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Literature summary for 3.2.1.180 extracted from

  • Xiong, J.; Xu, D.
    Insights into the catalytic mechanism of unsaturated glucuronyl hydrolase of Bacillus sp. GL1 (2017), J. Phys. Chem. B, 121, 931-941 .
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information free-energy profiles of the catalytic reaction, overview Bacillus sp. GL1

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
beta-D-4-deoxy-DELTA4-GlcAp-(1->3)-beta-D-GalNAc6S + H2O Bacillus sp. GL1
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5-dehydro-4-deoxy-D-glucuronate + N-acetyl-beta-D-galactosamine-6-O-sulfate
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?

Organism

Organism UniProt Comment Textmining
Bacillus sp. GL1
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
beta-D-4-deoxy-DELTA4-GlcAp-(1->3)-beta-D-GalNAc6S + H2O
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Bacillus sp. GL1 5-dehydro-4-deoxy-D-glucuronate + N-acetyl-beta-D-galactosamine-6-O-sulfate
-
?
additional information almost all interactions between the substrate and enzyme are related to the D-glucuronic acid unit, whereas no recognition specificity is observed for the N-acetyl-D-galactosamine unit Bacillus sp. GL1 ?
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?

Synonyms

Synonyms Comment Organism
UGL
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Bacillus sp. GL1
unsaturated glucuronyl hydrolase
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Bacillus sp. GL1

General Information

General Information Comment Organism
evolution the enzyme is a member of the glycoside hydrolase family 88, GH88 Bacillus sp. GL1
additional information glycosaminoglycan degradation mechanism, combined quantum mechanical and molecular mechanical method and simulation, modelling, two pathways, detailed overview. Almost all interactions between the substrate and enzyme are related to the D-glucuronic acid unit, whereas no recognition specificity is observed for the N-acetyl-D-galactosamine unit Bacillus sp. GL1