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Literature summary for 3.5.1.26 extracted from

  • Cui, T.; Liao, P.H.; Guan, C.; Guo, H.C.
    Purification and crystallization of precursors and autoprocessed enzymes of Flavobacterium glycosylasparaginase: an N-terminal nucleophile hydrolase (1999), Acta Crystallogr. Sect. D, 55, 1961-1964.
    View publication on PubMed
Search for more literature for 3.5.1.26

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Elizabethkingia meningoseptica

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging drop vapor diffusion technique, 1.9 A resolution, precursor and autoprocessed enzymes Elizabethkingia meningoseptica

Protein Variants

Protein Variants Comment Organism
T152A autoproteolytically deficient, no hydrolase activity Elizabethkingia meningoseptica

General Stability

General Stability Organism
glycine inhibits autoproteolysis reaction Elizabethkingia meningoseptica

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O Elizabethkingia meningoseptica belongs to N-terminal nucleophile hydrolase family 2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate
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 ?

Organism

Organism UniProt Comment Textmining
Elizabethkingia meningoseptica
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-
-

Source Tissue

Source Tissue Comment Organism Textmining
placenta
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 Elizabethkingia meningoseptica
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O belongs to N-terminal nucleophile hydrolase family Elizabethkingia meningoseptica 2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate
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 ?

Subunits

Subunits Comment Organism
tetramer alpha2 + beta2 Elizabethkingia meningoseptica