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Literature summary for 3.2.1.166 extracted from

  • Bohlmann, L.; Tredwell, G.D.; Yu, X.; Chang, C.W.; Haselhorst, T.; Winger, M.; Dyason, J.C.; Thomson, R.J.; Tiralongo, J.; Beacham, I.R.; Blanchard, H.; von Itzstein, M.
    Functional and structural characterization of a heparanase (2015), Nat. Chem. Biol., 11, 955-957 .
    View publication on PubMed
Search for more literature for 3.2.1.166

Application

Application Comment Organism
drug development overexpression of hepaxadranase in cancers is well known and is associated with angiogenesis, inflammation and increased metastatic potential, making this enzyme a promising drug target Burkholderia pseudomallei

Crystallization (Commentary)

Crystallization (Comment) Organism
wild-type enzyme BpHep, X-ray diffraction structure determination and analysis at 1.60 A resolution, PDB ID 5BWI Burkholderia pseudomallei

Protein Variants

Protein Variants Comment Organism
E144A site-directed mutagenesis, conserved active site residue mutant Burkholderia pseudomallei
E255A site-directed mutagenesis, conserved active site residue mutant Burkholderia pseudomallei

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
heparan sulfate + H2O Burkholderia pseudomallei
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 ?
-
 ?

Organism

Organism UniProt Comment Textmining
Burkholderia pseudomallei
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-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
heparan sulfate + H2O
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 Burkholderia pseudomallei ?
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 ?
heparan sulfate + H2O enzyme BpHep is specific for heparan sulfate Burkholderia pseudomallei ?
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 ?
additional information activity assays using fluorescein isothiocyanate (FITC)-labeled glycosaminoglycans. NMR spectroscopic study of enzyme cleavage site specificity, overview Burkholderia pseudomallei ?
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 ?

Subunits

Subunits Comment Organism
More wild-type enzyme BpHep comprises two funcxadtional domains: a catalytic domain consisting of an (alpha/beta)8 barrel and a beta-sandwich C-terminal domain. In the catalytic domain of BpHepwt, amino acid residues Glu144 and Glu255, with commenxadsurate residues highly conserved in hHep, are the catalytic residues, with Glu144 acting as a proton donor and Glu255 as a nucleoxadphile. A canyon-like cleft made up of several polar and nonpolar residue forms a putative binding site. Three-dimensional structure analysis, overview Burkholderia pseudomallei

Synonyms

Synonyms Comment Organism
BpHep
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 Burkholderia pseudomallei
endo-beta-glucuronidase
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 Burkholderia pseudomallei

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
40
-
-
 Burkholderia pseudomallei

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
4.5
-
-
 Burkholderia pseudomallei

pH Range

pH Minimum pH Maximum Comment Organism
2.5 6.5 activity range, profile overview Burkholderia pseudomallei

General Information

General Information Comment Organism
evolution the enzyme belongs to the glycoxadside hydrolase family 79, GH79, from GH clan A Burkholderia pseudomallei
additional information NMR study of the endo cleavage mechanism of the heparanase, overview. Conserved active site regions, including a His-His-Tyr sequence. The BpHep residues Glu144 and Glu255 are predicted to be located at similar positions postulated for BhHep and are within loops between the beta-strands and alpha-helices, which is typical of TIM-barrel glycoside hydrolases, comparison to the human enzyme Burkholderia pseudomallei
physiological function the enzyme degrades heparan sulfate (HS), a glycosaminoglycan (GAG), by hydrolysis of the beta-1,4-glycosidic linkage between glucuronic acid (GlcUA, G) and alpha-D-glucosamine (GlcN, N) residues. The overexpression of heparanase in cancers is well known and is associated with angiogenesis, inflammation and increased metastatic potential Burkholderia pseudomallei