Literature summary for 2.1.1.228 extracted from

Zhong, W.; Pasunooti, K.K.; Balamkundu, S.; Wong, Y.H.; Nah, Q.; Gadi, V.; Gnanakalai, S.; Chionh, Y.H.; McBee, M.E.; Gopal, P.; Lim, S.H.; Olivier, N.; Buurman, E.T.; Dick, T.; Liu, C.F.; Lescar, J.; Dedon, P.C.
Thienopyrimidinone derivatives that inhibit bacterial tRNA (guanine37-N1)-methyltransferase (TrmD) by restructuring the active site with a tyrosine-flipping mechanism (2019), J. Med. Chem., 62, 7788-7805 .

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Cloned(Commentary)

Cloned (Comment)	Organism
gene trmD, sequence comparisons	Staphylococcus aureus
gene trmD, sequence comparisons	Pseudomonas aeruginosa
gene trmD, sequence comparisons	Mycobacterium tuberculosis

Crystallization (Commentary)

Crystallization (Comment)	Organism
analysis of the crystal structure of apo-enzyme, of enzyme with bound ligand S-adenosyl-L-homocysteine (PDB IDs 5ZHI and 5ZHJ, respectively), and of enzyme with bound inhibitors N-(4-((octylamino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide, N-([4-[(4-aminopiperidin-1-yl)methyl]phenyl]methyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide , and N-(4-((cyclohexyl(ethyl)amino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide, PDB IDs 6JOF, 5ZHK, and 5ZHL, respectively, at resolutions of 1.75-2.76 A. Sitting drop vapor diffusion method, mixing of 0.002 ml of protein solution with 0.001 ml of precipitant solution containing 100 mM Bis-Tris propane, pH 6.5, 20% w/v PEG3350, and 0.1 M ammonium acetate, soaking of crystals with 1-5 mM inhibitor or 5 mM SAH in their respective precipitating solution supplemented with 20% v/v glycerol, X-ray diffraction structure determination and analysis	Mycobacterium tuberculosis
analysis of the crystal structure of enzyme with bound inhibitors N-([4-[(4-aminopiperidin-1-yl)methyl]phenyl]methyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide, N-(4-((diethylamino)methyl)benzyl)-4-oxo-3,4-dihydrothieno-[2,3-d]pyrimidine-5-carboxamide, and N-(4-((octylamino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide, PDB IDs 6JOE, 5ZHM, and 5ZHN, respectively. Hanging drop vapor diffusion method, mixing of equal volumes of 20 mg/m protein and precipitant solution containing 0.1 M Tris-HCl, pH 8.6-8.8, 20% v/v MPD, 20% w/v PEG 1000, and 5% w/v PEG200, and incubation at 20°C, soaking of crystals with 1-5 mM inhibitor in the precipitating solution supplemented with 20% v/v glycerol at 20°C for at least 4 h, X-ray diffraction structure determination and analysis	Pseudomonas aeruginosa

Crystallization (Comment)

Organism

analysis of the crystal structure of apo-enzyme, of enzyme with bound ligand S-adenosyl-L-homocysteine (PDB IDs 5ZHI and 5ZHJ, respectively), and of enzyme with bound inhibitors N-(4-((octylamino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide, N-([4-[(4-aminopiperidin-1-yl)methyl]phenyl]methyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide , and N-(4-((cyclohexyl(ethyl)amino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide, PDB IDs 6JOF, 5ZHK, and 5ZHL, respectively, at resolutions of 1.75-2.76 A. Sitting drop vapor diffusion method, mixing of 0.002 ml of protein solution with 0.001 ml of precipitant solution containing 100 mM Bis-Tris propane, pH 6.5, 20% w/v PEG3350, and 0.1 M ammonium acetate, soaking of crystals with 1-5 mM inhibitor or 5 mM SAH in their respective precipitating solution supplemented with 20% v/v glycerol, X-ray diffraction structure determination and analysis

Mycobacterium tuberculosis

analysis of the crystal structure of enzyme with bound inhibitors N-([4-[(4-aminopiperidin-1-yl)methyl]phenyl]methyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide, N-(4-((diethylamino)methyl)benzyl)-4-oxo-3,4-dihydrothieno-[2,3-d]pyrimidine-5-carboxamide, and N-(4-((octylamino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide, PDB IDs 6JOE, 5ZHM, and 5ZHN, respectively. Hanging drop vapor diffusion method, mixing of equal volumes of 20 mg/m protein and precipitant solution containing 0.1 M Tris-HCl, pH 8.6-8.8, 20% v/v MPD, 20% w/v PEG 1000, and 5% w/v PEG200, and incubation at 20°C, soaking of crystals with 1-5 mM inhibitor in the precipitating solution supplemented with 20% v/v glycerol at 20°C for at least 4 h, X-ray diffraction structure determination and analysis

Pseudomonas aeruginosa

General Stability

General Stability	Organism
stabilization of the enzyme by binding of small molecules, overview	Staphylococcus aureus
stabilization of the enzyme by binding of small molecules, overview	Pseudomonas aeruginosa
stabilization of the enzyme by binding of small molecules, overview	Mycobacterium tuberculosis

Inhibitors

Inhibitors	Comment	Organism
4-((4-azidobenzyl)oxy)-N-(4-((octylamino)methyl)benzyl)thieno-[2,3-d]pyrimidine-5-carboxamide	-	Pseudomonas aeruginosa
4-(hexyloxy)-N-(4-((octylamino)methyl)benzyl)thieno[2,3-d]-pyrimidine-5-carboxamide	-	Pseudomonas aeruginosa
4-methoxy-N-(4-(morpholinomethyl)benzyl)thieno[2,3-d]-pyrimidine-5-carboxamide	-	Pseudomonas aeruginosa
4-oxo-N-(4-((pentylamino)methyl)benzyl)-3,4-dihydrothieno-[2,3-d]pyrimidine-5-carboxamide	-	Pseudomonas aeruginosa
4-oxo-N-(4-(piperidin-1-ylmethyl)benzyl)-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide	-	Pseudomonas aeruginosa
additional information	synthesis of thienopyrimidinone derivatives that inhibit bacterial tRNA (guanine37-N1)-methyltransferase (TrmD) by restructuring the active site with a tyrosine-flipping mechanism, overview. The tyrosine-flipping mechanism is uniquely found in Pseudomonas aeruginosa TrmD and renders the enzyme inaccessible to the cofactor S-adenosyl-L-methionine (SAM) and probably to the substrate tRNA	Mycobacterium tuberculosis
additional information	synthesis of thienopyrimidinone derivatives that inhibit bacterial tRNA (guanine37-N1)-methyltransferase (TrmD) by restructuring the active site with a tyrosine-flipping mechanism, nanomolar potency against TrmD in vitro, overview. This tyrosine-flipping mechanism is uniquely found in Pseudomonas aeruginosa TrmD and renders the enzyme inaccessible to the cofactor S-adenosyl-L-methionine (SAM) and probably to the substrate tRNA. Biochemical structure-activity relationships (SAR) for TrmD inhibitors, the thienopyrimidinone substituent flexibility is critical for potent TrmD inhibition. Analysis of hemolytic activity of the compounds. Effect of side chain length of 15 analogues	Pseudomonas aeruginosa
additional information	synthesis of thienopyrimidinone derivatives that inhibit bacterial tRNA (guanine37-N1)-methyltransferase (TrmD) by restructuring the active site with a tyrosine-flipping mechanism, overview. The tyrosine-flipping mechanism is uniquely found in Pseudomonas aeruginosa TrmD and renders the enzyme inaccessible to the cofactor S-adenosyl-L-methionine (SAM) and probably to the substrate tRNA	Staphylococcus aureus
N-(4-((((3s,5s,7s)-adamantan-1-yl)amino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide	-	Pseudomonas aeruginosa
N-(4-(((2-(2-(2-aminoethoxy)ethoxy)ethyl)amino)methyl)-benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide	-	Pseudomonas aeruginosa
N-(4-(((2-(2-ethoxyethoxy)ethyl)amino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide	-	Pseudomonas aeruginosa
N-(4-(((2-(2-hydroxyethoxy)ethyl)amino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide	-	Pseudomonas aeruginosa
N-(4-(((4-aminobutyl)amino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide dihydrochloride	-	Pseudomonas aeruginosa
N-(4-(((5-(1,5-dihydroxy-4-oxo-1,4-dihydropyridine-2-carboxamido)pentyl)amino) methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide	-	Pseudomonas aeruginosa
N-(4-(((5-aminopentyl)amino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide	-	Pseudomonas aeruginosa
N-(4-(((7-aminohexyl)amino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide	-	Pseudomonas aeruginosa
N-(4-((1,5-dihydroxy-4-oxo-1,4-dihydropyridine-2-carboxamido)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]-pyrimidine-5-carboxamide	-	Pseudomonas aeruginosa
N-(4-((benzyl(ethyl)amino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide	-	Pseudomonas aeruginosa
N-(4-((benzyl(hexyl)amino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide	-	Pseudomonas aeruginosa
N-(4-((benzyl(octyl)amino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide	-	Pseudomonas aeruginosa
N-(4-((benzylamino)methyl)benzyl)-4-(hexyloxy)thieno[2,3-d]-pyrimidine-5-carboxamide	-	Pseudomonas aeruginosa
N-(4-((benzylamino)methyl)benzyl)-4-methoxythieno[2,3-d]-pyrimidine-5-carboxamide	-	Pseudomonas aeruginosa
N-(4-((benzylamino)methyl)benzyl)-4-oxo-3,4-dihydrothieno-[2,3-d]pyrimidine-5-carboxamide	-	Pseudomonas aeruginosa
N-(4-((benzylamino)methyl)benzyl)-4-propoxythieno[2,3-d]-pyrimidine-5-carboxamide	-	Pseudomonas aeruginosa
N-(4-((butylamino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide	-	Pseudomonas aeruginosa
N-(4-((cyclohexyl(ethyl)amino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide	enzyme-bound crystal structure, overview	Mycobacterium tuberculosis
N-(4-((cyclohexyl(ethyl)amino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide	-	Pseudomonas aeruginosa
N-(4-((cyclohexylamino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide	-	Pseudomonas aeruginosa
N-(4-((decylamino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide	-	Pseudomonas aeruginosa
N-(4-((diethylamino)methyl)benzyl)-4-oxo-3,4-dihydrothieno-[2,3-d]pyrimidine-5-carboxamide	enzyme-bound crystal structure, overview	Pseudomonas aeruginosa
N-(4-((dodecylamino)methyl)benzyl)-4-oxo-3,4-dihydrothieno-[2,3-d]pyrimidine-5-carboxamide	-	Pseudomonas aeruginosa
N-(4-((ethyl(octyl)amino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide	-	Pseudomonas aeruginosa
N-(4-((octylamino)methyl)benzyl)-4-moxythieno[2,3-d]-pyrimidine-5-carboxamide	-	Pseudomonas aeruginosa
N-(4-((octylamino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide	enzyme-bound crystal structure, overview	Mycobacterium tuberculosis
N-(4-((octylamino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide	enzyme-bound crystal structure, overview	Pseudomonas aeruginosa
N-(4-((octylamino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide	-	Staphylococcus aureus
N-(4-((octylamino)methyl)benzyl)-4-propoxythieno[2,3-d]-pyrimidine-5-carboxamide	-	Pseudomonas aeruginosa
N-(4-(morpholinomethyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide	-	Pseudomonas aeruginosa
N-(4-(morpholinomethyl)benzyl)-4-propoxythieno[2,3-d]-pyrimidine-5-carboxamide	-	Pseudomonas aeruginosa
N-([4-[(4-aminopiperidin-1-yl)methyl]phenyl]methyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide	the binding of AZ51 does not induce the side chain flip of Tyr111 in MtbTrmD, while the corresponding residue Tyr120 in PaTrmD turned 180° to form stacking interactions with the phenyl ring of the inhibitor, enzyme-bound crystal structure, overview	Mycobacterium tuberculosis
N-([4-[(4-aminopiperidin-1-yl)methyl]phenyl]methyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide	i.e. AZ51, inhibitor binding induces conformational changes of the wall loop, whereupon the side chain of aromatic ring of Tyr120 flips about 180° and forms stacking interactions with both the phenyl and piperidine rings of AZ51. This feature appears unique to AZ51 and P	Pseudomonas aeruginosa
N-([4-[(4-aminopiperidin-1-yl)methyl]phenyl]methyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide	-	Staphylococcus aureus

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism
additional information	-	additional information	binding kinetics of TrmD ligands	Staphylococcus aureus
additional information	-	additional information	binding kinetics of TrmD ligands	Pseudomonas aeruginosa
additional information	-	additional information	binding kinetics of TrmD ligands	Mycobacterium tuberculosis

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	required	Pseudomonas aeruginosa
Mg2+	required	Mycobacterium tuberculosis

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.
S-adenosyl-L-methionine + guanine37 in tRNA	Staphylococcus aureus	-	S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA	-	?
S-adenosyl-L-methionine + guanine37 in tRNA	Pseudomonas aeruginosa	-	S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA	-	?
S-adenosyl-L-methionine + guanine37 in tRNA	Mycobacterium tuberculosis	-	S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA	-	?

Organism

Organism	UniProt	Comment	Textmining
Mycobacterium tuberculosis	-	-	-
Pseudomonas aeruginosa	-	-	-
Staphylococcus aureus	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
S-adenosyl-L-methionine + guanine37 in tRNA	-	Staphylococcus aureus	S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA	-	?
S-adenosyl-L-methionine + guanine37 in tRNA	-	Pseudomonas aeruginosa	S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA	-	?
S-adenosyl-L-methionine + guanine37 in tRNA	-	Mycobacterium tuberculosis	S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA	-	?

Synonyms

Synonyms	Comment	Organism
bacterial tRNA (guanine37-N1)-methyltransferase	-	Staphylococcus aureus
bacterial tRNA (guanine37-N1)-methyltransferase	-	Pseudomonas aeruginosa
bacterial tRNA (guanine37-N1)-methyltransferase	-	Mycobacterium tuberculosis
MtbTrmD	-	Mycobacterium tuberculosis
PaTrmD	-	Pseudomonas aeruginosa
SaTrmD	-	Staphylococcus aureus
TrmD	-	Staphylococcus aureus
TrmD	-	Pseudomonas aeruginosa
TrmD	-	Mycobacterium tuberculosis
tRNA (guanine37-N1)-methyltransferase	-	Staphylococcus aureus
tRNA (guanine37-N1)-methyltransferase	-	Pseudomonas aeruginosa
tRNA (guanine37-N1)-methyltransferase	-	Mycobacterium tuberculosis

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
37	-	assay at	Pseudomonas aeruginosa

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
8	-	assay at	Pseudomonas aeruginosa

Cofactor

Cofactor	Comment	Organism
S-adenosyl-L-methionine	-	Staphylococcus aureus
S-adenosyl-L-methionine	-	Pseudomonas aeruginosa
S-adenosyl-L-methionine	-	Mycobacterium tuberculosis

IC50 Value

IC50 Value	IC50 Value Maximum	Comment	Organism	Inhibitor
0.000024	-	pH 8.0, 37°C	Pseudomonas aeruginosa	N-(4-((octylamino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
0.000025	-	pH 8.0, 37°C	Pseudomonas aeruginosa	N-(4-((decylamino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
0.00008	-	pH 8.0, 37°C	Pseudomonas aeruginosa	N-(4-(((4-aminobutyl)amino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide dihydrochloride
0.000085	-	pH 8.0, 37°C	Pseudomonas aeruginosa	4-oxo-N-(4-((pentylamino)methyl)benzyl)-3,4-dihydrothieno-[2,3-d]pyrimidine-5-carboxamide
0.00011	-	pH 8.0, 37°C	Pseudomonas aeruginosa	N-(4-(((2-(2-hydroxyethoxy)ethyl)amino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
0.00011	-	pH 8.0, 37°C	Pseudomonas aeruginosa	N-(4-(((5-aminopentyl)amino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
0.00013	-	pH 8.0, 37°C	Pseudomonas aeruginosa	N-(4-((benzylamino)methyl)benzyl)-4-oxo-3,4-dihydrothieno-[2,3-d]pyrimidine-5-carboxamide
0.00014	-	pH 8.0, 37°C	Pseudomonas aeruginosa	N-(4-(((7-aminohexyl)amino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
0.00015	-	pH 8.0, 37°C	Pseudomonas aeruginosa	N-(4-((butylamino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
0.00018	-	pH 8.0, 37°C	Pseudomonas aeruginosa	N-([4-[(4-aminopiperidin-1-yl)methyl]phenyl]methyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
0.00021	-	pH 8.0, 37°C	Pseudomonas aeruginosa	N-(4-(((2-(2-ethoxyethoxy)ethyl)amino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
0.00037	-	pH 8.0, 37°C	Pseudomonas aeruginosa	N-(4-((ethyl(octyl)amino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
0.00038	-	pH 8.0, 37°C	Pseudomonas aeruginosa	N-(4-((dodecylamino)methyl)benzyl)-4-oxo-3,4-dihydrothieno-[2,3-d]pyrimidine-5-carboxamide
0.00045	-	pH 8.0, 37°C	Pseudomonas aeruginosa	N-(4-(((2-(2-(2-aminoethoxy)ethoxy)ethyl)amino)methyl)-benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
0.00049	-	pH 8.0, 37°C	Pseudomonas aeruginosa	N-(4-((cyclohexyl(ethyl)amino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
0.0007	-	pH 8.0, 37°C	Pseudomonas aeruginosa	N-(4-((1,5-dihydroxy-4-oxo-1,4-dihydropyridine-2-carboxamido)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]-pyrimidine-5-carboxamide
0.00072	-	pH 8.0, 37°C	Pseudomonas aeruginosa	N-(4-((((3s,5s,7s)-adamantan-1-yl)amino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
0.00073	-	pH 8.0, 37°C	Pseudomonas aeruginosa	N-(4-((diethylamino)methyl)benzyl)-4-oxo-3,4-dihydrothieno-[2,3-d]pyrimidine-5-carboxamide
0.00079	-	pH 8.0, 37°C	Pseudomonas aeruginosa	N-(4-((cyclohexylamino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
0.0011	-	pH 8.0, 37°C	Pseudomonas aeruginosa	4-oxo-N-(4-(piperidin-1-ylmethyl)benzyl)-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
0.0013	-	pH 8.0, 37°C	Pseudomonas aeruginosa	N-(4-(((5-(1,5-dihydroxy-4-oxo-1,4-dihydropyridine-2-carboxamido)pentyl)amino) methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
0.0018	-	pH 8.0, 37°C	Pseudomonas aeruginosa	4-((4-azidobenzyl)oxy)-N-(4-((octylamino)methyl)benzyl)thieno-[2,3-d]pyrimidine-5-carboxamide
0.0022	-	pH 8.0, 37°C	Pseudomonas aeruginosa	N-(4-((benzyl(ethyl)amino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
0.0022	-	pH 8.0, 37°C	Pseudomonas aeruginosa	N-(4-((benzyl(hexyl)amino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
0.003	-	pH 8.0, 37°C	Pseudomonas aeruginosa	N-(4-(morpholinomethyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
0.012	-	pH 8.0, 37°C	Pseudomonas aeruginosa	N-(4-((benzyl(octyl)amino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide

General Information

General Information	Comment	Organism
physiological function	bacterial tRNA (guanine37-N1)-methyltransferase (TrmD) catalyzes methyl transfer from S-adenosyl-L-methionine (SAM) to the guanine N1 at nucleotide position 37 in a subset of bacterial tRNA isoacceptors and has proven to be an essential enzyme in most bacterial species	Staphylococcus aureus
physiological function	bacterial tRNA (guanine37-N1)-methyltransferase (TrmD) catalyzes methyl transfer from S-adenosyl-L-methionine (SAM) to the guanine N1 at nucleotide position 37 in a subset of bacterial tRNA isoacceptors and has proven to be an essential enzyme in most bacterial species	Pseudomonas aeruginosa
physiological function	bacterial tRNA (guanine37-N1)-methyltransferase (TrmD) catalyzes methyl transfer from S-adenosyl-L-methionine (SAM) to the guanine N1 at nucleotide position 37 in a subset of bacterial tRNA isoacceptors and has proven to be an essential enzyme in most bacterial species	Mycobacterium tuberculosis