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Methenyl-tetrahydromethanopterin cyclohydrolase in cell extracts of Methanobacterium.

Abstract：

:Cell extracts of Methanobacterium thermoautotrophicum possess a methenyl-tetrahydromethanopterin (methenyl-H4MPT) cyclohydrolase. The enzyme catalyzes the hydrolysis of methenyl-H4MPT to formyltetrahydromethanopterin (formyl-H4MPT). The reaction is reversible and both the rate and extent of the reaction depend on the pH and the buffer used. Similarly, the nonenzymatic hydrolysis of methenyl-H4MPT is highly dependent on pH and buffer. An active derivative of methenyl-H4MPT was obtained in 94% yield by reacting H4MPT with formic acid in the presence of excess acetic acid under anoxic conditions at 80 degrees C for 3 h. H NMR spectroscopy and fast atom bombardment mass spectrometry revealed the product to be a derivative of methenyl-H4MPT which had lost the alpha-hydroxyglutarylphosphate unit. In spite of this loss, this derivative served both as a substrate for methanogenesis and for the cyclohydrolase. Comparison of the properties of the products of the enzymatic and nonenzymatic hydrolyses indicates that the enzymatic reaction yields N5-formyl-H4MPT whereas the nonenzymatic reaction yields N10-formyl-H4MPT.

journal_name

Arch Biochem Biophys

journal_title

Archives of biochemistry and biophysics

authors

Donnelly MI,Escalante-Semerena JC,Rinehart KL Jr,Wolfe RS

doi

10.1016/0003-9861(85)90227-9

subject

Has Abstract

pub_date

1985-11-01 00:00:00

pages

430-9

issue

2

eissn

0003-9861

issn

1096-0384

pii

0003-9861(85)90227-9

journal_volume

242

pub_type

杂志文章

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