2.7.2.1	2,4,6-Trinitrobenzene sulfonic acid	-	19897	
2.7.2.1	2,4-diaminobutyric acid	-	19898	
2.7.2.1	2-oxobutyrate	-	371	
2.7.2.1	2-oxoglutarate	-	34	
2.7.2.1	5,5'-dithiobis(2-nitrobenzoic acid)	-	221	
2.7.2.1	6-oxopiperidine-3-carboxylic acid	82.6% inhibition at 70 mM	256828	
2.7.2.1	6-oxopiperidine-3-carboxylic acid	-	256828	
2.7.2.1	acetate	inhibition by preincubation with MgCl2, ADP, AlCl3, NaF, and acetate. When MgCl2, ADP, and acetate are omitted from the preincubation mixture, there is no detectable loss of activity; inhibition of acetate kinase by preincubation with MgCl2, ADP, AlCl3, NaF, and acetate (all of the components are necessary for maximum inhibition)	47	
2.7.2.1	acetyl phosphate	product inhibition is noncompetitive versus both acetate and ATP	358	
2.7.2.1	acetyl phosphate	-	358	
2.7.2.1	acetyl phosphate	product inhibition	358	
2.7.2.1	adenosine 5'-(gamma-thio)triphosphate	-	57033	
2.7.2.1	ADP	-	13	
2.7.2.1	ADP	inhibition by preincubation with MgCl2, ADP, AlCl3, NaF, and acetate. When MgCl2, ADP, and acetate are omitted from the preincubation mixture, there is no detectable loss of activity; inhibition of acetate kinase by preincubation with MgCl2, ADP, AlCl3, NaF, and acetate (all of the components are necessary for maximum inhibition). The transition state analog, MgADP-aluminum fluoride-acetate, forms an abortive complex in the active site	13	
2.7.2.1	ADP	competitive inhibition; competitive inhibition	13	
2.7.2.1	AlCl3	inhibition by preincubation with MgCl2, ADP, AlCl3, NaF, and acetate. When MgCl2, ADP, and acetate are omitted from the preincubation mixture, there is no detectable loss of activity; inhibition of acetate kinase by preincubation with MgCl2, ADP, AlCl3, NaF, and acetate (all of the components are necessary for maximum inhibition). The transition state analog, MgADP-aluminum fluoride-acetate, forms an abortive complex in the active site. Protection from inhibition by a non-hydrolyzable ATP analog or acetylphosphate. Preincubation of acetate kinase with MgCl2, AlCl3, NaF, acetate, and either IDP, UDP, or CDP in place of ADP results in almost complete inhibition of activity	1785	
2.7.2.1	ATP-gamma-S	non-hydrolyzable inhibitor	23521	
2.7.2.1	Bromoacetate	-	3803	
2.7.2.1	Ca2+	less than 1% residual activity at 1.3 mM	15	
2.7.2.1	CDP	preincubation of acetate kinase with MgCl2, AlCl3, NaF, acetate, and either IDP, UDP, or CDP in place of ADP results in almost complete inhibition of activity	212	
2.7.2.1	chlorogenic acid	58.74% inhibition at 70 mM	592	
2.7.2.1	chlorogenic acid	-	592	
2.7.2.1	citrate	-	131	
2.7.2.1	CrATP	-	20893	
2.7.2.1	CrGTP	-	113225	
2.7.2.1	D-fructose-1,6-bisphosphate	inhibits the activities of isozymes AckA1 and AckA2; inhibits the activities of isozymes AckA1 and AckA2	1895	
2.7.2.1	diethyldicarbonate	-	310	
2.7.2.1	diphosphate	about 70% inhibition in the acetate-forming direction and about 90% inhibition in the acetyl phosphate-forming direction	17	
2.7.2.1	EDTA	complete inhibition at 1.3 mM	21	
2.7.2.1	eugenyl acetate	66.52% inhibition at 70 mM	170814	
2.7.2.1	glyceraldehyde-3-phosphate	inhibits the activities of isozyme AckA1, but very poorly of isozyme AckA2; inhibits the activities of isozyme AckA1, but very poorly of isozyme AckA2	5971	
2.7.2.1	HgCl2	-	110	
2.7.2.1	hydroxylamine	inhibits acetate kinase reaction in a nonlinear and noncompetitive fashion, substantial inhibition at concentrations of 704 mM and minimal inhibition at concentrations of 250 microM hydroxylamine	85	
2.7.2.1	IDP	preincubation of acetate kinase with MgCl2, AlCl3, NaF, acetate, and either IDP, UDP, or CDP in place of ADP results in almost complete inhibition of activity	444	
2.7.2.1	iodoacetamide	-	67	
2.7.2.1	iodoacetate	-	93	
2.7.2.1	Iodosobenzoate	-	3856	
2.7.2.1	K+	-	39	
2.7.2.1	KCl	activity linearly decreases from 100% (at 0 mM added KCl) to 71% at 500 mM added KCl	79	
2.7.2.1	Li+	-	152	
2.7.2.1	MgCl2	inhibition by preincubation with MgCl2, ADP, AlCl3, NaF, and acetate. When MgCl2, ADP, and acetate are omitted from the preincubation mixture, there is no detectable loss of activity; inhibition of acetate kinase by preincubation with MgCl2, ADP, AlCl3, NaF, and acetate (all of the components are necessary for maximum inhibition). The transition state analog, MgADP-aluminum fluoride-acetate, forms an abortive complex in the active site. Preincubation of acetate kinase with MgCl2, AlCl3, NaF, acetate, and either IDP, UDP, or CDP in place of ADP results in almost complete inhibition of activity	196	
2.7.2.1	additional information	not inactivated by 5,5'-dithiobis(2-nitrobenzoic acid), tetranitromethane or 2-hydroxy-3-nitro-benzyl bromide	2	
2.7.2.1	additional information	not inactivated by N-ethylmaleimide	2	
2.7.2.1	additional information	5,5'-dithiobis(2-nitrobenzoic acid), p-chloromercuriphenylsulfonate, N-ethylmaleimide and phenylglyoxal does not affect the enzyme activity	2	
2.7.2.1	additional information	iodoacetate and iodoacetamide does not inhibit	2	
2.7.2.1	additional information	preincubation with butyrate does not significantly inhibit the enzyme	2	
2.7.2.1	additional information	inhibitor design using the the structure of the catalytic intermediate	2	
2.7.2.1	additional information	not inhibited by eugenyl acetate and pinoresinol	2	
2.7.2.1	additional information	not inhibited by phosphate	2	
2.7.2.1	N-ethylmaleimide	-	49	
2.7.2.1	Na+	-	59	
2.7.2.1	NaF	inhibition by preincubation with MgCl2, ADP, AlCl3, NaF, and acetate. When MgCl2, ADP, and acetate are omitted from the preincubation mixture, there is no detectable loss of activity; inhibition of acetate kinase by preincubation with MgCl2, ADP, AlCl3, NaF, and acetate (all of the components are necessary for maximum inhibition). The transition state analog, MgADP-aluminum fluoride-acetate, forms an abortive complex in the active site. Preincubation of acetate kinase with MgCl2, AlCl3, NaF, acetate, and either IDP, UDP, or CDP in place of ADP results in almost complete inhibition of activity	235	
2.7.2.1	p-chloromercuribenzoate	-	43	
2.7.2.1	p-hydroxymercuribenzoate	-	98	
2.7.2.1	p-mercuribenzoate	-	686	
2.7.2.1	Phenylglyoxal	-	301	
2.7.2.1	phosphate	-	16	
2.7.2.1	phospho-enol-pyruvate	PEP, a downstream intermediate of glycolysis, completely inhibits the activity of both enzymes at concentrations above 30 mM; PEP, a downstream intermediate of glycolysis, completely inhibits the activity of both enzymes at concentrations above 30 mM	213707	
2.7.2.1	pinoresinol	82.6% inhibition at 70 mM	256829	
2.7.2.1	potassium hydroxylamine	-	114268	
2.7.2.1	propionate	preincubation with MgCl2, ADP, AlCl3, NaF, and propionate results in almost complete inhibition of activity	312	
2.7.2.1	propionic acid	competitive inhibitor with respect to acetate	1724	
2.7.2.1	propionic acid	-	1724	
2.7.2.1	sodium hydroxylamine	-	114446	
2.7.2.1	succinate	-	58	
2.7.2.1	trifluoroethanol	leads to reduced growth and acetate content, binding mode by molecular docking	11162	
2.7.2.1	trifluoroethyl butyrate	leads to reduced growth and acetate content, binding mode by molecular docking	213708	
2.7.2.1	UDP	preincubation of acetate kinase with MgCl2, AlCl3, NaF, acetate, and either IDP, UDP, or CDP in place of ADP results in almost complete inhibition of activity	26	
2.7.2.1	Zn2+	less than 5% residual activity at 1.3 mM	14