DDSHDyssegmental Dysplasia, Silverman-Handmaker
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In such a mechanism, the heme-free AhbAB complex would catalyze the decarboxylation of SH to DDSH in M.
As shown in Figure 4, DDSH was formed by the action of purified AhbAB independent of the absence or presence of added heme.
During the alternative heme biosynthesis in archaea and sulfate-reducing bacteria the AhbC protein catalyzes the removal of the acetate side chains on rings A and B of DDSH yielding Fe-COPRO III.
These results clearly demonstrated that the gene MbarA1793 indeed encodes the enzyme AhbC which is responsible for the conversion of DDSH into Fe-COPRO III during the alternative heme biosynthesis in M.