Just Arrange.  The enzyme serine hydroxymethyltransferase (SHMT) requires pyridoxal phosphate (PLP) as a cofactor. Arrange the steps of the likely mechanism for SHMT‑catalyzed serine degradation (producing glycine and N5,N10‑methylenetetrahydrofolate)

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Just Arrange. 

The enzyme serine hydroxymethyltransferase (SHMT) requires pyridoxal phosphate (PLP) as a cofactor.

Arrange the steps of the likely mechanism for SHMT‑catalyzed serine degradation (producing glycine and N5,N10‑methylenetetrahydrofolate)

The enzyme serine hydroxymethyltransferase (SHMT) requires pyridoxal phosphate (PLP) as a cofactor.
Arrange the steps of the likely mechanism for SHMT-catalyzed serine degradation (producing glycine and
N°,N!0-methylenetetrahydrofolate).
First step
Last step
Answer Bank
Formaldehyde is released, forming a PLP-stabilized carbanion. The formaldehyde reacts with tetrahydrofolate to
form N°,N10-methylenetetrahydrofolate.
The enzyme acts as a base and abstracts the hydrogen of the hydroxyl group on serine.
The N-terminal amine of serine performs a nucleophilic attack on enzyme-bound PLP, forming a covalent imido
linkage between serine and PLP.
The carbanion is protonated by the enzyme, forming glycine covalently linked to PLP.
An active site lysine reacts with the PLP to restore the active enzyme and release glycine.
Transcribed Image Text:The enzyme serine hydroxymethyltransferase (SHMT) requires pyridoxal phosphate (PLP) as a cofactor. Arrange the steps of the likely mechanism for SHMT-catalyzed serine degradation (producing glycine and N°,N!0-methylenetetrahydrofolate). First step Last step Answer Bank Formaldehyde is released, forming a PLP-stabilized carbanion. The formaldehyde reacts with tetrahydrofolate to form N°,N10-methylenetetrahydrofolate. The enzyme acts as a base and abstracts the hydrogen of the hydroxyl group on serine. The N-terminal amine of serine performs a nucleophilic attack on enzyme-bound PLP, forming a covalent imido linkage between serine and PLP. The carbanion is protonated by the enzyme, forming glycine covalently linked to PLP. An active site lysine reacts with the PLP to restore the active enzyme and release glycine.
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