Search Results - "Stieglitz, Kimberly A"
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Structural Insights for Drugs Developed for Phospholipase D Enzymes
Published in Current drug discovery technologies (2018)“…In recent years human phospholipase D enzymes (PLD1 and PLD2 isozymes) have emerged as drug targets for various diseases such as cardiovascular disease,…”
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Characterization of recombinant fructose-1,6-bisphosphatase gene mutations: evidence of inhibition/activation of FBPase protein by gene mutation
Published in Bioscience reports (28-02-2019)“…Specific residues of the highly regulated fructose-1,6-bisphosphatase (FBPase) enzyme serve as important contributors to the catalytic activity of the enzyme…”
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Development, Risk, and Resilience of Transgender Youth
Published in The Journal of the Association of Nurses in AIDS Care (01-05-2010)“…Transgender youth face unique and complex issues as they confront cultural expectations of gender expression and how these fit with what is natural for them…”
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The Structure of the R184A Mutant of the Inositol Monophosphatase Encoded by suhB and Implications for Its Functional Interactions in Escherichia coli
Published in The Journal of biological chemistry (14-09-2007)“…The Escherichia coli product of the suhB gene, SuhB, is an inositol monophosphatase (IMPase) that is best known as a suppressor of temperature-sensitive growth…”
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Structural Basis for Ordered Substrate Binding and Cooperativity in Aspartate Transcarbamoylase
Published in Proceedings of the National Academy of Sciences - PNAS (21-06-2005)“…X-ray structures of aspartate transcarbamoylase in the absence and presence of the first substrate carbamoyl phosphate are reported. These two structures in…”
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240s Loop Interactions Stabilize the T State of Escherichia coli Aspartate Transcarbamoylase
Published in The Journal of biological chemistry (28-05-2004)“…Here the functional and structural importance of interactions involving the 240s loop of the catalytic chain for the stabilization of the T state of aspartate…”
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The first high pH structure of Escherichia coli aspartate transcarbamoylase
Published in Proteins, structure, function, and bioinformatics (01-02-2009)“…The activity and cooperativity of Escherichia coli aspartate transcarbamoylase (ATCase) vary as a function of pH, with a maximum of both parameters at…”
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Crystal structure of the tetrameric inositol 1‐phosphate phosphatase (TM1415) from the hyperthermophile, Thermotoga maritima
Published in The FEBS journal (01-05-2007)“…The structure of the first tetrameric inositol monophosphatase (IMPase) has been solved. This enzyme, from the eubacterium Thermotoga maritima, similarly to…”
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Metal Specificity Is Correlated with Two Crucial Active Site Residues in Escherichia coli Alkaline Phosphatase
Published in Biochemistry (Easton) (14-06-2005)“…Escherichia coli alkaline phosphatase exhibits maximal activity when Zn2+ fills the M1 and M2 metal sites and Mg2+ fills the M3 metal site. When other metals…”
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Mobile loop mutations in an archaeal inositol monophosphatase: Modulating three‐metal ion assisted catalysis and lithium inhibition
Published in Protein science (01-02-2010)“…The inositol monophosphatase (IMPase) enzyme from the hyperthermophilic archaeon Methanocaldococcus jannaschii requires Mg2+ for activity and binds three to…”
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Reaching for Mechanistic Consensus Across Life Kingdoms: Structure and Insights into Catalysis of the myo-Inositol-1-phosphate Synthase (mIPS) from Archaeoglobus fulgidus
Published in Biochemistry (Easton) (11-01-2005)“…myo-Inositol-1-phosphate synthase (mIPS) catalyzes the first step in the synthesis of l-myo-inositol-1-phosphate. We have solved and refined the structure of…”
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T-state Inhibitors of E. coli Aspartate Transcarbamoylase that Prevent the Allosteric Transition
Published in Biochemistry (Easton) (22-08-2006)“…Escherichia coli aspartate transcarbamoylase (ATCase) catalyzes the committed step in pyrimidine nucleotide biosynthesis, the reaction between carbamoyl…”
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Crystal structure of a dual activity IMPase/FBPase (AF2372) from Archaeoglobus fulgidus. The story of a mobile loop
Published in The Journal of biological chemistry (21-06-2002)“…Several hyperthermophilic organisms contain an unusual phosphatase that has dual activity toward inositol monophosphates and fructose 1,6-bisphosphate. The…”
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A Single Amino Acid Substitution in the Active Site of Escherichia coli Aspartate Transcarbamoylase Prevents the Allosteric Transition
Published in Journal of molecular biology (03-06-2005)“…Modeling of the tetrahedral intermediate within the active site of Escherichia coli aspartate transcarbamoylase revealed a specific interaction with the…”
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Structure of the E.coli aspartate transcarbamoylase trapped in the middle of the catalytic cycle
Published in Journal of molecular biology (16-09-2005)“…Snapshots of the catalytic cycle of the allosteric enzyme aspartate transcarbamoylase have been obtained via X-ray crystallography. The enzyme in the…”
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Binding of Proteolytically Processed Phospholipase D from Streptomyces chromofuscus to Phosphatidylcholine Membranes Facilitates Vesicle Aggregation and Fusion
Published in Biochemistry (Easton) (20-11-2001)“…Ca2+-dependent phospholipase D is secreted from Streptomyces chromofuscus as an intact enzyme of 57 kDa (PLD57). Under certain growth conditions, PLD is…”
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Comparison of two T-state structures of regulatory-chain mutants of Escherichia coli aspartate transcarbamoylase suggests that His20 and Asp19 modulate the response to heterotropic effectors
Published in Acta crystallographica. Section D, Biological crystallography. (01-12-2007)“…Asp19 and His20 of Escherichia coli aspartate transcarbamoylase (EC 2.1.3.2) function in the binding of the triphosphate and ribose moieties of ATP and CTP and…”
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Unexpected similarity in regulation between an archaeal inositol monophosphatase/fructose bisphosphatase and chloroplast fructose bisphosphatase
Published in Protein science (01-04-2003)“…Hyperthermophilic archaea have an unusual phosphatase that exhibits activity toward both inositol‐1‐phosphate and fructose‐1,6‐bisphosphate, activities carried…”
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Crystal Structure of a Dual Activity IMPase/FBPase (AF2372) from Archaeoglobus fulgidus
Published in The Journal of biological chemistry (21-06-2002)“…Several hyperthermophilic organisms contain an unusual phosphatase that has dual activity toward inositol monophosphates and fructose 1,6-bisphosphate. The…”
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