Low-solubility glycerol dehydratase, a chimeric enzyme of coenzyme B12-dependent glycerol and diol dehydratases
Low-solubility glycerol dehydratase, a chimeric enzyme of coenzyme B12-dependent glycerol and diol dehydratases
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低溶解度甘油脱水酶,辅酶 B12 依赖性甘油和二醇脱水酶的嵌合酶
DOI:
10.1007/s00203-008-0443-x
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发表时间:
2009
影响因子:
2.8
通讯作者:
T. Toraya
中科院分区:
文献类型:
--
作者:
T. Tobimatsu;Tsuneo Nishiki;Masaya Morimoto;Ryou Miyata;T. Toraya
Coenzyme B12-dependent diol and glycerol dehydratases are isofunctional enzymes, which catalyze dehydration of 1, 2-diols to produce corresponding aldehydes. Although the two types of dehydratases have high sequence homology, glycerol dehydratase is a soluble cytosolic enzyme, whereas diol dehydratase is a low-solubility enzyme associated with carboxysome-like polyhedral organelles. Since both the N-terminal 20 and 16 amino acid residues of the β and γ subunits, respectively, are indispensable for the low solubility of diol dehydratase, we constructed glycerol dehydratase-based chimeric enzymes which carried N-terminal portions of the β and γ subunits of diol dehydratase in the corresponding subunits of glycerol dehydratase. Addition of the diol dehydratase-specific N-terminal 34 and 33 amino acid residues of the β and γ subunits, respectively, was not enough to lower the solubility of glycerol dehydratase. A chimeric enzyme which carries the low homology region (residues 35–60) of the diol dehydratase β subunit in addition to the diol dehydratase-specific extra-regions of β and γ subunits showed low solubility comparable to diol dehydratase, although its hydropathy plot does not show any prominent hydrophobic peaks in these regions. It was thus concluded that short N-terminal sequences are sufficient to change the solubility of the enzyme.
影响因子:
2.9
作者:
McGee,DE;Richards,JH
通讯作者:
Richards,JH
影响因子:
2.9
作者:
GILL, SC;VONHIPPEL, PH
通讯作者:
VONHIPPEL, PH