Literature summary for 4.4.1.21 extracted from

Li, H.; Zhao, H.; Zhu, L.; Hong, L.; Zhang, H.; Lin, F.; Xu, C.; Li, S.; Zhang, Z.
Crystallization and preliminary X-ray analysis of S-ribosylhomocysteinase from Streptococcus mutans (2012), Acta Crystallogr. Sect. F, 68, 199-202.

Search for more literature for 4.4.1.21

Cloned(Commentary)

Cloned (Comment)	Organism
gene luxS, soluble expression of GST-tagged enzyme in Escherichia coli strain BL21(DE3)	Streptococcus mutans

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified recombinant enzyme, hanging-drop vapour-diffusion method, mixing of 0.001 ml of 10 mg/ml protein in 10 mM Tris-HCl pH 8.0, 100 mM NaCl, 1 mM DTT, with 0.001 ml of reservoir solution containing 0.1 M Tris-HCl pH 8.0, 20% w/v PEG 3350, and equilibartion against 0.2 ml of reservoir solution, 18°C, X-ray diffraction structure determination and analysis at 2.4 A resolution	Streptococcus mutans

Organism

Organism	UniProt	Comment	Textmining
Streptococcus mutans	-	gene luxS	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant soluble GST-tagged enzyme from Escherichia coli strain BL21(DE3) by glutathione affinity chromatography, desalting gel filtration, ultrafiltration, anion exchange chromatography, and gel filtration	Streptococcus mutans

Synonyms

Synonyms	Comment	Organism
LuxS	-	Streptococcus mutans
S-ribosylhomocysteinase	-	Streptococcus mutans

General Information

General Information	Comment	Organism
physiological function	S-ribosylhomocysteinase from Streptococcus mutans plays a crucial role in the quorum-sensing system	Streptococcus mutans

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Release 2023.1 (January 2023)