2.7.4.8	5,5'-dithiobis(2-nitrobenzoate)	-	303	
2.7.4.8	6-Selenoguanosine 5'-phosphate	GMP-phosphorylation, pI 4.9-isozyme, competitive with respect to GMP	92063	
2.7.4.8	6-Thioguanosine 5'-phosphate	dGMP-phosphorylation; not thiodeoxyguanosine derivative	29639	
2.7.4.8	6-Thioguanosine 5'-phosphate	GMP-phosphorylation, pI 4.9-isozyme, competitive with respect to GMP	29639	
2.7.4.8	8-azaguanosine 5'-monophosphate	(d)GMP-phosphorylation	15600	
2.7.4.8	8-bromoguanosine 5'-monophosphate	(d)GMP-phosphorylation	43653	
2.7.4.8	9-(1,3-dihydroxy-2-propylmethyl)guanine 5'-monophosphate	-	16912	
2.7.4.8	9-(2-hydroxyethoxymethyl)guanine 5'-monophosphate	-	12765	
2.7.4.8	9-(6,6-difluoro-6-phosphonohexyl)guanine	competitive with respect to GMP, non-competitive with respect to ATP	51497	
2.7.4.8	9-(6-phosphonohexyl)guanine	competitive with respect to GMP, non-competitive with respect to ATP	51498	
2.7.4.8	AMP	10-15% inhibition at 5 mM	30	
2.7.4.8	Ap5G	Ap5G locks an incompletely closed conformation of the enzyme, in which the adenine moiety is located outside its expected binding site. Instead, it binds at a subunit interface that is unique to the bacterial enzyme, which is in equilibrium between a dimeric and an hexameric form in solution.	36150	
2.7.4.8	ATP	-	4	
2.7.4.8	ATP	free form, substrate inhibition, competitive toward MgATP2-	4	
2.7.4.8	aurin	82% inhibition at 0.05 mM	212559	
2.7.4.8	Ca2+	in the presence of Mg2+	15	
2.7.4.8	Ca2+	high inhibition at 1 mM	15	
2.7.4.8	CMP	10-15% inhibition at 5 mM	100	
2.7.4.8	Cs+	strong	580	
2.7.4.8	dAMP	10-15% inhibition at 5 mM	716	
2.7.4.8	dCMP	10-15% inhibition at 5 mM	450	
2.7.4.8	dGMP	competitive inhibitor to GMP	729	
2.7.4.8	dGMP	competitive versus GMP and mixed-type versus ATP	729	
2.7.4.8	diospyrin	-	18445	
2.7.4.8	EDTA	-	21	
2.7.4.8	EDTA	85% inhibition at 3 mM	21	
2.7.4.8	EDTA	complete inhibition at 1 mM	21	
2.7.4.8	GDP	GMP-phosphorylation	53	
2.7.4.8	GDP	-	53	
2.7.4.8	GMP	competitive inhibitor to dGMP	162	
2.7.4.8	GMP	non competitive with respect to MgATP2- because of the formation of an abortive complex guanylate kinase-MgATP2-GMP	162	
2.7.4.8	GMP	-	162	
2.7.4.8	GTP	GMP-phosphorylation	37	
2.7.4.8	guanosine 3',5'-bisdiphosphate	specific inhibition of the organellar isozyme	133443	
2.7.4.8	guanosine 3',5'-bisdiphosphate	specific inhibition of the isozyme	133443	
2.7.4.8	indol-3-acetic acid	GMP + ATP protect	30088	
2.7.4.8	K+	weak	39	
2.7.4.8	Li+	-	152	
2.7.4.8	Li+	strong	152	
2.7.4.8	MgADP-	-	795	
2.7.4.8	MgATP2-	-	108	
2.7.4.8	additional information	GMP-phosphorylation is less sensitive to metal ions than dGMP-phosphorylation; minimal inactivation by iodoacetate and iodoacetamide not affected by the presence or absence of KCl; no inhibition by 2-mercaptoethanol, 1,4-dithiothreitol	2	
2.7.4.8	additional information	no inhibition by 2-mercaptoethanol, 1,4-dithiothreitol; no inhibition by guanosine, AMP, CMP, UMP, XMP, 6-thioinosine 5'-phosphate	2	
2.7.4.8	additional information	guanylic nucleotides strongly inhibit, compete with GMP	2	
2.7.4.8	additional information	no inhibition by 9-(5-phosphonopentyl)guanine (i.e. isosteric analogue of acyclovir 5'-monophosphate)	2	
2.7.4.8	additional information	no inhibition by TMP and by 2-mercaptoethanol up to 5 mM	2	
2.7.4.8	additional information	no inhibition of the cytosolic isozyme by guanosine 3',5'-bisdiphosphate	2	
2.7.4.8	additional information	no or poor inhibition by sulfhydryl group inhibitors p-chloromercuribenzoate and N-ethylmaleimide, reducing agents (DTT and BME) and His modification by diethyl dicarbonate. No or poor inhibition by DEC, ivermectin and levamisole	2	
2.7.4.8	additional information	in silico identification of novel antagonists and binding insights by structural and functional analyses of guanylate kinase of Leishmania donovani and interaction with inhibitors	2	
2.7.4.8	N-ethylmaleimide	-	49	
2.7.4.8	Ni2+	high inhibition at 1 mM	38	
2.7.4.8	p-chloromercuribenzoic acid	1,4-dithiothreitol reverses	614	
2.7.4.8	p-hydroxymercuribenzoate	no effect at 0.25 mM, 30% activity at 2.5 mM	98	
2.7.4.8	p-hydroxymercuribenzoate	-	98	
2.7.4.8	P1 -(5'-adenosyl)-P5 -(5'-guanosyl)pentaphosphate	a non-hydrolysable bi-substrate analogue	213759	
2.7.4.8	phosphate	weak	16	
2.7.4.8	PMSF	inhibits 65% at 5 mM	248	
2.7.4.8	suramin	83.5% inhibition at 0.01 mM	704	
2.7.4.8	UMP	10-15% inhibition at 5 mM	133	
2.7.4.8	Zn2+	high inhibition at 1 mM	14