The study of PLP-dependent enzymes and their part in amino acid changes is a fascinating aspect. These chemicals can catalyze a variety of responses, including decarboxylation, racemization, and transformation of one amino acid to another. In this discussion, we'll investigate these changes beginning from the PLP adduct of (S)-serine, a common amino acid. This investigation will give insights into the flexibility and complexity of biochemical reactions catalyzed by PLP-dependent enzymes.
We learned that three different amino acid transformations of PLP-dependent enzymes can result from different conformations of the PLP-amino acid imine adduct in the active site. Starting from the PLP adduct of (S)-serine, show mechanisms for a) Decarboxylation of serine b) Racemization of serine c) Conversion of serine to glycine and formaldehyde.
We learned that three different amino acid transformations of PLP-dependent enzymes can result from different conformations of the PLP-amino acid imine adduct in the active site. Starting from the PLP adduct of (S)-serine, show mechanisms for a) Decarboxylation of serine b) Racemization of serine c) Conversion of serine to glycine and formaldehyde.
Human Anatomy & Physiology (11th Edition)
11th Edition
ISBN:9780134580999
Author:Elaine N. Marieb, Katja N. Hoehn
Publisher:Elaine N. Marieb, Katja N. Hoehn
Chapter1: The Human Body: An Orientation
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We learned that three different amino acid transformations of PLP-dependent enzymes can
result from different conformations of the PLP-amino acid imine adduct in the active site.
Starting from the PLP adduct of (S)-serine, show mechanisms for
a) Decarboxylation of serine
b) Racemization of serine
c) Conversion of serine to glycine and formaldehyde.
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