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Crystallization and some properties of acetylpolyamine amidohydrolase from Mycoplana bullata.

Abstract：

:During the course of investigations on the catabolism of acetylpolyamines by microorganisms, we found that acetylpolyamine amidohydrolase was produced by Mycoplana bullata FERM BP-1845 and isolated the enzyme from the cell-free extract in crystalline form. The enzyme had an apparent molecular weight of 67 kDa and was composed of two identical subunits. The enzyme activity was inhibited by o-oxyquinoline and the crystalline enzyme contained one zinc atom per each subunit. The enzyme had an optimal pH around 8.0 with acetylputrescine as substrate and showed broad substrate specificity and high affinity towards various acetylpolyamines, such as acetylputrescine, acetylcadaverine, acetylspermidine, and acetylspermine.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Fujishiro K,Ando M,Uwajima T

doi

10.1016/s0006-291x(88)80997-5

subject

Has Abstract

pub_date

1988-12-30 00:00:00

pages

1169-74

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(88)80997-5

journal_volume

157

pub_type

杂志文章

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