Abstract

During the next five years studies will focus on the enzymology of dehalogenation and the enzymology of phosphorus-carbon bond formation and cleavage. These investigations are aimed at discovering, exploring and developing novel enzyme catalysts. The six specific aims of this project are: (1) to determine the substrate specificities and mechanisms of action of the enzymes of the 4-chlorobenzoate to the 4-hydroxybenzoate pathway of pseudomonas sp. CBS-3; (2) to engineer the pseudomonas sp. CBS-3 4-chlorobenzoate-CoA dehalogenase, (3) to determine the mechanism of P-C bond formation catalyzed by PEp mutase; (4) to determine the mechanism of action of the P-C bond cleaving enzymes phosphonoacetaldehyde hydrolase and phosphonoacetate hydrolase; (5) to determine the mode of P-C bond formation in the biosynthesis of phosphonotyrosine, and (6) to purify and characterize the phosphonopyruvate -ketodecarboxylase and 2-aminoethyl phosphonate transaminase of the 2-aminoethylphosphonate pathway.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
2R01GM028688-14
Application #
2175248
Study Section
Biochemistry Study Section (BIO)
Project Start
1981-02-01
Project End
1998-01-31
Budget Start
1994-02-01
Budget End
1995-01-31
Support Year
14
Fiscal Year
1994
Total Cost
Indirect Cost

  Institution

Name
University of Maryland College Park
Department
Chemistry
Type
Schools of Earth Sciences/Natur
DUNS #
City
College Park
State
MD
Country
United States
Zip Code
20742

  Publications

Latham, John A; Ji, Tianyang; Matthews, Kaila et al. (2017) Catalytic Mechanism of the Hotdog-Fold Thioesterase PA1618 Revealed by X-ray Structure Determination of a Substrate-Bound Oxygen Ester Analogue Complex. Chembiochem 18:1935-1943
Wu, Rui; Latham, John A; Chen, Danqi et al. (2014) Structure and catalysis in the Escherichia coli hotdog-fold thioesterase paralogs YdiI and YbdB. Biochemistry 53:4788-805
Latham, John A; Chen, Danqi; Allen, Karen N et al. (2014) Divergence of substrate specificity and function in the Escherichia coli hotdog-fold thioesterase paralogs YdiI and YbdB. Biochemistry 53:4775-87
Wang, Min; Song, Feng; Wu, Rui et al. (2013) Co-evolution of HAD phosphatase and hotdog-fold thioesterase domain function in the menaquinone-pathway fusion proteins BF1314 and PG1653. FEBS Lett 587:2851-9
Chen, Danqi; Latham, John; Zhao, Hong et al. (2012) Human brown fat inducible thioesterase variant 2 cellular localization and catalytic function. Biochemistry 51:6990-9
Zhuang, Zhihao; Latham, John; Song, Feng et al. (2012) Investigation of the catalytic mechanism of the hotdog-fold enzyme superfamily Pseudomonas sp. strain CBS3 4-hydroxybenzoyl-CoA thioesterase. Biochemistry 51:786-94
Song, Feng; Thoden, James B; Zhuang, Zhihao et al. (2012) The catalytic mechanism of the hotdog-fold enzyme superfamily 4-hydroxybenzoyl-CoA thioesterase from Arthrobacter sp. strain SU. Biochemistry 51:7000-16
Zhao, Hong; Lim, Kap; Choudry, Anthony et al. (2012) Correlation of structure and function in the human hotdog-fold enzyme hTHEM4. Biochemistry 51:6490-2
Kim, Alexander; Benning, Matthew M; OkLee, Sang et al. (2011) Divergence of chemical function in the alkaline phosphatase superfamily: structure and mechanism of the P-C bond cleaving enzyme phosphonoacetate hydrolase. Biochemistry 50:3481-94
Chen, Danqi; Wu, Rui; Bryan, Tyrel L et al. (2009) In vitro kinetic analysis of substrate specificity in enterobactin biosynthetic lower pathway enzymes provides insight into the biochemical function of the hot dog-fold thioesterase EntH. Biochemistry 48:511-3

Showing the most recent 10 out of 73 publications