Zinc is a cofactor. While N-benzylformamide is the best substrate, the enzyme from Arthrobacter pascens can also act on the N-substituted formamides N-butylformamide, N-allylformamide, N-[2-(cyclohex-1-enyl)ethyl]formamide and N-(1-phenylethyl)formamide, but much more slowly. Amides of other acids do not act as substrates.
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
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
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SYSTEMATIC NAME
IUBMB Comments
N-benzylformamide amidohydrolase
Zinc is a cofactor. While N-benzylformamide is the best substrate, the enzyme from Arthrobacter pascens can also act on the N-substituted formamides N-butylformamide, N-allylformamide, N-[2-(cyclohex-1-enyl)ethyl]formamide and N-(1-phenylethyl)formamide, but much more slowly. Amides of other acids do not act as substrates.
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
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
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
a benzylamine analogue, dead-end inhibition study, overview; inhibits the reverse enzyme reaction, uncompetitive versus benzylamine, competitive versus formate
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
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
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
development of six inducible shuttle vectors, pESH19cF, pESH19cR, pESH19kF, pESH19kR, pESH19aF, and pESH19aR, for Streptomyces-Escherichia coli, evaluation of stability and activity in expression of different enzymes including the N-substituted formamide deformylase as model enzymes, overview. Catechol 2,3-dioxygenase, nitrilase, and N-substituted formamide deformylase encoding genes are expressed from the different vectors as reporter genes showing that pESH19cF, pESH19kF, and pESH19aF possess inducible expression ability in Streptomyces lividans strain TK24. The stability test shows that the pSH19-derived shuttle vectors are stable in Escherichia coli strain Stbl2 and Streptomyces lividans strain TK24. Streptomyces lividans strain TK24 is the better host
development of six inducible shuttle vectors, pESH19cF, pESH19cR, pESH19kF, pESH19kR, pESH19aF, and pESH19aR, for Streptomyces-Escherichia coli, evaluation of stability and activity in expression of different enzymes including the N-substituted formamide deformylase as model enzymes, overview. Catechol 2,3-dioxygenase, nitrilase, and N-substituted formamide deformylase encoding genes are expressed from the different vectors as reporter genes showing that pESH19cF, pESH19kF, and pESH19aF possess inducible expression ability in Streptomyces lividans strain TK24. The stability test shows that the pSH19-derived shuttle vectors are stable in Escherichia coli strain Stbl2 and Streptomyces lividans strain TK24. Streptomyces lividans strain TK24 is the better host
gene nfdA, recombinant expression of the enzyme from vectors pESH19cF-nfdA, pESH19kF-nfdA, and pESH19aF-nfdA in Escherichia coli strain Stbl2 and Streptomyces lividans strain TK24
High-level expression of a novel amine-synthesizing enzyme, N-substituted formamide deformylase, in Streptomyces with a strong protein expression system