A5043323040- Enzyme Structure and Function
- Biochemical and Molecular Research
- Amino Acid Enzymes and Metabolism
- Protein Structure and Dynamics
- Metabolism and Genetic Disorders
- Microbial Metabolic Engineering and Bioproduction
- Enzyme Production and Characterization
- Biochemical Acid Research Studies
- Microbial bioremediation and biosurfactants
- ATP Synthase and ATPases Research
- Metal complexes synthesis and properties
- Folate and B Vitamins Research
- Organophosphorus compounds synthesis
- Mitochondrial Function and Pathology
- Cancer Research and Treatments
- Chemical Reaction Mechanisms
- Organometallic Complex Synthesis and Catalysis
- Neurological diseases and metabolism
- Metabolomics and Mass Spectrometry Studies
- Bacterial Genetics and Biotechnology
- Chemical Synthesis and Characterization
- Porphyrin Metabolism and Disorders
- Crystal structures of chemical compounds
- Enzyme function and inhibition
- Metalloenzymes and iron-sulfur proteins
University of New Mexico
2010-2020
Case Western Reserve University
1997-2011
Boston University
2000-2009
Biotechnology Institute
1996-2009
Institute of Biophysics
2009
Chinese Academy of Sciences
2009
Illinois Institute of Technology
2001-2008
Physical Sciences (United States)
2005-2008
Hauptman-Woodward Medical Research Institute
2007-2008
The Ohio State University
2008
Enzymes provide enormous rate enhancements, unmatched by any other type of catalyst. The stabilization high-energy states along the reaction coordinate is crux catalytic power enzymes. We report atomic-resolution structure a intermediate stabilized in active site an enzyme. Crystallization phosphorylated beta-phosphoglucomutase presence Mg(II) cofactor and either substrates glucose 1-phosphate or 6-phosphate produced crystals enzyme-Mg(II)-glucose 1,6-(bis)phosphate complex, which diffracted...
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTAncestry of the 4-chlorobenzoate dehalogenase: analysis amino acid sequence identities among families acyl:adenyl ligases, enoyl-CoA hydratases/isomerases, and acyl-CoA thioesterasesPatricia C. Babbitt, George L. Kenyon, Brian M. Martin, Hugues Charest, Michel Slyvestre, Jeffrey D. Scholten, Kai Hsuan Chang, Po Huang Liang, Debra Dunaway-MarianoCite this: Biochemistry 1992, 31, 24, 5594–5604Publication Date (Print):June 1, 1992Publication History...
Microbial enzyme systems may be used in the biodegradation of persistent environmental pollutants. The three polypeptide components one such system, 4-chlorobenzoate dehalogenase have been isolated, and chemical steps 4-hydroxybenzoate-forming reaction that they catalyze identified. genes contained within a 4.5-kilobase Pseudomonas sp. strain CBS3 chromosomal DNA fragment encode activity were selectively expressed transformed Escherichia coli . Oligonucleotide sequencing revealed stretch...
Significance Here, we examine the activity profile of haloalkanoic acid dehalogenase (HAD) superfamily by screening a customized library against >200 enzymes from broad sampling superfamily. From this dataset, can infer function nearly 35% Overall, was found to show high substrate ambiguity, with 75% utilizing greater than five substrates. In addition, HAD members least amount structural accessorization Rossmann fold were be most specific, suggesting that elaboration core domain may have...
Here we describe the three-dimensional structure of 4-chlorobenzoyl-CoA dehalogenase from Pseudomonas sp. strain CBS-3. This enzyme catalyzes hydrolysis to 4-hydroxybenzoyl-CoA. The molecular enzyme/4-hydroxybenzoyl-CoA complex was solved by techniques multiple isomorphous replacement, solvent flattening, and averaging. Least-squares refinement protein model reduced crystallographic R factor 18.8% for all measured X-ray data 30 1.8 Å resolution. investigation this revealed that is a trimer....
Phosphonoacetaldehyde hydrolase (phosphonatase) catalyzes the hydrolysis of phosphonoacetaldehyde to acetaldehyde and phosphate using Mg(II) as cofactor. The reaction proceeds via a novel bicovalent catalytic mechanism in which an active-site nucleophile abstracts phosphoryl group from Schiff-base intermediate formed Lys53 phosphonoacetaldehyde. In this study, X-ray crystal structure Bacillus cereus phosphonatase homodimer complexed with (product) analogue tungstate (K(i) = 50 microM)...
The crystal structure of pyruvate phosphate dikinase, a histidyl multiphosphotransfer enzyme that synthesizes adenosine triphosphate, reveals three-domain molecule in which the phosphohistidine domain is flanked by nucleotide and phosphoenolpyruvate/pyruvate domains, with two substrate binding sites approximately 45 angstroms apart. modes have been deduced analogy to D-Ala-D-Ala ligase kinase. Coupling between remote active facilitated conformational states domain. While represents state...
Members of the adenylate-forming family enzymes play a role in metabolism halogenated aromatics and short, medium, long chain fatty acids, as well biosynthesis menaquinone, peptide antibiotics, siderophores. This includes subfamily acyl- aryl-CoA ligases that catalyze thioester synthesis through two half-reactions. A carboxylate substrate first reacts with ATP to form an acyl-adenylate. Subsequent release product PP i, enzyme binds CoA, which attacks activated acyl group displace AMP....
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTInvestigations of substrate specificity and reaction mechanism several kinases using chromium(III) adenosine 5'-triphosphate 5'-diphosphateDebra Dunaway-Mariano W. ClelandCite this: Biochemistry 1980, 19, 7, 1506–1515Publication Date (Print):April 1, 1980Publication History Published online1 May 2002Published inissue 1 April 1980https://doi.org/10.1021/bi00548a038RIGHTS & PERMISSIONSArticle Views131Altmetric-Citations103LEARN ABOUT THESE...
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTPreparation and properties of chromium(III) adenosine 5'-triphosphate, 5'-diphosphate, related complexesDebra Dunaway-Mariano W. ClelandCite this: Biochemistry 1980, 19, 7, 1496–1505Publication Date (Print):April 1, 1980Publication History Published online1 May 2002Published inissue 1 April 1980https://pubs.acs.org/doi/10.1021/bi00548a037https://doi.org/10.1021/bi00548a037research-articleACS PublicationsRequest reuse permissionsArticle...
Oxalate secretion by fungi is known to be associated with fungal pathogenesis. In addition, oxalate toxicity a concern for the commercial application of in food and drug industries. Although generated through several different biochemical pathways, oxaloacetate acetylhydrolase (OAH)-catalyzed hydrolytic cleavage appears an especially important route. Below, we report cloning Botrytis cinerea oahA gene demonstration that disruption this results loss formation. complementation have shown...
Features of the oxidative cleavage reactions diastereomers dimeric lignin model compounds, which are models major types structural units found in backbone, were examined. Cation radicals these substances generated by using SET-sensitized photochemical and Ce(IV) peroxidase promoted processes, nature kinetics their C−C bond determined. The results show that significant differences exist between rates cation radical C1−C2 1,2-diaryl-(β-1) 1-aryl-2-aryloxy-(β-O-4) propan-1,3-diol lignins....
4-Chlorobenzoate:coenzyme A (4-CBA:CoA) ligase catalyzes 4-chlorobenzoyl-coenzyme formation in a two-step reaction consisting of the adenylation 4-chlorobenzoate with adenosine 5'-triphosphate followed by acyl transfer from 4-chlorobenzoyl 5'-monophosphate diester intermediate to coenzyme A. In this study, two core motifs present Pseudomonas sp. strain CBS3 4-CBA:CoA (motif I, 161T-S-G-T-T-G-L-P-K-G170, and motif II, 302Y-G-T-T-E306) conserved among sequences representing...
The soil-dwelling microbe,<i>Pseudomonas</i> sp. strain CBS-3, has attracted recent attention due to its ability survive on 4-chlorobenzoate as sole carbon source. biochemical pathway by which this organism converts 4-hydroxybenzoate consists of three enzymes: 4-chlorobenzoyl-CoA ligase, dehalogenase, and 4-hydroxybenzoyl-CoA thioesterase. Here we describe the three-dimensional structure thioesterase determined 2.0-Å resolution. Each subunit homotetramer is characterized a five-stranded...
Phosphoglucomutases catalyze the interconversion of D-glucose 1-phosphate and 6-phosphate, a reaction central to energy metabolism in all cells synthesis cell wall polysaccharides bacterial cells. Two classes phosphoglucomutases (alpha-PGM beta-PGM) are distinguished on basis their specificity for alpha- beta-glucose-1-phosphate. beta-PGM is member haloacid dehalogenase (HAD) superfamily, which includes sarcoplasmic Ca(2+)-ATPase, phosphomannomutase, phosphoserine phosphatase. unusual among...
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTCatalysis and thermodynamics of the phosphoenolpyruvate/phosphonopyruvate rearrangement. Entry into phosphonate class naturally occurring organophosphorus compoundsElise. Bowman, Michael. McQueney, Robert J. Barry, Debra. Dunaway-MarianoCite this: Am. Chem. Soc. 1988, 110, 16, 5575–5576Publication Date (Print):August 1, 1988Publication History Published online1 May 2002Published inissue 1 August...
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTAnalysis of sequence homologies in plant and bacterial pyruvate phosphate dikinase, enzyme I the phospoenolpyruvate:sugar phosphotransferase system other PEP-utilizing enzymes. Identification potential catalytic regulatory motifsDavid J. Pocalyko, Lawrence Carroll, Brian M. Martin, Patricia C. Babbitt, Debra Dunaway-MarianoCite this: Biochemistry 1990, 29, 48, 10757–10765Publication Date (Print):December 4, 1990Publication History Published online1...
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTIsolation and characterization of the three polypeptide components 4-chlorobenzoate dehalogenase from Pseudomonas sp. strain CBS-3Kai Hsuan Chang, Po Haung Liang, Wendie Beck, Jeffrey D. Scholten, Debra Dunaway-MarianoCite this: Biochemistry 1992, 31, 24, 5605–5610Publication Date (Print):June 1, 1992Publication History Published online1 May 2002Published inissue 1 June...
4-Chlorobenzoate:CoA ligase (CBAL) is a member of family adenylate-forming enzymes that catalyze two-step adenylation and thioester-forming reactions. In previous studies, we have provided structural evidence members this enzyme (exemplified by acetyl-CoA synthetase) use large domain rotation to the respective partial reactions [A. M. Gulick, V. J. Starai, A. R. Horswill, K. Homick, C. Escalante-Semerena, (2003) Biochemistry 42, 2866-2873]. CBAL catalyzes synthesis 4-chlorobenzoyl-CoA, first...
The haloacid dehalogenase (HAD) superfamily includes a variety of enzymes that catalyze the cleavage substrate C-Cl, P-C, and P-OP bonds via nucleophilic substitution pathways. All members possess alpha/beta core domain, many also small cap domain. active site domain is formed by four loops (corresponding to sequence motifs 1-4), which position cofactor-binding residues as well catalytic groups mediate "core" chemistry. responsible for diversification chemistry within family. A tight...