Information on EC - thioglycine synthase

for references in articles please use BRENDA:EC6.2.2.1
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EC Tree
     6 Ligases
         6.2 Forming carbon-sulfur bonds
             6.2.2 Amide---thiol ligases
       thioglycine synthase
IUBMB Comments
Requires Mg2+. The enzyme is found in anaerobic methanogenic and methanotrophic archaea, where it modifies a glycine residue in EC, coenzyme-B sulfoethylthiotransferase (methyl-CoM reductase). Upon binding to its substrate, an external source of sulfide attacks the target amide bond generating a tetrahedral intermediate. The amide oxyanion attacks the gamma-phosphate of ATP, releasing ADP and forming a phosphorylated thiolate intermediate that collapses to form thioglycine and phosphate. In most organisms activity requires a second protein (TfuA) , which may allosterically activate this enzyme or assist in the delivery of sulfide to the substrate.
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The expected taxonomic range for this enzyme is: Archaea, Bacteria
Reaction Schemes
a [methyl-coenzyme M reductase]-glycine
a [methyl-coenzyme M reductase]-thioglycine
tvaH, ycaO, more
ATP + sulfide + a [methyl-coenzyme M reductase]-glycine = ADP + phosphate + a [methyl-coenzyme M reductase]-thioglycine
show the reaction diagram
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