| Entry |
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| Name |
S-ribosylhomocysteine lyase;
S-ribosylhomocysteinase;
LuxS
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| Class |
Lyases;
Carbon-sulfur lyases;
Carbon-sulfur lyases (only sub-subclass identified to date)
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| Sysname |
S-(5-deoxy-D-ribos-5-yl)-L-homocysteine L-homocysteine-lyase [(4S)-4,5-dihydroxypentan-2,3-dione-forming]
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| Reaction(IUBMB) |
S-(5-deoxy-D-ribos-5-yl)-L-homocysteine = L-homocysteine + (4S)-4,5-dihydroxypentan-2,3-dione [RN: R01291]
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| Reaction(KEGG) |
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| Substrate |
S-(5-deoxy-D-ribos-5-yl)-L-homocysteine [CPD: C03539]
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| Product |
L-homocysteine [CPD: C00155];
(4S)-4,5-dihydroxypentane-2,3-dione [CPD: C11838]
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| Comment |
Contains Fe2+. The 4,5-dihydroxypentan-2,3-dione formed spontaneously cyclizes and combines with borate to form an autoinducer (AI-2) in the bacterial quorum-sensing mechanism, which is used by many bacteria to control gene expression in response to cell density [2].
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| History |
EC 4.4.1.21 created 2004
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| Pathway |
| ec00270 | Cysteine and methionine metabolism |
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| Orthology |
| K07173 | S-ribosylhomocysteine lyase |
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| Genes |
» show all
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| Reference |
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| Authors |
Zhu J, Dizin E, Hu X, Wavreille AS, Park J, Pei D. |
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| Title |
S-Ribosylhomocysteinase (LuxS) is a mononuclear iron protein. |
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| Journal |
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| Sequence |
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| Reference |
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| Authors |
Miller MB, Bassler BL. |
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| Title |
Quorum sensing in bacteria. |
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| Journal |
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| Other DBs |
| ExplorEnz - The Enzyme Database: | 4.4.1.21 |
| ExPASy - ENZYME nomenclature database: | 4.4.1.21 |
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