How does an inhibitor of n-acetylglucosamine phosphotransferase affect lysosomal protein sorting?

Biology

1 answer:

nalin [4]3 years ago

8 0

<h3><u>Answer;</u></h3>

Lysosomal proteins are secreted from the cell

<h3><u>Explanation</u>;</h3>

N-acetylglucosamine phosphotransferase is a golgi-localized enzyme that catalyzes the first step in the synthesis of the mannose 6-phosphate recognition marker on lysosomal acid hydrolases.
<em><u>The loss of function of this enzyme results in impaired lysosomal targeting of the acid hydrolases and decreased lysosomal degradatio</u></em>n.
Mannose 6-phosphate receptor sorts lysosomal hydrolases in trans Golgi Network; the first step is the recognition of lysosomal hydrolyses in the Golgi apparatus by N-acetylglucosamine phosphotransferase.
The enzyme has both the catalytic sites which binds both high mannose N-linked oligosaccharides and UDP-GlcNAc, and recognition site that binds to a signal patch present only on the surface of lysosomal hydrolases.

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