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2,942 Newest Publications in biochemistry
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A Route from Darkness to Light: Emergence and Evolution of Luciferase Activity in AMP-CoA-Ligases Inferred from a Mealworm Luciferase-like Enzyme
30-05-2013 | V. R. Viviani; R. A. Prado; D. R. Neves; D. Kato; J. A. Barbosa, Biochemistry, 2013
The origin of luciferases and of bioluminescence is enigmatic. In beetles, luciferases seem to have evolved from AMP-CoA-ligases. How the new oxygenase luminogenic function originated from AMP-ligases leading to luciferases is one of the most challenging mysteries of bioluminescence. ...
Reversal of the Substrate Specificity of CMP N-Glycosidase to dCMP
28-05-2013 | Megan D. Sikowitz; Lisa E. Cooper; Tadhg P. Begley; Pierre Alexandre Kaminski; Steven E. Ealick, Biochemistry, 2013
MilB is a CMP hydrolase involved in the early steps of biosynthesis of the antifungal compound mildiomycin. An enzyme from the bacimethrin biosynthetic pathway, BcmB, is closely related to MilB in both sequence and function. These two enzymes belong to the nucleoside ...
Interactions between Cytochromes P450 2B4 (CYP2B4) and 1A2 (CYP1A2) Lead to Alterations in Toluene Disposition and P450 Uncoupling
28-05-2013 | James R. Reed; George F. Cawley; Wayne L. Backes, Biochemistry, 2013
The goal of this study was to characterize the effects of CYP1A2·CYP2B4 complex formation on the rates and efficiency of toluene metabolism by comparing the results from simple reconstituted systems containing P450 reductase (CPR) and a single P450 to those using a mixed system containing CPR ...
The Crystal Structure of Mycobacterium tuberculosis NrdH at 0.87 Å Suggests a Possible Mode of Its Activity
28-05-2013 | Swastik Phulera; Shekhar C. Mande, Biochemistry, 2013
Members of the NrdH family of redox proteins, which consists of small glutaredoxin-like proteins with thioredoxin-like activity, serve as the reducing partners of class Ib ribonucleotide reductases. Here, we report the crystal structure of NrdH from Mycobacterium tuberculosis, refined to a ...
The Lipid Bilayer-Inserted Membrane Protein BamA of Escherichia coli Facilitates Insertion and Folding of Outer Membrane Protein A from Its Complex with Skp
24-05-2013 | Geetika J. Patel; Jörg H. Kleinschmidt, Biochemistry, 2013
Folding of β-barrel membrane proteins, either from a urea-unfolded form or from chaperone-bound aqueous forms, has been characterized for pure lipid bilayers. The impact of preinserted integral proteins from biomembranes has not been examined in biophysical comparisons, but this knowledge is ...
Correction to Metal Binding Properties of Escherichia coli YjiA, a Member of the Metal Homeostasis-Associated COG0523 Family of GTPases
24-05-2013 | Andrew M. Sydor; Marco Jost; Katherine S. Ryan; Kaitlyn E. Turo; Colin D. Douglas; Catherine L. Drennan; Deborah B. ..., Biochemistry, 2013
Biochemistry DOI: 10.1021/bi4006094
Defining a Key Receptor–CheA Kinase Contact and Elucidating Its Function in the Membrane-Bound Bacterial Chemosensory Array: A Disulfide Mapping and TAM-IDS Study
23-05-2013 | Kene N. Piasta; Caleb J. Ulliman; Peter F. Slivka; Brian R. Crane; Joseph J. Falke, Biochemistry, 2013
The three core components of the ubiquitous bacterial chemosensory array — the transmembrane chemoreceptor, the histidine kinase CheA, and the adaptor protein CheW — assemble to form a membrane-bound, hexagonal lattice in which receptor transmembrane signals regulate kinase activity. Both the ...
The 3.2 Å Resolution Structure of a Receptor:CheA:CheW Signaling Complex Defines Overlapping Binding Sites and Key Residue Interactions within Bacterial Chemosensory Arrays
23-05-2013 | Xiaoxiao Li; Aaron D. Fleetwood; Camille Bayas; Alexandrine M. Bilwes; Davi R. Ortega; Joseph J. Falke; Igor B. Zhul ..., Biochemistry, 2013
Bacterial chemosensory arrays are composed of extended networks of chemoreceptors (also known as methyl-accepting chemotaxis proteins, MCPs), the histidine kinase CheA, and the adaptor protein CheW. Models of these arrays have been developed from cryoelectron microscopy, crystal structures of ...
Broad Substrate Specificity of the Loading Didomain of the Lipomycin Polyketide Synthase
23-05-2013 | Satoshi Yuzawa; Clara H. Eng; Leonard Katz; Jay D. Keasling, Biochemistry, 2013
LipPks1, a polyketide synthase subunit of the lipomycin synthase, is believed to catalyze the polyketide chain initiation reaction using isobutyryl-CoA as a substrate, followed by an elongation reaction with methylmalonyl-CoA to start the biosynthesis of antibiotic α-lipomycin in Streptomyces ...
Effect of Dimerization on Dihydrofolate Reductase Catalysis
22-05-2013 | Jiannan Guo; E. Joel Loveridge; Louis Y. P. Luk; Rudolf K. Allemann, Biochemistry, 2013
Dihydrofolate reductase (DHFR) from the hyperthermophile Thermotoga maritima (TmDHFR) forms a very stable homodimer, while DHFRs from other organisms are monomers. We investigated the effect of dimerization on DHFR catalysis by preparing a dimeric variant, Xet-3, of DHFR from Escherichia coli ...
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