EC Number   |
General Information |
Reference |
|---|
   3.2.1.139 | evolution |
the enzyme is a member of the family GH 115 |
731265 |
| 3.2.1.139 | evolution |
the enzyme is a member of the glycoside hydrolase family 115, GH115 |
732167 |
| 3.2.1.139 | evolution |
the enzyme is classified in family 67 of the glycosyl hydrolases |
-, 731869 |
| 3.2.1.139 | metabolism |
the enzyme acts in synergy with endoxylanases and other xylanolytic enzymes in the biodegradation of xylan |
-, 731869 |
| 3.2.1.139 | more |
the crystal structure of BoAgu115A reveals a four-domain protein in which the active site, comprising a pocket that abuts a cleft-like structure, is housed in the second domain that adopts a TIM barrel-fold. The third domain, a five-helical bundle, and the C-terminal beta-sandwich domain make inter-chain contacts leading to protein dimerization, topology of the xylan binding cleft of the enzyme. Active site structure, overview. Residue Arg328 may contribute to substrate binding by also interacting with the carboxylate of the glucuronic acid substrate, residue His422 is a component of the catalytic apparatus |
732167 |
| 3.2.1.139 | more |
the enzyme binds strongly to cellulose, thus it likely possesses a carbohydrate binding module |
-, 731869 |
| 3.2.1.139 | more |
the enzyme protein sequence contains two highly conserved amino acids, D43 and E462, that are implicated as critical catalytic residues |
732277 |
| 3.2.1.139 | physiological function |
alpha-glucuronidase enzymes play an essential role in the full enzymatic hydrolysis of hemicellulose |
732877 |
| 3.2.1.139 | physiological function |
expression in Arabidopsis thaliana and targeting to apoplast. The enzyme is active on the internally substituted aldopentaouronic acid. The transgenic plants do not show any change in growth or in lignocellulose saccharification. The cell wall (Me)GlcA and other non-cellulosic sugars, as well as the lignin content, remain unchanged. The cell wall-targeted AGU115 affects those glucuronate substitutions of xylan, which are accessible to UX1 antibody and constitute a small fraction in Arabidopsis, whereas majority of (Me)GlcA substitutions are resistant, most likely due to the shielding by acetyl groups. Plants expressing AGU115 do not show any defects under laboratory conditions indicating that the glucoronoxylan epitope of xylan is not essential under these conditions |
737933 |
| 3.2.1.139 | physiological function |
the enzyme catalyzes removal of 4-O-methylglucuronate residues alpha-1,2 linked to internal xylose residues in oligoxylosides generated by GH11 and GH30 xylanases and releases methylglucuronate from polymeric methylglucuronoxylan |
737522 |
