The Enzyme Database

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EC 4.1.2.53     
Accepted name: 2-keto-3-deoxy-L-rhamnonate aldolase
Reaction: 2-dehydro-3-deoxy-L-rhamnonate = pyruvate + (S)-lactaldehyde
For diagram of L-Rhamnose metabolism, click here
Glossary: 2-dehydro-3-deoxy-L-rhamnonate = 3,6-dideoxy-L-erythro-hex-2-ulosonate
Other name(s): KDR aldolase; 2-dehydro-3-deoxyrhamnonate aldolase; 2-keto-3-deoxy acid sugar aldolase; YfaU; 2-dehydro-3-deoxy-L-rhamnonate (S)-lactaldehyde lyase (pyruvate-forming); 2-dehydro-3-deoxy-L-rhamnonate (R)-lactaldehyde lyase (pyruvate-forming)
Systematic name: 2-dehydro-3-deoxy-L-rhamnonate (S)-lactaldehyde-lyase (pyruvate-forming)
Comments: Requires Mg2+ for activity. The enzyme can also use 2-oxo-3-deoxy-L-mannonate, 2-oxo-3-deoxy-L-lyxonate and 4-hydroxy-2-ketoheptane-1,7-dioate (HKHD) as substrates [2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Rakus, J.F., Fedorov, A.A., Fedorov, E.V., Glasner, M.E., Hubbard, B.K., Delli, J.D., Babbitt, P.C., Almo, S.C. and Gerlt, J.A. Evolution of enzymatic activities in the enolase superfamily: L-rhamnonate dehydratase. Biochemistry 47 (2008) 9944–9954. [DOI] [PMID: 18754693]
2.  Rea, D., Hovington, R., Rakus, J.F., Gerlt, J.A., Fulop, V., Bugg, T.D. and Roper, D.I. Crystal structure and functional assignment of YfaU, a metal ion dependent class II aldolase from Escherichia coli K12. Biochemistry 47 (2008) 9955–9965. [DOI] [PMID: 18754683]
[EC 4.1.2.53 created 2013]
 
 
EC 4.2.1.176     
Accepted name: L-lyxonate dehydratase
Reaction: L-lyxonate = 2-dehydro-3-deoxy-L-arabinonate + H2O
Glossary: L-lyxonate = (2R,3R,4S)-2,3,4,5-tetrahydroxypentanoate
Other name(s): lyxD (gene name)
Systematic name: L-lyxonate hydro-lyase
Comments: The enzyme, characterized from several bacterial species, is involved in an L-lyxonate degradation pathway.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Ghasempur, S., Eswaramoorthy, S., Hillerich, B.S., Seidel, R.D., Swaminathan, S., Almo, S.C. and Gerlt, J.A. Discovery of a novel L-lyxonate degradation pathway in Pseudomonas aeruginosa PAO1. Biochemistry 53 (2014) 3357–3366. [DOI] [PMID: 24831290]
[EC 4.2.1.176 created 2021]
 
 


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