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CATH domain | Related DB codes (homologues) |
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2.60.120.260 : Jelly Rolls | M00124,T00005,T00065 | 2.60.40.320 : Immunoglobulin-like | M00026 | 3.20.20.80 : TIM Barrel | S00202,S00210,S00748,S00906,S00907,S00911,S00912,S00915,M00134,M00160,D00479,S00204,S00205,S00206,S00207,S00203,S00208,S00209,S00211,S00213,S00214,M00113,T00307,D00165,D00166,D00169,D00176,D00501,D00502,D00503,D00844,D00861,D00864,M00026,M00112,M00193,M00346,T00057,T00062,T00063,T00067 |
KEGG pathways | MAP code | Pathways |
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MAP00040 | Pentose and glucuronate interconversions | MAP00500 | Starch and sucrose metabolism | MAP00531 | Glycosaminoglycan degradation | MAP00860 | Porphyrin and chlorophyll metabolism | MAP00944 | Flavone and flavonol biosynthesis | MAP00983 | Drug metabolism - other enzymes | MAP01032 | Glycan structures - degradation |
UniProtKB:Accession Number | P08236 |
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Entry name | BGLR_HUMAN |
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Activity | A beta-D-glucuronoside + H(2)O = D-glucuronate + an alcohol. |
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Subunit | Homotetramer. |
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Subcellular location | Lysosome. |
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Cofactor |
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References for Catalytic Mechanism | References | Sections | No. of steps in catalysis |
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[4] | p.379 |
| [5] | FIG.1, p.34058 |
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references | [1] |
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PubMed ID | 5063464 |
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Journal | J Biol Chem |
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Year | 1972 |
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Volume | 247 |
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Pages | 2644-9 |
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Authors | Wang CC, Touster O |
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Title | Studies of catalysis by -glucuronidase. Active site. |
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[2] |
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PubMed ID | 2467874 |
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Journal | Indian J Biochem Biophys |
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Year | 1988 |
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Volume | 25 |
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Pages | 319-25 |
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Authors | Gupta GS, Singh G |
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Title | Catalytic properties and immunoprecipitation of beta-glucuronidase in presence of its IgG and Fab fragments: identification of antigenic domains. |
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[3] |
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PubMed ID | 8377186 |
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Journal | J Mol Biol |
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Year | 1993 |
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Volume | 233 |
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Pages | 173-6 |
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Authors | Drendel WB, Grubb JH, Sly WS, Chen Z, Mathews FS, Jain S |
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Title | Crystallization and preliminary crystallographic studies of human beta-glucuronidase. |
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[4] |
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Comments | X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS). |
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Medline ID | 96185449 |
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PubMed ID | 8599764 |
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Journal | Nat Struct Biol |
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Year | 1996 |
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Volume | 3 |
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Pages | 375-81 |
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Authors | Jain S, Drendel WB, Chen ZW, Mathews FS, Sly WS, Grubb JH |
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Title | Structure of human beta-glucuronidase reveals candidate lysosomal targeting and active-site motifs. |
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Related PDB | 1bhg |
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Related UniProtKB | P08236 |
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[5] |
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PubMed ID | 9852062 |
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Journal | J Biol Chem |
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Year | 1998 |
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Volume | 273 |
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Pages | 34057-62 |
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Authors | Wong AW, He S, Grubb JH, Sly WS, Withers SG |
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Title | Identification of Glu-540 as the catalytic nucleophile of human beta-glucuronidase using electrospray mass spectrometry. |
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[6] |
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PubMed ID | 10366443 |
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Journal | Genomics |
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Year | 1999 |
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Volume | 58 |
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Pages | 121-8 |
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Authors | Fyfe JC, Kurzhals RL, Lassaline ME, Henthorn PS, Alur PR, Wang P, Wolfe JH, Giger U, Haskins ME, Patterson DF, Sun H, Jain S, Yuhki N |
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Title | Molecular basis of feline beta-glucuronidase deficiency: an animal model of mucopolysaccharidosis VII. |
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[7] |
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PubMed ID | 10438523 |
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Journal | J Biol Chem |
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Year | 1999 |
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Volume | 274 |
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Pages | 23451-5 |
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Authors | Islam MR, Tomatsu S, Shah GN, Grubb JH, Jain S, Sly WS |
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Title | Active site residues of human beta-glucuronidase. Evidence for Glu(540) as the nucleophile and Glu(451) as the acid-base residue. |
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[8] |
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PubMed ID | 11124909 |
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Journal | J Mol Biol |
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Year | 2001 |
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Volume | 305 |
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Pages | 331-9 |
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Authors | Matsumura I, Ellington AD |
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Title | In vitro evolution of beta-glucuronidase into a beta-galactosidase proceeds through non-specific intermediates. |
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[9] |
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PubMed ID | 11786015 |
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Journal | J Mol Biol |
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Year | 2002 |
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Volume | 315 |
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Pages | 325-37 |
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Authors | Flores H, Ellington AD |
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Title | Increasing the thermal stability of an oligomeric protein, beta-glucuronidase. |
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[10] |
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PubMed ID | 15069062 |
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Journal | J Biol Chem |
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Year | 2004 |
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Volume | 279 |
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Pages | 26462-8 |
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Authors | Geddie ML, Matsumura I |
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Title | Rapid evolution of beta-glucuronidase specificity by saturation mutagenesis of an active site loop. |
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comments | This family belongs to glycosidase family-2, which has an retaining mechanism (equatorial to equatorial conformation), and also a member of 4/7 superfamily, which has got catalytic residues at the C-terminal ends of beta-4 and beta-7 on the (alpha/beta)8 barrel fold. According to the literature [4] & [5], Glu451 may act as a general acid, whilst Glu540 acts as a nucleophile. This enzyme must adopt a similar mechanism to that of the other 4/7 superfamily members. Moreover, comparing the structural data with that of xylanase (E.C. 3.2.1.8) (D00479 in EzCatDB), Tyr504 might stabilize the leaving nucleophile, Glu540, in deglycosylation. On the other hand, Tyr504 might modulate the activity of the nucleophile, according to the data of the other homologous enzyme, beta-glucosidase (E.C. 3.2.1.21) (S00205 in EzCatDB).
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created | updated |
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2005-04-02 | 2009-02-26 |
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