BRENDA - Enzyme Database
show all sequences of 3.5.1.106

Deciphering the genetic determinants for aerobic nicotinic acid degradation: The nic cluster from Pseudomonas putida KT2440

Jimenez, J.; Canales, A.; Jimenez-Barbero, J.; Ginalski, K.; Rychlewski, L.; Garcia, J.; Diaz, E.; Proc. Natl. Acad. Sci. USA 105, 11329-11334 (2008)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expression in Escherichia coli
Pseudomonas putida
Engineering
Amino acid exchange
Commentary
Organism
D125A
mutation leads to a complete loss of the deformylase activity
Pseudomonas putida
E221A
70% of wild-type deformylase acticity
Pseudomonas putida
H245A
mutation leads to a complete loss of the deformylase activity
Pseudomonas putida
S101A
mutation leads to a complete loss of the deformylase activity
Pseudomonas putida
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
29000
-
x * 29000, SDS-PAGE
Pseudomonas putida
29100
-
x * 29100, calculated from sequence
Pseudomonas putida
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
N-formylmaleamic acid + H2O
Pseudomonas putida
aerobic catabolism of nicotinic acid
maleamate + formate
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Pseudomonas putida
-
-
-
Pseudomonas putida KT 2240
-
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
N-formylmaleamic acid + H2O
aerobic catabolism of nicotinic acid
700940
Pseudomonas putida
maleamate + formate
-
-
-
?
N-formylmaleamic acid + H2O
S101, D125, and H245 are essential for the enzyme activity, constituting the catalytic triad of the NicD deformylase
700940
Pseudomonas putida
maleamate + formate
-
-
-
?
Subunits
Subunits
Commentary
Organism
?
x * 29000, SDS-PAGE; x * 29100, calculated from sequence
Pseudomonas putida
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Escherichia coli
Pseudomonas putida
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
D125A
mutation leads to a complete loss of the deformylase activity
Pseudomonas putida
E221A
70% of wild-type deformylase acticity
Pseudomonas putida
H245A
mutation leads to a complete loss of the deformylase activity
Pseudomonas putida
S101A
mutation leads to a complete loss of the deformylase activity
Pseudomonas putida
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
29000
-
x * 29000, SDS-PAGE
Pseudomonas putida
29100
-
x * 29100, calculated from sequence
Pseudomonas putida
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
N-formylmaleamic acid + H2O
Pseudomonas putida
aerobic catabolism of nicotinic acid
maleamate + formate
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
N-formylmaleamic acid + H2O
aerobic catabolism of nicotinic acid
700940
Pseudomonas putida
maleamate + formate
-
-
-
?
N-formylmaleamic acid + H2O
S101, D125, and H245 are essential for the enzyme activity, constituting the catalytic triad of the NicD deformylase
700940
Pseudomonas putida
maleamate + formate
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 29000, SDS-PAGE; x * 29100, calculated from sequence
Pseudomonas putida
Other publictions for EC 3.5.1.106
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
700940
Jimenez
Deciphering the genetic determ ...
Pseudomonas putida, Pseudomonas putida KT 2240
Proc. Natl. Acad. Sci. USA
105
11329-11334
2008
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