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Literature summary extracted from

  • Hashimoto, Y.; Sakashita, T.; Fukatsu, H.; Sato, H.; Kobayashi, M.
    A new synthetic route to N-benzyl carboxamides through the reverse reaction of N-substituted formamide deformylase (2014), Appl. Environ. Microbiol., 80, 61-69.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.5.1.91 ammonium persulfate 12% activation at 1 mM Arthrobacter pascens
3.5.1.91 diisopropyl fluorophosphate 17% activation at 1 mM Arthrobacter pascens
3.5.1.91 EDTA 27% activation at 1 mM Arthrobacter pascens
3.5.1.91 KCN slight activation at 1 mM Arthrobacter pascens

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.5.1.91 2,2'-dipyridyl 15% inhibition at 1 mM Arthrobacter pascens
3.5.1.91 2-mercaptoethanol 64% inhibition at 1 mM Arthrobacter pascens
3.5.1.91 3-Phenylpropylamine inhibits the reverse enzyme reaction Arthrobacter pascens
3.5.1.91 8-hydroxyquinoline 84% inhibition at 1 mM Arthrobacter pascens
3.5.1.91 AgNO3 complete inhibition at 1 mM Arthrobacter pascens
3.5.1.91 aminoguanidine 19% inhibition at 1 mM Arthrobacter pascens
3.5.1.91 aniline a benzylamine analogue, dead-end inhibition study, overview; inhibits the reverse enzyme reaction, uncompetitive versus benzylamine, competitive versus formate Arthrobacter pascens
3.5.1.91 Butyrate slight inhibition of the reverse reaction, competitive versus benzylamine, noncompetitive versus formate Arthrobacter pascens
3.5.1.91 CdCl2 57% inhibition at 1 mM Arthrobacter pascens
3.5.1.91 CuCl complete inhibition at 0.25 mM Arthrobacter pascens
3.5.1.91 CuCl2 complete inhibition at 1 mM Arthrobacter pascens
3.5.1.91 dithiothreitol complete inhibition at 1 mM Arthrobacter pascens
3.5.1.91 H2O2 slight inhibition at 1 mM Arthrobacter pascens
3.5.1.91 HgCl2 complete inhibition at 1 mM Arthrobacter pascens
3.5.1.91 Isobutyrate slight inhibition of the reverse reaction Arthrobacter pascens
3.5.1.91 additional information no or poor inhibition by 1 mM of LiCl, NaCl, MgCl2, CaCl2, BaCl2, MnCl2, AlCl3, Pb(NO3)2, FeSO4, FeCl3, RbCl, SrCl2, CsCl, Na2MoO4, CoCl2, NiCl2, and ZnCl2. No inhibition by iodoacetate, 5,5'-dithio-bis-2-nitrobenzoate, diethyldithiocarbamate, NaN3, and phenylmethanesulfonyl fluoride. Valerate, isovalerate, and caproate cannot be tested because they are insoluble in the reaction buffer Arthrobacter pascens
3.5.1.91 N-ethylmaleimide 79% inhibition at 1 mM Arthrobacter pascens
3.5.1.91 o-phenanthroline 32% inhibition at 1 mM Arthrobacter pascens
3.5.1.91 p-chloromercuribenzoate complete inhibition at 1 mM Arthrobacter pascens
3.5.1.91 phenethylamine inhibits the reverse enzyme reaction Arthrobacter pascens
3.5.1.91 phenylhydrazine 23% inhibition at 1 mM Arthrobacter pascens
3.5.1.91 Semicarbazide 8% inhibition at 1 mM Arthrobacter pascens
3.5.1.91 SnCl2 44% inhibition at 1 mM Arthrobacter pascens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.5.1.91 additional information
-
 additional information bisubstrate kinetic analysis using formate and benzylamine, overview Arthrobacter pascens
3.5.1.91 0.075
-
 N-benzylformamide pH 7.5, 25°C Arthrobacter pascens
3.5.1.91 53.6
-
 benzylamine pH 7.0, 25°C Arthrobacter pascens
3.5.1.91 1210
-
 acetate pH 7.0, 25°C Arthrobacter pascens
3.5.1.91 3010
-
 formate pH 7.0, 25°C Arthrobacter pascens
3.5.1.91 3850
-
 propionate pH 7.0, 25°C Arthrobacter pascens

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.5.1.91 additional information no or poor inhibition by 1 mM of LiCl, NaCl, MgCl2, CaCl2, BaCl2, MnCl2, AlCl3, Pb(NO3)2, FeSO4, FeCl3, RbCl, SrCl2, CsCl, Na2MoO4, CoCl2, NiCl2, and ZnCl2 Arthrobacter pascens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.5.1.91 N-benzylformamide + H2O Arthrobacter pascens
-
 formate + benzylamine
-
 r
3.5.1.91 N-benzylformamide + H2O Arthrobacter pascens F164
-
 formate + benzylamine
-
 r

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.91 Arthrobacter pascens
-
-
-
3.5.1.91 Arthrobacter pascens F164
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
3.5.1.91 N-benzylformamide + H2O = formate + benzylamine the reverse reaction of this enzyme proceeds via an ordered two-substrate, two-product (bi-bi) mechanism in which formate binds first to the enzyme active site, followed by benzylamine binding and the subsequent release of N-benzylformamide, kinetic mechanism, overview Arthrobacter pascens
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.1.91 additional information mass spectra on LC-ESI-MS of the reverse-reaction products of N-substituted formamide deformylase, overview. No activity with butyrate and isobutyrate Arthrobacter pascens ?
-
 ?
3.5.1.91 additional information mass spectra on LC-ESI-MS of the reverse-reaction products of N-substituted formamide deformylase, overview. No activity with butyrate and isobutyrate Arthrobacter pascens F164 ?
-
 ?
3.5.1.91 N-benzylacetamide + H2O the enzyme catalyzes the reverse reaction from acetate and benzylamine at high substrate concentrations Arthrobacter pascens acetate + benzylamine
-
 r
3.5.1.91 N-benzylacetamide + H2O the enzyme catalyzes the reverse reaction from acetate and benzylamine at high substrate concentrations Arthrobacter pascens F164 acetate + benzylamine
-
 r
3.5.1.91 N-benzylformamide + H2O
-
 Arthrobacter pascens formate + benzylamine
-
 r
3.5.1.91 N-benzylformamide + H2O the enzyme catalyzes the reverse reaction at high substrate concentrations, synthesizing N-benzylformamide from benzylamine and formate. The reverse reaction proceeds only in the presence of high substrate concentrations. Effects of pH and inhibitors on the reverse reaction are almost the same as those on the forward reaction, suggesting that the forward and reverse reactions are both catalyzed at the same catalytic site Arthrobacter pascens formate + benzylamine
-
 r
3.5.1.91 N-benzylformamide + H2O
-
 Arthrobacter pascens F164 formate + benzylamine
-
 r
3.5.1.91 N-benzylformamide + H2O the enzyme catalyzes the reverse reaction at high substrate concentrations, synthesizing N-benzylformamide from benzylamine and formate. The reverse reaction proceeds only in the presence of high substrate concentrations. Effects of pH and inhibitors on the reverse reaction are almost the same as those on the forward reaction, suggesting that the forward and reverse reactions are both catalyzed at the same catalytic site Arthrobacter pascens F164 formate + benzylamine
-
 r
3.5.1.91 N-benzylpropionamide + H2O the enzyme catalyzes the reverse reaction from propionate and benzylamine at high substrate concentrations Arthrobacter pascens propionate + benzylamine
-
 r
3.5.1.91 N-benzylpropionamide + H2O the enzyme catalyzes the reverse reaction from propionate and benzylamine at high substrate concentrations Arthrobacter pascens F164 propionate + benzylamine
-
 r

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.5.1.91 25
-
 reverse reaction Arthrobacter pascens

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.5.1.91 45
-
 pH 7.5, 30 min, completely stable up to Arthrobacter pascens
3.5.1.91 50
-
 pH 7.5, 30 min, 78% activity remaining Arthrobacter pascens
3.5.1.91 55
-
 pH 7.5, 30 min, and above, no activity remaining Arthrobacter pascens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.5.1.91 7
-
 reverse reaction Arthrobacter pascens

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.5.1.91 5 9 activity range, profile overview Arthrobacter pascens

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.5.1.91 6.5 9.5 25°C, 30 min, 80% activity remaining at pH 8.0, below 20% at pH 6,5 and pH 9.5, inactivation at pH 6.0 and pH 10.0, profile overview Arthrobacter pascens

IC50 Value

EC Number IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
3.5.1.91 13.3
-
 pH 7.0, 25°C Arthrobacter pascens 3-Phenylpropylamine
3.5.1.91 14.5
-
 pH 7.0, 25°C Arthrobacter pascens aniline
3.5.1.91 27.8
-
 pH 7.0, 25°C Arthrobacter pascens phenethylamine
3.5.1.91 275
-
 pH 7.0, 25°C Arthrobacter pascens Butyrate
3.5.1.91 280
-
 pH 7.0, 25°C Arthrobacter pascens Isobutyrate

General Information

EC Number General Information Comment Organism
3.5.1.91 evolution the enzyme belongs to the the amidohydrolase superfamily. Although N-substituted formamide deformylase is one of the amine-forming deformylases, it shows no amino acid sequence similarity to any other deformylases known so far. Contrary to expectation, the deduced amino acid sequence of N-substituted formamide deformylase exhibited the highest overall sequence identity (28%) to those of regulatory proteins Arthrobacter pascens
3.5.1.91 additional information the enzyme contains (alpha/beta)8 barrel structure in the N-terminal region with five conserved residues (four histidines and one aspartic acid) Arthrobacter pascens
3.5.1.91 physiological function N-substituted formamide deformylase is involved in the degradation of toxic isonitriles Arthrobacter pascens

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
3.5.1.91 0.003
-
 propionate pH 7.0, 25°C Arthrobacter pascens
3.5.1.91 0.008
-
 acetate pH 7.0, 25°C Arthrobacter pascens
3.5.1.91 0.011
-
 formate pH 7.0, 25°C Arthrobacter pascens
3.5.1.91 0.411
-
 benzylamine pH 7.0, 25°C Arthrobacter pascens
3.5.1.91 687
-
 N-benzylformamide pH 7.5, 25°C Arthrobacter pascens