RLCP 1.30.35885.972 :EzCatDB EzCatDB

R L C P
Hierarchic Classification of Catalytic Mechanisms


R 1.-.-.- : Hydrolysis (bond cleavage by water) (Reaction)

L 1.30.-.- : C-O bond (O-glycoside bond) (Ligand group involved)

C 1.30.35885.- : beta-xylosidase-like mechanism (Nucleophile/Acid-Base/Modulator-Stabilizer/Modulator/Stabilizer); Modulation of nucleophile & acid-base; Acid protonation to leaving group leads to transition-state; Stabilization of transition-state; Nucleophilic attack forms intermediate; Base deprotonation of water; Activated water attacks on intermediate; SN1-like reaction (Catalytic mechanism)

P 1.30.35885.972 : Two acidic residues + Arg/His/Tyr + Asn or Gln (Residues/cofactors in Protein)

1st Nucleophile : a catalytic residue
Catalytic groups : groups in residue/substrate
General Base : a catalytic residue
General Acid : a catalytic residue

Related Enzymes

There are 11 entries in this class.
  • S00203 : 3.2.1.4; Endoglucanase C (Catalytic domain; 3.20.20.80)
  • S00208 : 3.2.1.58; Glucan 1,3-beta-glucosidase (Catalytic domain; 3.20.20.80)
  • S00210 : 3.2.1.78; Mannan endo-1,4-beta-mannosidase 4 (Catalytic domain; 3.20.20.80)
  • S00906 : 3.2.1.78; Beta-mannanase (Catalytic domain; 3.20.20.80)
  • S00907 : 3.2.1.78; Mannan endo-1,4-beta-mannosidase (Catalytic domain; 3.20.20.80)
  • D00501 : 3.2.1.4; Endoglucanase Z (Catalytic domain; 3.20.20.80)
  • D00502 : 3.2.1.4; Endoglucanase E1 (Catalytic domain; 3.20.20.80)
  • D00503 : 3.2.1.4; Endoglucanase A (Catalytic domain; 3.20.20.80)
  • D00861 : 3.2.1.78; Mannanase (Catalytic domain; 3.20.20.80)
  • D00844 : 3.2.1.37; Beta-xylosidase (Catalytic domain; 3.20.20.80)
  • D00864 : 3.2.1.45; Glucosylceramidase (Catalytic domain; 3.20.20.80)
    • Copyright: Nozomi Nagano, JST & CBRC-AIST
    Funded by PRESTO/Japan Science and Technology Agency (JST) (December 2001 - November 2004)
    Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
    Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
    Funded by BIRD/Japan Science and Technology Agency (JST) (September 2005 - September 2008)
    Funded by BIRD/Japan Science and Technology Agency (JST) (October 2007 - September 2010)
    Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)
    Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
    Supported by the commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from the Ministry of Economy, Trade and Industry (METI) (October 2012 - March 2016)
    Funded by the project commissioned by the New Energy and Industrial Technology Development Organization (NEDO) (April 2016 -)