Ligand hydroxylamine

competitive and uncompetitive inhibition; inhibits rVCPO both competitively and uncompetitively. The competitive inhibition constant: 0.04 mM, uncompetitive inhibition 0.08 mM

659641

1.11.1.B8

672311

1.13.11.49

complete loss of activity

slight inhibition at 10 mM

10 mM, complete inhibition

1-3 mM

inhibition of the exchange reaction of diphosphate and ATP

288180

1.2.1.31

in presence of substrate

protonated and neutral form, compete with the attacking water molecule for the binding site E268, inhibition mechanism

288346

1.2.3.1

1 mM, 52% residual activity

699045

1.2.3.4

0.1 mM concentration 100% inhibition

inhibits protein B and fraction C

enzyme preincubated with the inhibitor, 0.00166 mM, for 60 min at room temperature before the addition of the substrate, 9% inhibition

competitive inhibitor with ammonia and uncompetitive inhibitor with both 2-oxoglutarate and NADPH

391965, 391966, 391967

1.4.9.1

396574, 396576, 396585

0.1 M, strong inhibition

392335

1.5.1.8

3 mM, 33% loss of activity

slight

0.1 mM, 69% inhibition

694075

1.5.3.7

15% inhibition at 1 mM

392478

1.5.99.4

22% inhibition at 5 mM

at 5 mM 58% inhibition

slight

34% inhibition at 10 mM

reversible

0.01 M

pyridoxal 5'-phosphate restores

slightly inhibitory

100 mM, complete inhibition

487853

2.5.1.144

3% residual activity at 10 mM

95% inhibition at 1 mM, 76% at 0.1 mM

661358

2.5.1.51

50 mM, almost complete inhibition

100 mM, complete

1 mM, 23% inhibition

inhibition of PfAspAT abolishes all glutamate oxaloacetate transamination activity in the cytoplasm of cultured parasites, demonstrating that no other enzyme within the cytoplasm can complement PfAspAT activity

strong inhibition

637035, 637055, 637056, 637059

70% inhibition at 1 mM

639934

2.6.1.29

complete inhibition at 0.5 mM

639951

2.6.1.33

complete inhibition by a mixture of hydroxylamine, (aminooxy)acetic acid, and gabaculine as inhibitors specific for pyridoxal 5'-phosphate-dependent enzymes

1 mM, 50% inhibition

3.3 mM: 87% inhibition, 0.33 mM: 58.3% inhibition, 0.033 mM: 16.6% inhibition

2 mM, 58% inhibition

0.5 mM: 63% inhibition

inhibits the aldehyde form of the enzyme while the amino form is found to be inert

37% activity retained at 1 mM, 6% activity retained at 10 mM

640193

2.6.1.75

1 mM, complete inhibition of the three isoenzymes

640196

2.6.1.9

0.004 M, 80% inhibition

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

rapid and irreversible inactivation

645949

2.8.3.24

after incubation with 200 mM hydroxylamine at pH 7.0 in the presence of 0.2 mM (R)-2-hydroxyisocaproyl-CoA and removal of the small molecules by gel filtration, the transferase sample shows 94% inactivation, while no inactivation is observed under the same conditions in the absence of (R)-2-hydroxyisocaproyl-CoA

135554, 135674, 135683

inhibits the reaction between ADP-ribose and polypeptides

inactivates the thioester bond on C3, dramatically decreases the deposition of C3b on microbes

699342

3.4.22.1

from Angeli's salt or induced by LPS and IFN-gamma in RAW macrophages, causes DTT-irreversible inhibition and covalently and permanently inactivation of cathepsin B. Cathepsin B activity is reduced to 53%, 25%, and 57% of maximal activity in nonstimulated, LPS-, and IFN-gamma-treated cells, respectively. Endogenous NO production can provide direct protection for the less reactive protein cysteines by scavenging HNO. Additionally, endogenous cellular production of NO can rescue enzyme function by protective nitrosation of cysteines prior to exposure to HNO

competitive inhibitor at pH 7.2

complete inhibition at 0.05 mM, reversible by 100 nM pyridoxal 5'-phosphate

1 mM

67% inhibition at 1 mM

weak

2 mM, complete inhibition

4408, 4411, 4415

formation of a catalytically inactive SH-enzyme from the catalytically active acetyl-S-enzyme

686490

4.1.1.88

formation of a catalytically inactive SH-enzyme from the catalytically active acetyl-S-enzyme

686490

4.1.1.91

1 mM, 23% inhibition of carboxylation activity, 9% inhibition of decarboxylation activity

1 mM, 35% inhibition

82.7% residual activity at 1 mM

1 mM, 95% inhibition

1 mM, 100% inhibition

715045

4.1.2.5

1 mM, complete inhibition

5199

4.1.3.6

reversed with acetic anhydride

partial

1 mM, 10% inhibition

50 mM almost complete inhibition

65% inhibition at 1 mM

competitive

the enzyme is strongly inhibited by hydroxylamine (91.2% inhibition at 1 mM)

almost completely reversible by dialysis against pyridoxal 5'-phosphate

no inhibition

20 mM, 60% inhibition

inhibition of ATP-diphosphate exchange

above 400 mM

3 mM, 80% inhibition

the enzyme is sensitive to treatment with hydroxylamine

sensitive to

complete inhibition

Metals and Ions (1 result)

top print hide

1.13.11.24

nitrosyl hydride replaces dioxygen in nitroxygenase activity of manganese quercetin dioxygenase resulting in the incorporation of both N and O atoms into the product. Turnover is demonstrated by consumption of quercetin and other related substrates under anaerobic conditions in the presence of HNO-releasing compounds and the enzyme. As with dioxygenase activity, a nonenzymatic base-catalyzed reaction of quercetin with HNO isobserved above pH 7, but no enhancement of this basal reactivity is found upon addition of divalent metal salts. Unique and regioselective N-containing products are characterized by MS analysis for both the enzymatic and nonenzymatic reactions

726373