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Crystallization (Commentary)
Reference
6.4.1.5
structure of the 750-kDa alpha6beta6 holoenzyme and comparison with 3-methylcrotonyl-CoA carboxylase, EC 6.4.1.4. Structural differences in the active site region of both enzymes explain their distinct substrate preferences and support two distinct lineages of biotin-dependent acyl-CoA carboxylases, one carboxylating the alpha carbon of a saturated organic acid and the other carboxylating the gamma carbon of an alpha-beta unsaturated acid. A glycine residue in geranyl-CoA carboxylase is replaced by phenylalanine in 3-methylcrotonyl-CoA carboxylase, which blocks access by the larger geranyl-CoA substrate
745854
6.4.1.5
structure of the hexamer of the beta-subunit, to 2.4 A resolution
745854
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