2.7.7.4 2,2'-azino-di-(3-ethylbenzothiazoline)-6-sulfonic acid - 256889 2.7.7.4 3',5'-adenosine diphosphate - 33051 2.7.7.4 3'-phosphoadenosine 5'-phosphosulfate allosteric, binding of the inhibitor to the catalytic site as well as to the allosteric site of the wild type enzyme acts to decrease the degree of cooperativity 2171 2.7.7.4 3'-phosphoadenosine-5'-phosphate strong 7470 2.7.7.4 3'-phosphoadenosine-5'-phosphate - 7470 2.7.7.4 3'-phosphoadenosine-5'-phosphate allosteric 7470 2.7.7.4 3'-phosphoadenosine-5'-phosphosulfate - 3782 2.7.7.4 3,5-di-tert-butyl-4-hydroxytoluene - 256890 2.7.7.4 3-tert-butyl-4-hydroxyanisole ligand diffuses through the gate formed by residues Glu332, Thr312 and His290 to the outside of enzyme. When the gate opens, the ligand is expelled from active site of enzyme, thereafter the ligand returns when the gate closes and binds itself in another region of active site nearby the zinc atom 188709 2.7.7.4 5,5'-dithiobis(2-nitrobenzoic acid) 0.05 mM, rapid decrease in activity of wild-type enzyme (t1/2: 20 s), truncated enzyme del396-573 retains more than 97% of its activity after 30 min 221 2.7.7.4 adenosine 5'-monosulfate - 12414 2.7.7.4 adenosine 5'-phosphoramidate - 5927 2.7.7.4 adenosine 5'-phosphosulfate potent product inhibitor, competitive with respect to MgATP2-, and a mixed type inhibitor with respect to molybdate 425 2.7.7.4 adenosine 5'-phosphosulfate potent product inhibition, competitive with both MgATP2- and MoO42- in molybdolysis assay 425 2.7.7.4 adenosine 5'-phosphosulfate - 425 2.7.7.4 adenosine 5'-phosphosulfate 1 mM, 30% inhibition 425 2.7.7.4 adenosine 5'-phosphosulfate 1 mM, 90% inhibition 425 2.7.7.4 adenosine 5'-phosphosulfate inhibits molybdolysis 425 2.7.7.4 adenosine 5'-phosphosulfate competitive with ATP and molybdate 425 2.7.7.4 adenosine 5'-phosphosulfate competitive with both substrates 425 2.7.7.4 adenylyl sulfate APS, binding mode, overview. On the ATP sulfurylase domain that initially produces APS from sulfate and ATP, APS acts as a potent product inhibitor, being competitive with both ATP and sulfate. For the APS kinase domain that phosphorylates APS to PAPS, APS is an uncompetitive substrate inhibitor that can bind both at the ATP/ADP-binding site and the PAPS/APS-binding site; APS, binding mode, overview. On the ATP sulfurylase domain that initially produces APS from sulfate and ATP, APS acts as a potent product inhibitor, being competitive with both ATP and sulfate. For the APS kinase domain that phosphorylates APS to PAPS, APS is an uncompetitive substrate inhibitor that can bind both at the ATP/ADP-binding site and the PAPS/APS-binding site 1311 2.7.7.4 ADP linear competitive inhibitor with respect to SO42-, uncompetitive with respect to ATP 13 2.7.7.4 ADP - 13 2.7.7.4 AMP linear competitive inhibitor with respect to SO42-, uncompetitive with respect to ATP 30 2.7.7.4 AMP competitive with MgATP2- and mixed-type with respect to SO42- 30 2.7.7.4 AMP - 30 2.7.7.4 ATP MgATP2- is the actual substrate, free ATP is an inhibitor of the forward reaction 4 2.7.7.4 ATP free ATP 4 2.7.7.4 ATP product inhibitor in formation of ATP from diphosphate and adenylylsulfate 4 2.7.7.4 ATP - 4 2.7.7.4 Ba2+ 2 mM 111 2.7.7.4 beta-fluoro-adenosine 5'-phosphosulfate - 33118 2.7.7.4 beta-methylene-adenosine 5'-phosphosulfate - 33119 2.7.7.4 Ca2+ - 15 2.7.7.4 Ca2+ 2 mM 15 2.7.7.4 ClO3- competitive with SO42- and apparently uncompetitive with respect to MgATP2- 4799 2.7.7.4 ClO3- - 4799 2.7.7.4 ClO3- competitive with SO42- or MoO42-, competitive against MgATP2- 4799 2.7.7.4 ClO4- competitive with SO42- and apparently uncompetitive with respect to MgATP2- 2832 2.7.7.4 ClO4- linear competitive inhibitor with respect to SO42- and uncompetitive with respect to ATP 2832 2.7.7.4 ClO4- competitive with SO42- or MoO42-, competitive against MgATP2- 2832 2.7.7.4 ClO4- - 2832 2.7.7.4 ClO4- competitive with sulfate and adenylyl sulfate 2832 2.7.7.4 Cys 2 mM, slight 553 2.7.7.4 deoxyadenylylsulfate 1 mM, in presence of about 20% inhibition 51615 2.7.7.4 diacetyl significant inhibition in the presence of borate, protection by adenosine 5'-phosphosulfate, ATP or MgATP2- plus nitrate 746 2.7.7.4 diphosphate mixed-type inhibitor with respect to both MgATP2- and MoO42- 17 2.7.7.4 diphosphate noncompetitive with respect to MgATP and sulfate 17 2.7.7.4 EDTA inhibits due to chelation of Mg2+ 21 2.7.7.4 EDTA inhibition is reversed by mn2+, Mg2+, Cu2+, Co2+ 21 2.7.7.4 FSO3- competitive with SO42- and apparently uncompetitive with respect to MgATP2- 5150 2.7.7.4 FSO3- - 5150 2.7.7.4 FSO3- inhibition in absence of 3'-phosphoadenosine-5'-phosphate 5150 2.7.7.4 FSO3- competitive with SO42- or MoO42-, competitive against MgATP2- 5150 2.7.7.4 FSO3- 0.03 mM, 50% inhibition 5150 2.7.7.4 guanylylsulfate 1 mM, in presence of adenylylsulfate about 20% inhibition 97975 2.7.7.4 Hg2+ - 33 2.7.7.4 inosylylsulfate 1 mM, in presence of adenylylsulfate about 20% inhibition 113666 2.7.7.4 iodoacetic acid - 213 2.7.7.4 Met 2 mM, slight 678 2.7.7.4 methylene blue inactivated by light in presence of methylene blue, protection by adenosine 5'-phosphosulfate 512 2.7.7.4 MgATP2- - 108 2.7.7.4 MgATP2- competitive with respect to adenosine 5'-phosphosulfate 108 2.7.7.4 MgATP2- competitive with respect to adenosine 5'-phosphosulfate; mixed-type with respect to diphosphate 108 2.7.7.4 molybdate - 509 2.7.7.4 MoO42- - 2413 2.7.7.4 N-Acetylimidazole 76% of the original activity can be restored by treatment with hydroxylamine 1559 2.7.7.4 N-ethylmaleimide - 49 2.7.7.4 NAD+ - 7 2.7.7.4 NEM 10 mM, inhibits reaction with diphosphate and adenylylsulfate 89 2.7.7.4 NEM 0.15 mM, rapid decrease in activity of wild-type enzyme (t1/2: 45 s), truncated enzyme del396-573 retains more than 97% of its activity after 30 min 89 2.7.7.4 Ni2+ 2 mM 38 2.7.7.4 NO3- competitive with SO42- and apparently uncompetitive with respect to MgATP2- 673 2.7.7.4 NO3- linear competitive inhibitor with respect to SO42- and uncompetitive with respect to ATP 673 2.7.7.4 NO3- dead-end inhibitor, competitive with SO42- 673 2.7.7.4 NO3- competitive with SO42- or MoO42-, competitive against MgATP2- 673 2.7.7.4 NO3- - 673 2.7.7.4 PCMB 5 mM, inhibits reaction with diphosphate and adenylylsulfate 78 2.7.7.4 Phenylglyoxal 3 mM, irreversible inactivation of wild-type enzyme and mutant enzyme del396-573, t1/2: 5 min for both forms 301 2.7.7.4 phosphate inhibition is enhanced by increasing concentrations of Mg2+ 16 2.7.7.4 S2O32- noncompetitive mixed-type inhibition with respect to MgATP2- 3364 2.7.7.4 S2O32- - 3364 2.7.7.4 S2O32- 1 mM, 62% inhibition 3364 2.7.7.4 S2O32- dead-end inhibitor, competitive with SO42- or MoO42-, noncompetitive against MgATP2- 3364 2.7.7.4 SeO42- - 5615 2.7.7.4 SeO42- competitive inhibition at and above 0.075 mM 5615 2.7.7.4 SO32- 1 mM, 10-25% inhibition 902 2.7.7.4 SO42- product inhibitor in formation of ATP from diphosphate and adenylylsulfate 245 2.7.7.4 SO42- competitive with respect to MoO42- 245 2.7.7.4 sulfate - 160 2.7.7.4 Sulfide - 318 2.7.7.4 Sulfide no inhibition 318 2.7.7.4 Sulfide 4 mM, 65% inhibition 318 2.7.7.4 Sulfide inhibitory effect 318 2.7.7.4 Tetranitromethane partial 1453 2.7.7.4 thiosulfate competitive with molybdate and noncompetitive with MgATP 475 2.7.7.4 Tris-malic acid-KOH buffer pH 6-8.5 22167 2.7.7.4 Zn2+ inhibitory effect even at concentrations as low as 40 mg/l 14