Serine hydroxymethyltransferase: Difference between revisions
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== Introduction == | == Introduction == | ||
<Structure load='1kkj' size='450' frame='true' align='right' caption='Structure of Serine hydroxymethyltransferase' scene='Insert optional scene name here' /> | <Structure load='1kkj' size='450' frame='true' align='right' caption='Structure of Serine hydroxymethyltransferase isolated from Bacillus stearothermophilus' scene='Insert optional scene name here' /> | ||
[[Serine hydroxymethyltransferase]] (SHMT) is part of the pyridoxal phosphate-dependent enzymes. Specifically, the enzyme belongs to the alpha-class. | [[Serine hydroxymethyltransferase]] (SHMT) is part of the pyridoxal phosphate (PLP)-dependent enzymes. Specifically, the enzyme belongs to the alpha-class. This enzyme is utilized mainly for two functions. First, the enzyme catalyzes the reversible conversion of serine to glycine. Chemically speaking, the enzyme performs a retro-aldol cleavage. Second, the enzyme catalyzes the reversible conversion of tetrahydrofolate to 5,10-methylene tetrahydrofolate. | ||
</StructureSection> | </StructureSection> | ||
Revision as of 23:14, 28 October 2013
IntroductionIntroduction
|
Serine hydroxymethyltransferase (SHMT) is part of the pyridoxal phosphate (PLP)-dependent enzymes. Specifically, the enzyme belongs to the alpha-class. This enzyme is utilized mainly for two functions. First, the enzyme catalyzes the reversible conversion of serine to glycine. Chemically speaking, the enzyme performs a retro-aldol cleavage. Second, the enzyme catalyzes the reversible conversion of tetrahydrofolate to 5,10-methylene tetrahydrofolate. </StructureSection>