Search Results - "Thoden, J B"
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Galactokinase: structure, function and role in type II galactosemia
Published in Cellular and molecular life sciences : CMLS (01-10-2004)“…The conversion of beta- D-galactose to glucose 1-phosphate is accomplished by the action of four enzymes that constitute the Leloir pathway. Galactokinase…”
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2
Molecular Structure of Dihydroorotase: A Paradigm for Catalysis through the Use of a Binuclear Metal Center
Published in Biochemistry (Easton) (19-06-2001)“…Dihydroorotase plays a key role in pyrimidine biosynthesis by catalyzing the reversible interconversion of carbamoyl aspartate to dihydroorotate. Here we…”
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3
The Small Subunit of Carbamoyl Phosphate Synthetase: Snapshots along the Reaction Pathway
Published in Biochemistry (Easton) (07-12-1999)“…Carbamoyl phosphate synthetase (CPS) plays a key role in both arginine and pyrimidine biosynthesis by catalyzing the production of carbamoyl phosphate. The…”
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Carbamoyl Phosphate Synthetase: Caught in the Act of Glutamine Hydrolysis
Published in Biochemistry (Easton) (23-06-1998)“…Carbamoyl phosphate synthetase from Escherichia coli catalyzes the production of carbamoyl phosphate from two molecules of Mg2+ATP, one molecule of…”
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Carbamoyl phosphate synthetase: an amazing biochemical odyssey from substrate to product
Published in Cellular and molecular life sciences : CMLS (30-10-1999)“…Carbamoyl phosphate synthetase (CPS) catalyzes one of the most remarkable reactions ever described in biological chemistry, in which carbamoyl phosphate is…”
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6
Three-Dimensional Structure of ATP:Corrinoid Adenosyltransferase from Salmonella typhimurium in Its Free State, Complexed with MgATP, or Complexed with Hydroxycobalamin and MgATP
Published in Biochemistry (Easton) (16-01-2001)“…In Salmonella typhimurium, formation of the cobalt−carbon bond in the biosynthetic pathway for adenosylcobalamin is catalyzed by the product of the cobA gene…”
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7
High‐resolution X‐ray structure of UDP‐galactose 4‐epimerase complexed with UDP‐phenol
Published in Protein science (01-11-1996)“…UDP‐galactose 4‐epimerase from Escherichia coli catalyzes the interconversion of UDP‐glucose and UDP‐galactose. In recent years, the enzyme has been the…”
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8
Molecular Structure of Escherichia coli PurT-Encoded Glycinamide Ribonucleotide Transformylase
Published in Biochemistry (Easton) (01-08-2000)“…In Escherichia coli, the PurT-encoded glycinamide ribonucleotide transformylase, or PurT transformylase, catalyzes an alternative formylation of glycinamide…”
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9
X-ray structures of the apo and MgATP-bound states of Dictyostelium discoideum myosin motor domain
Published in The Journal of biological chemistry (08-12-2000)“…Myosin is the most comprehensively studied molecular motor that converts energy from the hydrolysis of MgATP into directed movement. Its motile cycle consists…”
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10
Molecular Structure of Galactokinase
Published in The Journal of biological chemistry (29-08-2003)“…Galactokinase plays a key role in normal galactose metabolism by catalyzing the ATP-dependent phosphorylation of α-d-galactose to galactose 1-phosphate. In…”
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11
Human UDP-galactose 4-epimerase. Accommodation of UDP-N-acetylglucosamine within the active site
Published in The Journal of biological chemistry (04-05-2001)“…UDP-galactose 4-epimerase catalyzes the interconversion of UDP-galactose and UDP-glucose during normal galactose metabolism. One of the key structural features…”
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12
Crystallographic Evidence for Tyr 157 Functioning as the Active Site Base in Human UDP−Galactose 4-Epimerase
Published in Biochemistry (Easton) (16-05-2000)“…UDP-galactose 4-epimerase catalyzes the interconversion of UDP-glucose and UDP-galactose during normal galactose metabolism. In humans, deficiencies in this…”
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13
Three-Dimensional Structure of Escherichia coli Asparagine Synthetase B: A Short Journey from Substrate to Product
Published in Biochemistry (Easton) (07-12-1999)“…Asparagine synthetase B catalyzes the assembly of asparagine from aspartate, Mg2+ATP, and glutamine. Here, we describe the three-dimensional structure of the…”
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14
The Structure of 4-Hydroxybenzoyl-CoA Thioesterase from Arthrobacter sp. strain SU
Published in The Journal of biological chemistry (31-10-2003)“…The 4-chlorobenzoyl-CoA dehalogenation pathway in certain Arthrobacter and Pseudomonas bacterial species contains three enzymes: a ligase, a dehalogenase, and…”
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15
Rhodococcus l-Phenylalanine Dehydrogenase: Kinetics, Mechanism, and Structural Basis for Catalytic Specifity
Published in Biochemistry (Easton) (08-08-2000)“…Phenylalanine dehydrogenase catalyzes the reversible, pyridine nucleotide-dependent oxidative deamination of l-phenylalanine to form phenylpyruvate and…”
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Evolution of Enzymatic Activity in the Enolase Superfamily: Functional Studies of the Promiscuous o-Succinylbenzoate Synthase from Amycolatopsis
Published in Biochemistry (Easton) (13-01-2004)“…o-Succinylbenzoate synthase (OSBS) from Amycolatopsis, a member of the enolase superfamily, catalyzes the Mn2+-dependent exergonic dehydration of…”
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17
The Amidotransferase Family of Enzymes: Molecular Machines for the Production and Delivery of Ammonia
Published in Biochemistry (Easton) (22-06-1999)“…The amidotransferase family of enzymes utilizes the ammonia derived from the hydrolysis of glutamine for a subsequent chemical reaction catalyzed by the same…”
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18
Mechanism of the Reaction Catalyzed by Isoaspartyl Dipeptidase from Escherichia coli
Published in Biochemistry (Easton) (17-05-2005)“…Isoaspartyl dipeptidase (IAD) is a member of the amidohydrolase superfamily and catalyzes the hydrolytic cleavage of β-aspartyl dipeptides. Structural studies…”
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19
The 1.5-angstrom resolution crystal structure of bacterial luciferase in low salt conditions
Published in The Journal of biological chemistry (06-09-1996)“…Bacterial luciferase is a flavin monooxygenase that catalyzes the oxidation of a long-chain aldehyde and releases energy in the form of visible light. A new…”
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20
Movement of the Biotin Carboxylase B-domain as a Result of ATP Binding
Published in The Journal of biological chemistry (26-05-2000)“…Acetyl-CoA carboxylase catalyzes the first committed step in fatty acid synthesis. In Escherichia coli, the enzyme is composed of three distinct protein…”
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