Reverse action of ribonuclease T1 in frozen aqueous systems.

Abstract:

:We have studied ribonuclease T1 (EC 3.1-27.3)-catalysed synthesis of guanylyl-(3'-->5')cytidine in frozen aqueous reaction mixtures at -10 degrees C and in solution at 0 degree C in order to investigate whether ribonuclease-catalysed synthetic reactions can take advantage of the yield-increasing effect of freezing as was reported for protease-catalysed peptide synthesis. Under frozen state conditions, substantially increased yields of GpC were obtained compared to the reactions in solution. From the fact that no irreversible hydrolysis of the 2'3'-cyclic donor was observed it can be concluded that transesterification of the newly formed phosphodiester bond is the most important yield-limiting factor in ribonuclease T1-catalysed dinucleoside phosphate synthesis.

journal_name

Biol Chem

journal_title

Biological chemistry

authors

Haensler M,Hahn U,Jakubke HD

doi

10.1515/bchm.1997.378.2.115

subject

Has Abstract

pub_date

1997-02-01 00:00:00

pages

115-8

issue

2

eissn

1431-6730

issn

1437-4315

journal_volume

378

pub_type

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