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Ornithine cyclodeaminase: structure, mechanism of action, and implications for the mu-crystallin family.
- J. L. Goodman, Susan C Wang, S. Alam, F. Ruzicka, P. Frey, J. Wedekind
- Chemistry, BiologyBiochemistry
- 16 October 2004
The structure revealed that the substrate carboxyl group interacts with the side chains of Arg45, Lys69, and Arg112, and the ammonia leaving group hydrogen bonds to the side chain of Asp228 and the site of hydride transfer is 3.8 A from C4 of the nicotinamide.
S-adenosylmethionine as an oxidant: the radical SAM superfamily.
Crystallization and X-ray diffraction analysis of ornithine cyclodeaminase from Pseudomonas putida.
- S. Alam, Susan C Wang, F. Ruzicka, P. Frey, J. Wedekind
- ChemistryActa crystallographica. Section D, Biological…
- 1 May 2004
In order to elucidate the functional groups of this enzyme that are involved in catalysis, the crystallization of OCD from Pseudomonas putida was undertaken using microbatch-under-oil screening at the high-throughput crystallization laboratory (HTC).
Binding energy in the one-electron reductive cleavage of S-adenosylmethionine in lysine 2,3-aminomutase, a radical SAM enzyme.
The energetics of the reductive cleavage of SAM is an outstanding question in the actions of radical SAM enzymes and is here reported for the action of lysine 2,3-aminomutase (LAM), which catalyzes the interconversion of l-lysine and l-beta-lysines.
In vitro phosphinate methylation by PhpK from Kitasatospora phosalacinea.
- W. J. Werner, Kylie D. Allen, K. Hu, G. Helms, B. Chen, Susan C Wang
- Chemistry, BiologyBiochemistry
- 25 October 2011
The activity of the P-methyltransferase enzyme, PhpK, is demonstrated from the phosalacine producer Kitasatosporaphosalacinea to give rise to the only carbon-phosphorus-carbon linkage known to occur in nature.
Initial characterization of Fom3 from Streptomyces wedmorensis: The methyltransferase in fosfomycin biosynthesis.
Secretory leukocyte protease inhibitor: inhibition of human immunodeficiency virus-1 infection of monocytic THP-1 cells by a newly cloned protein.
Reactions of trans-3-chloroacrylic acid dehalogenase with acetylene substrates: Consequences of and evidence for a hydration reaction
The genes for the α- and β-subunits of CaaD have been synthesized using a polymerase chain reaction-based strategy, cloned into separate plasmids, and the proteins expressed and purified as the functional heterohexamer.
The 4-oxalocrotonate tautomerase- and YwhB-catalyzed hydration of 3E-haloacrylates: implications for the evolution of new enzymatic activities.
- Susan C Wang, W. Johnson, C. P. Whitman
- Chemistry, BiologyJournal of the American Chemical Society
- 1 November 2003
Two mechanisms are proposed in which Pro-1 functions as a general base or a general acid catalyst and, along with the arginine, facilitates the Michael addition of water, which suggest an intriguing route for the evolution of the CaaD activity.
The roles of active-site residues in the catalytic mechanism of trans-3-chloroacrylic acid dehalogenase: a kinetic, NMR, and mutational analysis.
- H. Azurmendi, Susan C Wang, M. Massiah, G. Poelarends, C. P. Whitman, A. Mildvan
- Biology, ChemistryBiochemistry
- 13 April 2004
These results provide the first evidence for an amino-terminal proline, conserved in all known tautomerase superfamily members, functioning as a general acid, rather than as ageneral base as in 4-OT.