Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
twitter

MetaCyc Enzyme: S-ribosylhomocysteine lyase

Gene: luxS Accession Number: G-11132 (MetaCyc)

Species: Vibrio harveyi

Subunit composition of S-ribosylhomocysteine lyase = [LuxS]2
         S-ribosylhomocysteine lyase monomer = LuxS

Summary:
S-ribosylhomocysteine lyase (LuxS) is a small metalloenzyme with Fe2+ ion at its active site [Zhu03b]. LuxS was shown to exist as a homodimer in its biologically active form, with two identical active sites being formed at the dimer interface [Lewis01]. LuxS is unique in its ability to catalyze a non-redox cleavage of a stable thioether bond without the need for any redox-active cofactor [Pei04].

The luxS gene of Vibrio harveyi was cloned by its ability to confer AI-2 production on Escherichia coli K-12 strain DH5α, which contains a defective version of the gene [Surette99]. Inactivation of the gene in the Vibrio harveyi chromosome eliminated the ability to produce AI-2 [Surette99].

Molecular Weight of Polypeptide: 15.569 kD (from nucleotide sequence)

Unification Links: UniProt:B0LUE4

Relationship Links: Entrez-Nucleotide:PART-OF:EU373093 , InterPro:IN-FAMILY:IPR003815 , InterPro:IN-FAMILY:IPR011249 , Pfam:IN-FAMILY:PF02664 , Prints:IN-FAMILY:PR01487 , ProDom:IN-FAMILY:PD013172

Gene-Reaction Schematic: ?

Credits:
Created 10-Mar-2009 by Caspi R , SRI International


Enzymatic reaction of: S-ribosylhomocysteine lyase

EC Number: 4.4.1.21

S-ribosyl-L-homocysteine <=> L-homocysteine + (S)-4,5-dihydroxypentan-2,3-dione

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.

In Pathways: autoinducer AI-2 biosynthesis II (Vibrio)

Cofactors or Prosthetic Groups: Fe2+


References

Lewis01: Lewis HA, Furlong EB, Laubert B, Eroshkina GA, Batiyenko Y, Adams JM, Bergseid MG, Marsh CD, Peat TS, Sanderson WE, Sauder JM, Buchanan SG (2001). "A structural genomics approach to the study of quorum sensing: crystal structures of three LuxS orthologs." Structure 9(6);527-37. PMID: 11435117

Pei04: Pei D, Zhu J (2004). "Mechanism of action of S-ribosylhomocysteinase (LuxS)." Curr Opin Chem Biol 8(5);492-7. PMID: 15450491

Surette99: Surette MG, Miller MB, Bassler BL (1999). "Quorum sensing in Escherichia coli, Salmonella typhimurium, and Vibrio harveyi: a new family of genes responsible for autoinducer production." Proc Natl Acad Sci U S A 96(4);1639-44. PMID: 9990077

Zhu03b: Zhu J, Dizin E, Hu X, Wavreille AS, Park J, Pei D (2003). "S-Ribosylhomocysteinase (LuxS) is a mononuclear iron protein." Biochemistry 42(16);4717-26. PMID: 12705835


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Mon Dec 22, 2014, biocyc11.