia B, Olivera ER, Luengo JM, Garcia JL, Diaz E. Catabolism of phenylacetic acid in Escherichia coli. Characterization of a new aerobic hybrid pathway. J Biol Chem. 1998 Oct 2;273(40):25974-86. PMID:9748275
- ↑ Teufel R, Mascaraque V, Ismail W, Voss M, Perera J, Eisenreich W, Haehnel W, Fuchs G. Bacterial phenylalanine and phenylacetate catabolic pathway revealed. Proc Natl Acad Sci U S A. 2010 Aug 10;107(32):14390-5. doi:, 10.1073/pnas.1005399107. Epub 2010 Jul 21. PMID:20660314 doi:10.1073/pnas.1005399107
Categories: 3-hydroxybutyryl-CoA dehydrogenase | Escherichia coli | Almo, S C. | Burley, S K. | Gilmore, M. | Miller, S. | NYSGXRC, New York SGX Research Center for Structural Genomics. | Patskovsky, Y. | Ramagopal, U. | Sauder, J M. | Toro, R. | New york sgx research center for structural genomic | New york structural genomix research consortium | Nysgrc | Nysgxrc | Oxidoreductase | Protein structure initiative | Psi | Structural genomic
