NMR Studies of Enzymes/Metal Substrate Interactions

Mildvan, Albert S.

Abstract

Funding Agency

• Agency: National Institute of Health (NIH)
• Institute: National Institute of Diabetes and Digestive and Kidney Diseases (NIDDK)
• Type: Method to Extend Research in Time (MERIT) Award (R37)
• Project #: 5R37DK028616-16
• Application #: 2138212
• Study Section: Special Emphasis Panel (NSS)
• Project Start: 1981-04-01
• Project End: 1997-03-31
• Budget Start: 1996-04-01
• Budget End: 1997-03-31
• Support Year: 16
• Fiscal Year: 1996

Institution

• Name: Johns Hopkins University
• Department: Biochemistry
• Type: Schools of Medicine
• DUNS #: 045911138
• City: Baltimore
• State: MD
• Country: United States
• Zip Code: 21218

Publications

Gabelli, Sandra B; Azurmendi, Hugo F; Bianchet, Mario A et al. (2006) X-ray, NMR, and mutational studies of the catalytic cycle of the GDP-mannose mannosyl hydrolase reaction. Biochemistry 45:11290-303

Xia, Zuyong; Azurmendi, Hugo F; Lairson, Luke L et al. (2005) Mutational, structural, and kinetic evidence for a dissociative mechanism in the GDP-mannose mannosyl hydrolase reaction. Biochemistry 44:8989-97

Xia, Zuyong; Azurmendi, Hugo F; Mildvan, Albert S (2005) Transient state kinetic studies of the MutT-catalyzed nucleoside triphosphate pyrophosphohydrolase reaction. Biochemistry 44:15334-44

Mildvan, A S; Xia, Z; Azurmendi, H F et al. (2005) Structures and mechanisms of Nudix hydrolases. Arch Biochem Biophys 433:129-43

Azurmendi, Hugo F; Miller, Scott G; Whitman, Christian P et al. (2005) Half-of-the-sites binding of reactive intermediates and their analogues to 4-oxalocrotonate tautomerase and induced structural asymmetry of the enzyme. Biochemistry 44:7725-37

Azurmendi, Hugo F; Wang, Susan C; Massiah, Michael A et al. (2004) The roles of active-site residues in the catalytic mechanism of trans-3-chloroacrylic acid dehalogenase: a kinetic, NMR, and mutational analysis. Biochemistry 43:4082-91

Saraswat, Vibhor; Azurmendi, Hugo F; Mildvan, Albert S (2004) Mutational, NMR, and NH exchange studies of the tight and selective binding of 8-oxo-dGMP by the MutT pyrophosphohydrolase. Biochemistry 43:3404-14

Mildvan, Albert S (2004) Inverse thinking about double mutants of enzymes. Biochemistry 43:14517-20

Gabelli, Sandra B; Bianchet, Mario A; Azurmendi, Hugo F et al. (2004) Structure and mechanism of GDP-mannose glycosyl hydrolase, a Nudix enzyme that cleaves at carbon instead of phosphorus. Structure 12:927-35

Massiah, Michael A; Saraswat, Vibhor; Azurmendi, Hugo F et al. (2003) Solution structure and NH exchange studies of the MutT pyrophosphohydrolase complexed with Mg(2+) and 8-oxo-dGMP, a tightly bound product. Biochemistry 42:10140-54