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

Tomasz Manszewski; Kriti Singh; Barbara Imiolczyk; Mariusz Jaskolski

doi:10.5114/bta.2013.46434

eISSN: 2353-9461
ISSN: 0860-7796

BioTechnologia

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abstract:

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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

DOI: https://doi.org/10.5114/bta.2013.46434

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.

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

Tomasz Manszewski , Kriti Singh , Barbara Imiolczyk , Mariusz Jaskolski

Tomasz Manszewski

,

Kriti Singh

,

Barbara Imiolczyk

,

Mariusz Jaskolski