Serine hydroxymethyltransferase: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
== Introduction == | == Introduction == | ||
<Structure load='1kkj' size='450' frame='true' align='right' caption='Structure of [[Serine hydroxymethyltransferase]] isolated from Bacillus' 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 (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. There appear to be multiple isoforms of the enzyme in bacteria. Serine hydroxymethyltransferase isoforms have namely been identified from | [[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. There appear to be multiple isoforms of the enzyme in bacteria. Serine hydroxymethyltransferase isoforms have namely been identified from ''Escherichia coli'' and ''Bacillus stearothermophilus'' | ||
</StructureSection> | </StructureSection> | ||