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Information on EC 3.5.1.56 - N,N-dimethylformamidase
for references in articles please use BRENDA:EC3.5.1.56
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EC Tree 3 Hydrolases
3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
3.5.1 In linear amides
3.5.1.56 N,N-dimethylformamidase
IUBMB Comments
An iron protein. Also acts on N-ethylformamide and N-methyl-formamide and, more slowly, on N,N-diethylformamide, N,N-dimethylacetamide and unsubstituted acyl amides.
The enzyme appears in viruses and cellular organisms
- 3.5.1.56
- paracoccus
-
methylotrophic
- waste
- alcaligenes
- aminophilus
- environmental protection
showSynonyms
dmfase, dimethylformamidase, n,n-dimethylformamidase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dimethylformamidase
DMFase
N,N-dimethylformamidase
dimethylformamidase
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-
-
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DMFase
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-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
N,N-dimethylformamide + H2O = dimethylamine + formate
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N,N-dimethylformamide + H2O = dimethylamine + formate
an enzyme of high substrate specificity that catalyzes the first step in the degradation of N,N-dimethylformamide
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of linear amides
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-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
N,N-dimethylformamide amidohydrolase
An iron protein. Also acts on N-ethylformamide and N-methyl-formamide and, more slowly, on N,N-diethylformamide, N,N-dimethylacetamide and unsubstituted acyl amides.
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CAS REGISTRY NUMBER
COMMENTARY
104645-73-0
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
formamide + H2O
NH3 + formate
-
Substrates: 3.8% of the activity with N,N-dimethylformamide
Products: -
Products: -
?
prolinamide + H2O
NH3 + proline
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Substrates: 1.6% of the activity with N,N-dimethylformamide
Products: -
Products: -
?
N,N-diethylformamide + H2O
diethylamine + formate
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Substrates: 29% of the activity with N,N-dimethylformamide
Products: -
Products: -
?
N,N-diethylformamide + H2O
diethylamine + formate
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Substrates: 29% of the activity with N,N-dimethylformamide
Products: -
Products: -
?
N,N-diethylformamide + H2O
diethylamine + formate
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Substrates: 2.6% of the activity with N,N-dimethylformamide
Products: -
Products: -
?
N,N-diethylformamide + H2O
diethylamine + formate
-
Substrates: 2.6% of the activity with N,N-dimethylformamide
Products: -
Products: -
?
N,N-dimethylacetamide + H2O
dimethylamine + acetate
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Substrates: 31% of the activity with N,N-dimethylformamide
Products: -
Products: -
?
N,N-dimethylacetamide + H2O
dimethylamine + acetate
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Substrates: 31% of the activity with N,N-dimethylformamide
Products: -
Products: -
?
N,N-dimethylacetamide + H2O
dimethylamine + acetate
-
Substrates: 3.4% of the activity with N,N-dimethylformamide
Products: -
Products: -
?
N,N-dimethylformamide + H2O
dimethylamine + formate
-
Substrates: -
Products: -
Products: -
?
N,N-dimethylformamide + H2O
dimethylamine + formate
-
Substrates: -
Products: -
Products: -
?
N,N-dimethylformamide + H2O
dimethylamine + formate
A0A2Y9CJ10
Substrates: -
Products: -
Products: -
?
N,N-dimethylformamide + H2O
dimethylamine + formate
-
Substrates: -
Products: -
Products: -
?
N,N-dimethylformamide + H2O
dimethylamine + formate
-
Substrates: catabolic pathway and related enzymes, degradation by strain DGVK1 leads to accumulation of ammonia and dimethylamine, overview
Products: -
Products: -
?
N,N-dimethylformamide + H2O
dimethylamine + formate
-
Substrates: -
Products: -
Products: -
?
N,N-dimethylformamide + H2O
dimethylamine + formate
-
Substrates: catabolic pathway and related enzymes, degradation by strain DGVK1 leads to accumulation of ammonia and dimethylamine, overview
Products: -
Products: -
?
N,N-dimethylformamide + H2O
dimethylamine + formate
-
Substrates: an enzyme of high substrate specificity that catalyzes the first step in the degradation of N,N-dimethylformamide
Products: -
Products: -
?
N,N-dimethylformamide + H2O
dimethylamine + formate
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Substrates: N,N-dimethylformamide, a toxic solvent used in the chemical industry, is frequently present in industrial waste
Products: -
Products: -
?
N,N-dimethylformamide + H2O
dimethylamine + formate
-
Substrates: -
Products: -
Products: -
?
N,N-dimethylformamide + H2O
dimethylamine + formate
-
Substrates: -
Products: -
Products: -
?
N-ethylformamide + H2O
ethylamine + formate
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Substrates: 31.5% of the activity with N,N-dimethylformamide
Products: -
Products: -
?
N-ethylformamide + H2O
ethylamine + formate
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Substrates: 31.5% of the activity with N,N-dimethylformamide
Products: -
Products: -
?
N-methylformamide + H2O
methylamine + formate
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Substrates: 14.8% of the activity with N,N-dimethylformamide
Products: -
Products: -
?
N-methylformamide + H2O
methylamine + formate
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Substrates: 14.8% of the activity with N,N-dimethylformamide
Products: -
Products: -
?
additional information
?
-
-
Substrates: less than 1% of the activity with N,N-dimethylformamide: acetamide, acrylamide, butyramide
Products: -
Products: -
?
additional information
?
-
-
Substrates: less than 1% of the activity with N,N-dimethylformamide: acetamide, acrylamide, butyramide
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
N,N-dimethylformamide + H2O
dimethylamine + formate
-
Substrates: -
Products: -
Products: -
?
N,N-dimethylformamide + H2O
dimethylamine + formate
-
Substrates: -
Products: -
Products: -
?
N,N-dimethylformamide + H2O
dimethylamine + formate
A0A2Y9CJ10
Substrates: -
Products: -
Products: -
?
N,N-dimethylformamide + H2O
dimethylamine + formate
-
Substrates: catabolic pathway and related enzymes, degradation by strain DGVK1 leads to accumulation of ammonia and dimethylamine, overview
Products: -
Products: -
?
N,N-dimethylformamide + H2O
dimethylamine + formate
-
Substrates: catabolic pathway and related enzymes, degradation by strain DGVK1 leads to accumulation of ammonia and dimethylamine, overview
Products: -
Products: -
?
N,N-dimethylformamide + H2O
dimethylamine + formate
-
Substrates: an enzyme of high substrate specificity that catalyzes the first step in the degradation of N,N-dimethylformamide
Products: -
Products: -
?
N,N-dimethylformamide + H2O
dimethylamine + formate
-
Substrates: -
Products: -
Products: -
?
N,N-dimethylformamide + H2O
dimethylamine + formate
-
Substrates: -
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
27.6
N,N-Dimethylformamide
A0A2Y9CJ10
pH 6.5, 37°C, recombinant enzyme
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isolated from soil samples collected from coalmine leftovers
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
A0A2Y9CJ10
strain DM1 can utilize N,N-dimethylformamide, DMA, MA, methanol, ethanol, formamide, toluene, glycerol, and trisodium citrate as the sole source of carbon or carbon and nitrogen
brenda
additional information
-
strain DGVK1 is able to grow on N,N-dimethylformamide as sole carbon and nitrogen source, overview
brenda
additional information
-
strain DGVK1 is able to grow on N,N-dimethylformamide as sole carbon and nitrogen source, overview
-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
A0A2Y9CJ10
the enzyme is important and initial in the N,N-dimethylformamide (DMF) degradation pathway, transcriptional analysis of genes specific to DMF degradation, overview
physiological function
physiological function
-
plasmid pAMI2 of Paracoccus aminophilus JCM 7686 carries genetic information which is crucial for the methylotrophic growth, using N,N-dimethylformamide as the sole source of carbon and energy. The plasmid carries a three-gene cluster coding for DmfR, a transcription regulator of the LuxR familiy and two subunits, DmfA1 and DmfA2 of N,N-dimethylformamidase, an enzyme of high substrate specificity that catalyzes the first step in the degradation of N,N-dimethylformamide
physiological function
A0A2Y9CJ10
the enzyme is responsible for N,N-dimethylformamide degradation, molecular mechanism, overview
Show AA Sequence and Transmembrane Helices (156 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heterotetramer
A0A2Y9CJ10
recombinent enzyme, alpha2beta2, 2 * 20000, alpha-subunit, + 2 * 80000, beta-subunit, SDS-PAGE
tetramer
additional information
additional information
-
plasmid pAMI2 of Paracoccus aminophilus JCM 7686 carries genetic information which is crucial for the methylotrophic growth, using N,N-dimethylformamide as the sole source of carbon and energy. The plasmid carries a three-gene cluster coding for DmfR, a transcription regulator of the LuxR familiy and two subunits, DmfA1 and DmfA2 of N,N-dimethylformamidase, an enzyme of high substrate specificity that catalyzes the first step in the degradation of N,N-dimethylformamide
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
A0A2Y9CJ10
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, expression in Escherichai coli
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encoded on plasmid pLVM1, DNA and amino acid sequence determination and analysis, genetic organization, sequence comparisons and phylogenetic analysis, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)
A0A2Y9CJ10
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
environmental protection
environmental protection
-
the enzyme activity is useful to treat industrial effluent containing dimethylformamide obtained from pharmaceutical industry
environmental protection
-
the enzyme activity is useful to treat industrial effluent containing dimethylformamide obtained from pharmaceutical industry
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Schär, H.P.; Holzmann, W.; Ramos Tombo, G.M.; Ghisalba, O.
Purification and characterization of N,N-dimethylformamidase from Pseudomonas DMF 3/3
Eur. J. Biochem.
158
469-475
1986
Pseudomonas sp., Pseudomonas sp. DMF 3/3
brenda
Hasegawa, Y.; Matsuo, M.; Sigemoto, Y.; Sakai, T.; Tokuyama, T.
Purification and characterisation of N,N-dimethylformamidase from Alcaligenes sp. KUFA-1
J. Ferment. Bioeng.
84
543-547
1997
Alcaligenes sp., Alcaligenes sp. KUFA-1
-
brenda
Veeranagouda, Y.; Emmanuel Paul, P.V.; Gorla, P.; Siddavattam, D.; Karegoudar, T.B.
Complete mineralisation of dimethylformamide by Ochrobactrum sp. DGVK1 isolated from the soil samples collected from the coalmine leftovers
Appl. Microbiol. Biotechnol.
71
369-375
2006
Ochrobactrum sp., Ochrobactrum sp. DGVK1
brenda
Dziewit, L.; Dmowski, M.; Baj, J.; Bartosik, D.
Plasmid pAMI2 of Paracoccus aminophilus JCM 7686 carries N,N-dimethylformamide degradation-related genes whose expression is activated by a LuxR family regulator
Appl. Environ. Microbiol.
76
1861-1869
2010
Paracoccus aminophilus
brenda
Lu, X.; Wang, W.; Zhang, L.; Hu, H.; Xu, P.; Wei, T.; Tang, H.
Molecular mechanism of N,N-dimethylformamide degradation in Methylobacterium sp. strain DM1
Appl. Environ. Microbiol.
85
e00275-19
2019
Methylobacterium sp. DM1 (A0A2Y9CJ10)
brenda
EXTERNAL LINKS (specific for EC-Number 3.5.1.56)
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Release 2023.1 (January 2023)
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