EzCatDB

R L C P
Hierarchic Classification of Catalytic Mechanisms


R 9.-.-.- : Hydride transfer (Reaction)

L 9.5010.-.- : From nicotinamide (NADH/NADPH) to C=O (Ligand group involved)

C 9.5010.536200.- : dTDP dehydrorhamnose reductase-like mechanism (Acid/Modulator); Modulation of adjacent atom to hydride acceptor; Modulator/NAD-assisted acid protonation of adjacent atom to hydride acceptor; Hydride transfer (Catalytic mechanism)

P 9.5010.536200.8010 : Tyr/Ser + Lys bound to ribose-nicotinamide (Residues/cofactors in Protein)


1st Nucleophile : non-existent
Catalytic groups : cofactor + groups in residue/substrate
General Base : a group in substrate/cofactor
General Acid : a group in substrate/cofactor

Related Enzymes

There are 24 entries in this class.
  • S00319 : 1.1.1.1; Alcohol dehydrogenase (Catalytic domain; 3.40.50.720)
  • S00320 : 1.1.1.304; Acetoin(diacetyl) reductase (Catalytic domain; 3.40.50.720)
  • S00324 : 1.1.1.47; Glucose 1-dehydrogenase (Catalytic domain; 3.40.50.720)
  • S00325 : 1.1.1.50, 1.1.1.184; 3-alpha-hydroxysteroid dehydrogenase (Catalytic domain; 3.40.50.720)
  • S00326 : 1.1.1.53; 3-alpha-(or 20-beta)-hydroxysteroid dehydrogenase (Catalytic domain; 3.40.50.720)
  • S00327 : 1.1.1.62; Estradiol 17-beta-dehydrogenase 1 (Catalytic domain; 3.40.50.720)
  • S00328 : 1.1.1.100; 3-oxoacyl-[acyl-carrier-protein] reductase (Catalytic domain; 3.40.50.720)
  • S00329 : (reaction 1) 1.1.1.153; Sepiapterin reductase (Catalytic domain; 3.40.50.720)
  • S00329 : (reaction 3) 1.1.1.153; Sepiapterin reductase (Catalytic domain; 3.40.50.720)
  • S00331 : 1.1.1.184; Sniffer (Catalytic domain; 3.40.50.720)
  • S00332 : 1.1.1.236; Tropinone reductase 2 (Catalytic domain; 3.40.50.720)
  • S00336 : (reaction 2) 1.1.1.252; Tetrahydroxynaphthalene reductase (Catalytic domain; 3.40.50.720)
  • S00543 : 1.1.1.184, 1.1.1.189, 1.1.1.197; Carbonyl reductase [NADPH] 1 (Catalytic domain; 3.40.50.720)
  • S00552 : 1.1.1.206; Tropinone reductase 1 (Catalytic domain; 3.40.50.720)
  • S00553 : 1.1.1.100; 3-oxoacyl-[acyl carrier protein] reductase (Catalytic domain; 3.40.50.720)
  • S00602 : 1.1.1.10; L-xylulose reductase (Catalytic domain; 3.40.50.720)
  • S00604 : 1.1.1.138; NADP-dependent mannitol dehydrogenase (Catalytic domain; 3.40.50.720)
  • S00605 : 1.1.1.14; Sorbitol dehydrogenase (Catalytic domain; 3.40.50.720)
  • S00608 : 1.1.1.268; 2-(R)-hydroxypropyl-CoM dehydrogenase (Catalytic domain; 3.40.50.720)
  • S00610 : 1.1.1.51; 3-beta-hydroxysteroid dehydrogenase (Catalytic domain; 3.40.50.720)
  • D00274 : (reaction 2) 5.1.3.2; UDP-glucose 4-epimerase (Catalytic domain; 3.40.50.720)
  • D00275 : (reaction 1) 5.1.3.20; ADP-L-glycero-D-manno-heptose-6-epimerase (Catalytic domains; 3.40.50.720, 3.90.25.10)
  • D00545 : 1.1.1.100; 3-oxoacyl-(Acyl-carrier protein) reductase (Catalytic domain; 3.40.50.720)
  • D00604 : (reaction 5) 1.1.1.271; GDP-L-fucose synthetase (Catalytic domains; 3.40.50.720, 3.90.25.10)
  • 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 -)