Literature summary for 2.4.2.29 extracted from

Ritschel, T.; Atmanene, C.; Reuter, K.; Van Dorsselaer, A.; Sanglier-Cianferani, S.; Klebe, G.
An integrative approach combining noncovalent mass spectrometry, enzyme kinetics and X-ray crystallography to decipher Tgt protein-protein and protein-RNA interaction (2009), J. Mol. Biol., 393, 833-847.

Search for more literature for 2.4.2.29

Cloned(Commentary)

Cloned (Comment)	Organism
mutants introduced into plasmid pET9d-ZM4 and transformed into Escherichia coli BL21(DE3) GOLD cells	Zymomonas mobilis

Crystallization (Commentary)

Crystallization (Comment)	Organism
mutant K52M, by hanging-drop, vapor-diffusion method and followed by macroseeding, at a resolution of 2.0 A, forms crystals under the same conditions as wild-type, while all attempts to obtain diffracting crystals from mutant Y330F are unsuccessful. Compared to wild-type, crystals of mutant K52M are very fragile and show only a limited diffraction quality	Zymomonas mobilis

Protein Variants

Protein Variants	Comment	Organism
K52M	reduced turnover value. At a concentration of protein of 0.01 mM appears almost exclusively as a homodimer as the wild-type, when the concentration of protein is lowered to a minimal value of 0.001 mM, a substantial proportion of monomer becomes evident	Zymomonas mobilis
Y330F	reduced turnover value. At a concentration of protein of 0.01 mM reveals a significant amount of monomer, when the concentration of protein is lowered to a minimal value of 0.001 mM, a substantial proportion of monomer becomes evident	Zymomonas mobilis

Inhibitors

Inhibitors	Comment	Organism	Structure
6-amino-2-[(3-piperidin-1-ylpropyl)amino]-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one	cannot modify the structure of the dimer interface, prevents the formation of the catalytically active Tgt:tRNA complex, and can disrupt the preformed complex	Zymomonas mobilis
6-amino-4-[2-(4-methoxyphenyl)ethyl]-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one	can modify the structure of the dimer interface, prevents the formation of the catalytically active Tgt:tRNA complex, and can disrupt the preformed complex	Zymomonas mobilis
6-amino-4-[2-(benzylamino)ethyl]-2-(methylamino)-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one	addresses a hydrophobic subpocket close to the dimer interface that may affect quarternary structure formation, prevents the formation of the catalytically active Tgt:tRNA complex, and can disrupt the preformed complex	Zymomonas mobilis
6-amino-4-[2-[(cyclohexylmethyl)amino]ethyl]-2-(methylamino)-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one	can modify the structure of the dimer interface, prevents the formation of the catalytically active Tgt:tRNA complex, and can disrupt the preformed complex	Zymomonas mobilis
6-amino-4-[2-[(cyclopentylmethyl)amino]ethyl]-2-(methylamino)-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one	addresses a hydrophobic subpocket close to the dimer interface that may affect quarternary structure formation, prevents the formation of the catalytically active Tgt:tRNA complex, and can disrupt the preformed complex	Zymomonas mobilis

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.00098	-	[tRNATyr]7-aminomethyl-7-carbaguanine	mutant K52M	Zymomonas mobilis
0.00158	-	[tRNATyr]7-aminomethyl-7-carbaguanine	mutant Y330F	Zymomonas mobilis
0.00217	-	[tRNATyr]7-aminomethyl-7-carbaguanine	wild-type	Zymomonas mobilis

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Zn2+	one structural Zn2+ per subunit	Zymomonas mobilis

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
85600	-	expected for a Tgt dimer containing one structural Zn2+ per subunit	Zymomonas mobilis
85610	-	Tgt, noncovalent mass spectrometry	Zymomonas mobilis
113100	-	Tgt:tRNA complex, noncovalent mass spectrometry	Zymomonas mobilis

Organism

Organism	UniProt	Comment	Textmining
Zymomonas mobilis	P28720	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
[tRNATyr]7-aminomethyl-7-carbaguanine + guanine	Tgt dimer binds specifically to a single tRNA molecule	Zymomonas mobilis	[tRNATyr]-guanine + 7-aminomethyl-7-carbaguanine	-	?

Subunits

Subunits	Comment	Organism
homodimer	noncovalent mass spectrometry, Tgt in solution	Zymomonas mobilis

Synonyms

Synonyms	Comment	Organism
TGT	-	Zymomonas mobilis
tRNA-guanine transglycosylase	-	Zymomonas mobilis

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
0.00023	-	[tRNATyr]7-aminomethyl-7-carbaguanine	mutant K52M	Zymomonas mobilis
0.00095	-	[tRNATyr]7-aminomethyl-7-carbaguanine	mutant Y330F	Zymomonas mobilis
0.011	-	[tRNATyr]7-aminomethyl-7-carbaguanine	wild-type	Zymomonas mobilis

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Release 2023.1 (January 2023)