Purification and Some Properties of Guanidinoacetate Amidinohydrolase Produced by Corynebacterium sp.

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概要

• 論文の詳細を見る

• Guanidinoacetate amidinohydrolase (EC 3.5.3.2) was purified from Corynebacterium sp. grown in a medium supplemented with guanidinoacetate, and some of its properties were investigated.The molecular weight of the enzyme was estimated to be 150,000 by gel filtration. SDS-polyacrylamide gel electrophoresis showed a single subunit component with a molecular weight of 38,000,suggesting that the enzyme is composed of four identical subunits. The isoelectric point of the enzyme was pH 5.8.The enzyme showed optimum activity at pH 9.0-9.5 and was stable at pH 6.0-10.5. 3-Guanidinopropionate and 4-guanidinobutyrate were respectively hydrolyzed 32% and 5% as fast as guanidinoacetate. The apparent K_m for guanidinoacetate was 16 mM. Incubation of the enzyme by 0-phenanthroline or 8-hydroxyquinoline resulted in almost complete inactivation. The activity of the inactivated enzyme was restored by incubation with Zn^<2+>. p-Chloromercuribenzoic acid and iodine effectively inhibited the enzyme activity. Glycine was a competitive inhibitor, and n-alkyl amines such as n-octylamine, n-decylamine and n-dodecylamine were uncompetitive inhibitors.

• 公益社団法人日本生物工学会の論文
• 1986-02-25

著者

• Shirokane Y

  Kikkoman Corp. Chiba Jpn

• Nakajima Moto-o

  Bioscience Research Laboratory Of Kikkoman Corporation

• SHIROKANE YOSHIO

  Bioscience Research Laboratory of Kikkoman Corporation

関連論文

• Purification and Some Properties of Guanidinoacetate Amidinohydrolase Produced by Corynebacterium sp.

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