Distinct reactions catalyzed by bacterial and yeast trans-aconitate methyltransferases.

Abstract:

:The trans-aconitate methyltransferase from the bacterium Escherichia coli catalyzes the monomethyl esterification of trans-aconitate and related compounds. Using two-dimensional (1)H/(13)C nuclear magnetic resonance spectroscopy, we show that the methylation is specific to one of the three carboxyl groups and further demonstrate that the product is the 6-methyl ester of trans-aconitate (E-3-carboxy-2-pentenedioate 6-methyl ester). A similar enzymatic activity is present in the yeast Saccharomyces cerevisiae. Although we find that yeast trans-aconitate methyltransferase also catalyzes the monomethyl esterification of trans-aconitate, we identify that the methylation product of yeast is the 5-methyl ester (E-3-carboxyl-2-pentenedioate 5-methyl ester). The difference in the reaction catalyzed by the two enzymes may explain why a close homologue of the E. coli methyltransferase gene is not found in the yeast genome and furthermore suggests that these two enzymes may play distinct roles. However, we demonstrate here that the conversion of trans-aconitate to each of these products can mitigate its inhibitory effect on aconitase, a key enzyme of the citric acid cycle, suggesting that these methyltransferases may achieve the same physiological function with distinct chemistries.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Cai H,Strouse J,Dumlao D,Jung ME,Clarke S

doi

10.1021/bi0022902

subject

Has Abstract

pub_date

2001-02-20 00:00:00

pages

2210-9

issue

7

eissn

0006-2960

issn

1520-4995

pii

bi0022902

journal_volume

40

pub_type

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