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Literature summary for 3.5.1.26 extracted from

  • Wang, Y.; Guo, H.C.
    Crystallographic snapshot of glycosylasparaginase precursor poised for autoprocessing (2010), J. Mol. Biol., 403, 120-130.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
-
Flavobacterium sp.

Protein Variants

Protein Variants Comment Organism
T152C the autoproteolysis-active precursor is kinetically slower than the wild type enzyme Flavobacterium sp.

Inhibitors

Inhibitors Comment Organism Structure
glycine reversible inhibitor Flavobacterium sp.

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Flavobacterium sp. glycosylasparaginase protein is synthesized as a single-chain precursor (inhibitor-free precursor) and requires a cis proteolysis of its own main-chain amide bond, splitting it into two subunits. Once autocleaved, the mature glycosylasparaginase with a free amino end exposed at Thr152 becomes active in glycoprotein degradation by binding to and processing its glycoasparagine substrate ?
-
?

Organism

Organism UniProt Comment Textmining
Flavobacterium sp.
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Flavobacterium sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information glycosylasparaginase protein is synthesized as a single-chain precursor (inhibitor-free precursor) and requires a cis proteolysis of its own main-chain amide bond, splitting it into two subunits. Once autocleaved, the mature glycosylasparaginase with a free amino end exposed at Thr152 becomes active in glycoprotein degradation by binding to and processing its glycoasparagine substrate Flavobacterium sp. ?
-
?

Synonyms

Synonyms Comment Organism
glycosylasparaginase
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Flavobacterium sp.