Results 61 to 70 of about 13,885 (249)

Evaluating the Potential for Halogen Bonding in the Oxyanion Hole of Ketosteroid Isomerase Using Unnatural Amino Acid Mutagenesis [PDF]

open access: yesACS Chemical Biology, 2009
There has recently been an increasing interest in controlling macromolecular conformations and interactions through halogen bonding. Halogen bonds are favorable electrostatic interactions between polarized, electropositive chlorine, bromine, or iodine atoms and electronegative atoms such as oxygen or nitrogen.
Daniel A, Kraut   +3 more
openaire   +2 more sources

The plant Nudix hydrolase family. [PDF]

open access: yes, 2008
Nudix hydrolases are a family of proteins defined by a conserved amino-acid sequence GX(5)-EX(7)REUXEEXGU, where U is a hydrophobic residue. These enzymes are widely distributed among all classes of organisms and catalyze, with varying degrees of ...
Kraszewska, Elzbieta
core  

The novel missense mutation Met48Lys in FKBP22 changes its structure and functions. [PDF]

open access: yes, 2020
Mutations in the FKBP14 gene encoding FKBP22 (FK506 Binding Protein 22 kDa) cause kyphoscoliotic Ehlers-Danlos Syndrome (kEDS). The first clinical report showed that a lack of FKBP22 protein due to mutations causing nonsense-mediated decay of the mRNA ...
Bächinger, Hans Peter   +7 more
core  

GENETICS AND BIOCHEMISTRY OF DEHALOGENATING ENZYMES [PDF]

open access: yes, 1994
Microorganisms that can utilize halogenated compounds as a growth substrate generally produce enzymes whose function is carbon-halogen bond cleavage. Based on substrate range, reaction type and gene sequences, the dehalogenating enzymes can be classified
Janssen, Dick B   +2 more
core   +2 more sources

Genetic analysis of the NifM dependence of the nitrogenase iron proteins

open access: yesmBio
NifH maturation in certain diazotrophic bacteria depends on NifM, a protein with a PpiC-isomerase domain. Intriguingly, the putative proline substrate for NifM is present in NifH proteins from strains lacking nifM, raising questions regarding the actual ...
Zhuoting Xie   +6 more
doaj   +1 more source

Homologies in the NH2-terminal amino acid sequences of gamma-carboxymuconolactone decarboxylases and muconolactone isomerases.

open access: yesJournal of Biological Chemistry, 1980
gamma-Carboxymuconolactone decarobxylase (EC 4.1.1.44) and muconolactone isomerase (EC 5.3.3.4) mediate chemically analogous reactions in bacteria. The enzymes are inducible, and different metabolites trigger the respective syntheses of the decarboxylases in Acinetobacter calcoaceticus and Pseudomonas putida. The decarobxylases share similar oligomeric
W K, Yeh, P, Fletcher, N, Ornston
openaire   +2 more sources

Review

open access: yes, 2020
The chalcogen elements oxygen, sulfur, and selenium are essential constituents of side chain functions of natural amino acids. Conversely, no structural and biological function has been discovered so far for the heavier and more metallic tellurium ...
Agh R   +13 more
core   +1 more source

Molecular characterization of cyclophilin A-like protein from Piriformospora indica for its potential role to abiotic stress tolerance in E. coli [PDF]

open access: yes, 2013
BACKGROUND: Cyclophilins (CyP), conserved in all genera, are known to have regulatory responses of various cellular processes including stress tolerance. Interestingly, CyP has a crucial role as peptidyl-prolyl cis–trans isomerases (PPIases). Our earlier
Dipesh Trivedi   +4 more
core   +1 more source

Recent Advances in Virus–Host Interactions, Antiviral Bioactive Compounds, and Breeding for Disease Resistance of Porcine Epidemic Diarrhea Virus

open access: yesAnimal Research and One Health, EarlyView.
Basic research on the PEDV infection cycle and virus–host interactions advances the development of anti‐PEDV drugs and disease‐resistant breeding and helps strengthen disease prevention and control while reducing economic losses in the swine industry.
Heyong Wu   +8 more
wiley   +1 more source

The platelet-surface thiol isomerase enzyme ERp57 modulates platelet function [PDF]

open access: yes, 2011
Background: Thiol isomerases are a family of endoplasmic reticulum enzymes which orchestrate redox-based modifications of protein disulphide bonds. Previous studies have identified important roles for the thiol isomerases PDI and ERp5 in the regulation ...
Bicknell, Andrew B.   +5 more
core   +1 more source

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