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1.21.4.2
Analysis of proline reduction in the nosocomial pathogen Clostridium difficile
Clostridioides difficile
1.21.4.2
Clostridial glycine reductase: protein C, the acetyl group acceptor, catalyzes the arsenate-dependent decomposition of acetyl phosphate
Acetoanaerobium sticklandii
1.21.4.2
Cys359 of GrdD is the active-site thiol that catalyses the final step of acetyl phosphate formation by glycine reductase from Eubacterium acidaminophilum
Peptoclostridium acidaminophilum
1.21.4.2
Glycine reductase mechanism
Acetoanaerobium sticklandii
1.21.4.2
Glycine reductase mechanism
Peptoclostridium acidaminophilum
1.21.4.2
Glycine reductase mechanism
Tissierella creatinophila
1.21.4.2
Glycine reductase mechanism
Treponema denticola
1.21.4.2
Glycine reductase of Clostridium littorale. Cloning, sequencing, and molecular analysis of the grdAB operon that contains two in-frame TGA codons for selenium incorporation
Peptoclostridium litorale
1.21.4.2
Glycine reductase protein C. Properties and characterization of its role in the reductive cleavage of Se-carboxymethyl-selenoprotein A
Acetoanaerobium sticklandii
1.21.4.2
Glycine reductase selenoprotein A is not a glycoprotein: the positive periodic acid-Schiff reagent test is the result of peptide bond cleavage and carbonyl group generation
Acetoanaerobium sticklandii
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