Literature summary for 2.6.1.16 extracted from

Gong, B.; Klein, D.J.; Ferre-Damare, A.R.; Carey, P.R.
The glmS ribozyme tunes the catalytically critical pK(a) of its coenzyme glucosamine-6-phosphate (2011), J. Am. Chem. Soc., 133, 14188-14191.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
crystals are composed of a trans-acting form of the Thermoanaerobacter tengcongensis ribozyme with a single 2'-deoxyribose substitution at the cleavage site, which traps the RNA in the precleavage state. These crystals yield an accurate structure of the RNA to 1.7 A resolution	Caldanaerobacter subterraneus subsp. tengcongensis

Protein Variants

Protein Variants	Comment	Organism
G40A	mutant with exchanged guanine is inactive. The 2.7 A resolution crystal structure of the mutant shows that the RNA is in a conformation nearly identical to that of the wild-type glmS ribozyme. The experimental electron density maps indicate that GlcN6P binds to the G40A mutant in the same location as in the wild-type ribozyme. Raman pH titrations of GlcN6P using crystals of the G40A mutant glmS ribozyme show that the pKa of the amine of the ribozyme-bound GlcN6P differs substantially for the wild-type and G40A mutant ribozymes	Caldanaerobacter subterraneus subsp. tengcongensis

Organism

Organism	UniProt	Comment	Textmining
Caldanaerobacter subterraneus subsp. tengcongensis	-	-	-

Synonyms

Synonyms	Comment	Organism
glmS ribozyme	-	Caldanaerobacter subterraneus subsp. tengcongensis

Cofactor

Cofactor	Comment	Organism	Structure
additional information	glmS ribozyme employs a small-molecule cofactor. Binding of D-glucosamine 6-phosphate (GlcN6P) uncovers the latent self-cleavage activity of the RNA, which adopts a catalytically competent conformation that is nonetheless inactive in the absence of GlcN6P	Caldanaerobacter subterraneus subsp. tengcongensis

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Release 2023.1 (January 2023)