SHORT COMMUNICATION
Structural enzymology at the legume-microbe interface:
S-adenosyl-L-homocysteine hydrolase of rhizobia
Publication date: 2014-10-23
BioTechnologia 2013;94(1):38-39
ABSTRACT
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.
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.
REFERENCES (6)
| eISSN: | 2353-9461 |
| ISSN: | 0860-7796 |
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