ビタミンB_6酵素の電子スペクトルと構造との関連

概要

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Most of vitamin B_6-dependent enzymes exhibit absorption maxima at about 420mμ assignable to the coenzyme (pyridoxal phosphate) bound to the apoenzymes. However, some B_6 enzymes have their absorption maxima at ca. 360mμ(for example, aspartate β-decarboxylase) or at ca. 330mμ(phosphorylase, and several ones show at both 420 and 360mμ which are considered to be protonated imine (and its resonance form, i.e., keto enamine) and nonprotonated imine, respectively. The species absorbing light at about 330mμ are very complicated. For example, the structure for pyridoxal phosphate bound to the apoenzyme of phosphorylase b has been recently proposed to be carbinol amine located in a hydrophobic environment. On the other hand, the 340mμ species of glutamate decarboxylase at high pH region is supposed to be a substituted aldamine. This paper summarizes the relationships of the electronic spectra of vitamin B_6-dependent enzymes to their structures and presents some discussion based on the data obtained using suitable models.
日本ビタミン学会の論文
1973-02-25