Search results for: Steven L. Roderick

Items from 1 to 17 out of 17 results

article

Design of O -Acetylserine Sulfhydrylase Inhibitors by Mimicking Nature

Enea Salsi, Alexander S. Bayden, Francesca Spyrakis, Alessio Amadasi, more

Journal of Medicinal Chemistry > 2010 > 53 > 1 > 345 - 356

article

Structure of the Ternary Complex of Phosphomevalonate Kinase: The Enzyme and Its Family

John L. Andreassi, Matthew W. Vetting, Patrick W. Bilder, Steven L. Roderick, more

Biochemistry > 2009 > 48 > 27 > 6461 - 6468

article

Roles of Histidines 154 and 189 and Aspartate 139 in the Active Site of Serine Acetyltransferase from Haemophilus influenzae ^†

Rong Guan, Steven L. Roderick, Bin Huang, Paul F. Cook

Biochemistry > 2008 > 47 > 24 > 6322 - 6328

article

Structure and function of phosphatidylcholine transfer protein (PC-TP)/StarD2

Keishi Kanno, Michele K. Wu, Erez F. Scapa, Steven L. Roderick, more

BBA - Molecular and Cell Biology of Lipids > 2007 > 1771 > 6 > 654-662

Phosphatidylcholine transfer protein (PC-TP) is a highly specific soluble lipid binding protein that transfers phosphatidylcholine between membranes in vitro. PC-TP is a member of the steroidogenic acute regulatory protein-related transfer (START) domain superfamily. Although its biochemical properties and structure are well characterized, the functions of PC-TP in vivo remain incompletely understood...

article

A polymorphism in New Zealand inbred mouse strains that inactivates phosphatidylcholine transfer protein

Huei-Ju Pan, Diana S. Agate, Benjamin L. King, Michele K. Wu, more

FEBS Letters > 2006 > 580 > 25 > 5953-5958

New Zealand obese (NZO/HlLt) male mice develop polygenic diabetes and altered phosphatidylcholine metabolism. The gene encoding phosphatidylcholine transfer protein (PC-TP) is sited within the support interval for Nidd3, a recessive NZO-derived locus on Chromosome 11 identified by prior segregation analysis between NZO/HlLt and NON/Lt. Sequence analysis revealed that the NZO-derived PC-TP contained...

article

Pentapeptide Repeat Proteins ^†

Matthew W. Vetting, Subray S. Hegde, J. Eduardo Fajardo, Andras Fiser, more

Biochemistry > 2006 > 45 > 1 > 1 - 10

article

The lac operon galactoside acetyltransferase

Steven L. Roderick

Comptes rendus - Biologies > 2005 > 328 > 6 > 568-575

Of the proteins encoded by the three structural genes of the lac operon, the galactoside acetyltransferase (thiogalactoside transacetylase, LacA, GAT) encoded by lacA is the only protein whose biological role remains in doubt. Here, we briefly note the classical literature that led to the identification and initial characterization of GAT, and focus on more recent results which have revealed its chemical...

article

The serine acetyltransferase reaction: acetyl transfer from an acylpantothenyl donor to an alcohol

Corey M. Johnson, Steven L. Roderick, Paul F. Cook

Archives of Biochemistry and Biophysics > 2005 > 433 > 1 > 85-95

Serine acetyltransferase is a member of the left-handed parallel β-helix family of enzymes that catalyzes the committed step in the de novo synthesis of l-cysteine in bacteria and plants. The enzyme has an ordered kinetic mechanism with acetyl CoA bound prior to l-serine and O-acetyl-l-serine released prior to CoA. The rate-limiting step along the reaction pathway is the nucleophilic attack of the...

article

Structure and functions of the GNAT superfamily of acetyltransferases

Matthew W. Vetting, Luiz Pedro S. de Carvalho, Michael Yu, Subray S. Hegde, more

Archives of Biochemistry and Biophysics > 2005 > 433 > 1 > 212-226

The Gcn5-related N-acetyltransferases are an enormous superfamily of enzymes that are universally distributed in nature and that use acyl-CoAs to acylate their cognate substrates. In this review, we will examine those members of this superfamily that have been both structurally and mechanistically characterized. These include aminoglycoside N-acetyltransferases, serotonin N-acetyltransferase, glucosamine-6-phosphate...

article

Chemical Mechanism of the Serine Acetyltransferase from Haemophilus influenzae ^†

Corey M. Johnson, Bin Huang, Steven L. Roderick, Paul F. Cook

Biochemistry > 2004 > 43 > 49 > 15534 - 15539

article

Kinetic mechanism of the serine acetyltransferase from Haemophilus influenzae

Corey M. Johnson, Bin Huang, Steven L. Roderick, Paul F. Cook

Archives of Biochemistry and Biophysics > 2004 > 429 > 2 > 115-122

The kinetic mechanism of serine acetyltransferase from Haemophilus influenzae was studied in both reaction directions. The enzyme catalyzes the conversion of acetyl CoA and l-serine to O-acetyl-l-serine (OAS) and coenzyme A (CoASH). In the direction of l-serine acetylation, an equilibrium ordered mechanism is assigned at pH 6.5. The initial velocity pattern in the absence of added inhibitors is best...

article

Structure of Serine Acetyltransferase in Complexes with CoA and Its Cysteine Feedback Inhibitor ^† ^, ^‡

Laurence R. Olsen, Bin Huang, Matthew W. Vetting, Steven L. Roderick

Biochemistry > 2004 > 43 > 20 > 6013 - 6019

article

A Bacterial Acetyltransferase Capable of Regioselective N-Acetylation of Antibiotics and Histones

Matthew W Vetting, Sophie Magnet, Edward Nieves, Steven L Roderick, more

Chemistry & Biology > 2004 > 11 > 4 > 565-573

The Salmonella enterica chromosomally encoded AAC(6′)-Iy has been shown to confer broad aminoglycoside resistance in strains in which the structural gene is expressed. The three-dimensional structures reported place the enzyme in the large Gcn5-related N-acetyltransferase (GNAT) superfamily. The structure of the CoA-ribostamycin ternary complex allows us to propose a chemical mechanism for the reaction,...

article

Human phosphatidylcholine transfer protein: purification, crystallization and preliminary X-ray diffraction data

Wayne W. Chan, Steven L. Roderick, David E. Cohen

Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular Enzymology > 2002 > 1596 > 1 > 1-5

We have expressed, purified and crystallized recombinant human phosphatidylcholine transfer protein (PC-TP) and selenomethionyl PC-TP bound to dilinoleoyl phosphatidylcholine. The biochemical properties of native and selenomethionyl PC-TP were indistinguishable, and the two proteins crystallized under similar conditions. Both native and selenomethionyl PC-TP crystallized in two distinct space groups...

article

Structure of the lac Operon Galactoside Acetyltransferase

Xing-Guo Wang, Laurence R. Olsen, Steven L. Roderick

Structure > 2002 > 10 > 4 > 581-588

The galactoside acetyltransferase (thiogalactoside transacetylase) of Escherichia coli (GAT, LacA, EC 2.3.1.18) is a gene product of the classical lac operon. GAT may assist cellular detoxification by acetylating nonmetabolizable pyranosides, thereby preventing their reentry into the cell. The structure of GAT has been solved in binary complexes with acetyl-CoA or CoA and in ternary complexes with...

article

Crystal Structure of Vat(D): An Acetyltransferase That Inactivates Streptogramin Group A Antibiotics ^† ^, ^‡

Michele Sugantino, Steven L. Roderick

Biochemistry > 2002 > 41 > 7 > 2209 - 2216

article

Structure of the Escherichia coli GlmU Pyrophosphorylase and Acetyltransferase Active Sites ^† ^, ^‡

Laurence R. Olsen, Steven L. Roderick

Biochemistry > 2001 > 40 > 7 > 1913 - 1921

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