Literature summary for 4.4.1.21 extracted from

Zhu, J.; Dizin, E.; Hu, X.; Wavreille, A.S.; Park, J.; Pei, D.
S-Ribosylhomocysteinase (LuxS) is a mononuclear iron protein (2003), Biochemistry, 42, 4717-4726.

Search for more literature for 4.4.1.21

Cloned(Commentary)

Cloned (Comment)	Organism
-	Bacillus subtilis

Protein Variants

Protein Variants	Comment	Organism
C84A	no catalytic activity	Bacillus subtilis
C84D	more than 220fold reduced activity	Bacillus subtilis
C84S	more than 220fold reduced activity	Bacillus subtilis
E57A	no detectable activity	Bacillus subtilis
E57D	220fold reduced activity	Bacillus subtilis
E57Q	no detectable activity	Bacillus subtilis

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	KM-values of enzyme forms enriched in either Fe2+, Co2+ or Zn2+	Bacillus subtilis
0.0025	-	S-ribosylhomocysteine	native enzyme	Bacillus subtilis
0.18	-	S-ribosylhomocysteine	mutant enzyme E57D	Bacillus subtilis

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Fe2+	contains	Bacillus subtilis
additional information	to gain insight into the catalytic mechanism of the unusual reaction and the function of the metal cofactor, an efficient expression and purification system is developed to produce LuxS enriched in either Fe2+, Co2+ or Zn2+	Bacillus subtilis

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
S-ribosylhomocysteine	Bacillus subtilis	key step in biosynthesis pathway of type II autoinducer AI-2	L-homocysteine + 4,5-dihydroxy-2,3-pentanedione	-	?

Organism

Organism	UniProt	Comment	Textmining
Bacillus subtilis	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Bacillus subtilis

Reaction

Reaction	Comment	Organism	Reaction ID
S-(5-deoxy-D-ribos-5-yl)-L-homocysteine = L-homocysteine + (4S)-4,5-dihydroxypentan-2,3-dione	catalytic mechanism in which the metal ion catalyzes an intramolecular redox reaction, shifting the carbonyl group from the C-1 position to the C-3 position of the ribose. Subsequent beta-elimination at the C-4 and C-5 position releases homocysteine as a free thiol	Bacillus subtilis	a

Storage Stability

Storage Stability	Organism
-80°C, when stored in the frozen form, the LuxS proteins are stable for at least 6 months	Bacillus subtilis

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
S-ribosylhomocysteine	-	Bacillus subtilis	L-homocysteine + 4,5-dihydroxy-2,3-pentanedione	-	?
S-ribosylhomocysteine	key step in biosynthesis pathway of type II autoinducer AI-2	Bacillus subtilis	L-homocysteine + 4,5-dihydroxy-2,3-pentanedione	-	?

Synonyms

Synonyms	Comment	Organism
LuxS protein	-	Bacillus subtilis

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
additional information	-	additional information	turnover numbers of enzyme forms enriched in either Fe2+, Co2+ or Zn2+	Bacillus subtilis

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Release 2023.1 (January 2023)