eISSN: 2353-9461
ISSN: 0860-7796
BioTechnologia
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1/2013
vol. 94
 
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abstract:
Short communication

Structural enzymology at the legume-microbe interface: S-adenosyl-L-homocysteine hydrolase of rhizobia

Tomasz Manszewski
,
Kriti Singh
,
Barbara Imiolczyk
,
Mariusz Jaskolski

BioTechnologia vol. 94(1) C pp. 38-39 C 2013
Online publish date: 2014/10/23
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S-adenosyl-L-methionine (SAM) is the most common substrate used in biological methylation reactions. During

methyl group transfer, S-adenosyl-L-homocysteine (SAH) is formed as a byproduct. Since SAH is a strong inhibitor

of the ubiquitous SAM dependent methylation reactions, removal of SAH by enzymatic hydrolysis serves as an

important mechanism in the control of cellular methylation processes.
 
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