BRENDA - Enzyme Database show
show all sequences of 3.5.2.16

[Reactivity and function of cysteine residues in imidase from Pseudomonas putida YZ-26]

Niu, L.; Liu, X.; Shi, Y.; Wei Sheng Wu Xue Bao 51, 776-782 (2011)

Data extracted from this reference:

Engineering
Amino acid exchange
Commentary
Organism
C108G
72% of wild-type activity. Like wild-type, mutant forms tetramers. It has a high binding ability for Zn2+
Pseudomonas putida
C7G
complete loss of activity. Mutant is a mixture of monomers and oligomers and displays decreased binding of Zn2+
Pseudomonas putida
C7G/C108G
complete loss of activity. Mutants is a multimer, with decreased binding ability for Zn2+
Pseudomonas putida
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Zn2+
residue C7 is required or binding of Zn2+ and maintaining the stability of the enzyme
Pseudomonas putida
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Pseudomonas putida
Q4JG22
-
-
Pseudomonas putida YZ-26
Q4JG22
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
DL-5-hydantoin + H2O
-
721108
Pseudomonas putida
hydantoic acid monoamide
-
-
-
?
DL-5-hydantoin + H2O
-
721108
Pseudomonas putida YZ-26
hydantoic acid monoamide
-
-
-
?
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
C108G
72% of wild-type activity. Like wild-type, mutant forms tetramers. It has a high binding ability for Zn2+
Pseudomonas putida
C7G
complete loss of activity. Mutant is a mixture of monomers and oligomers and displays decreased binding of Zn2+
Pseudomonas putida
C7G/C108G
complete loss of activity. Mutants is a multimer, with decreased binding ability for Zn2+
Pseudomonas putida
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Zn2+
residue C7 is required or binding of Zn2+ and maintaining the stability of the enzyme
Pseudomonas putida
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
DL-5-hydantoin + H2O
-
721108
Pseudomonas putida
hydantoic acid monoamide
-
-
-
?
DL-5-hydantoin + H2O
-
721108
Pseudomonas putida YZ-26
hydantoic acid monoamide
-
-
-
?
Other publictions for EC 3.5.2.16
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)
718510
Fan
Crystallization and preliminar ...
Pseudomonas putida, Pseudomonas putida YZ-26
Acta Crystallogr. Sect. F
67
521-523
2011
-
-
1
1
-
-
-
-
-
-
2
-
-
5
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
721108
Niu
[Reactivity and function of cy ...
Pseudomonas putida, Pseudomonas putida YZ-26
Wei Sheng Wu Xue Bao
51
776-782
2011
-
-
-
-
3
-
-
-
-
1
-
-
-
5
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
711007
Shi
Characterization of zinc-bindi ...
Pseudomonas putida, Pseudomonas putida YZ-26
Arch. Biochem. Biophys.
494
1-6
2010
-
-
-
-
4
-
3
-
-
3
-
-
-
5
-
-
-
-
1
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
4
-
-
3
-
-
-
3
-
-
-
-
-
-
1
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
679388
Shi
Gene cloning, expression, and ...
Pseudomonas putida, Pseudomonas putida YZ-26
Curr. Microbiol.
55
61-64
2007
-
-
1
-
-
-
-
4
-
-
2
-
-
9
-
-
1
-
-
-
-
-
5
1
-
-
-
5
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
4
-
-
2
-
-
-
-
1
-
-
-
-
5
1
-
-
-
5
-
-
-
-
-
-
-
-
-
-
654446
Huang
A novel cold-adapted imidase f ...
Agrobacterium tumefaciens, Oreochromis niloticus, Sus scrofa
Biochem. Biophys. Res. Commun.
312
467-472
2003
-
-
-
-
-
-
-
6
-
-
-
1
-
8
-
-
1
-
-
6
1
-
7
-
2
1
3
6
-
-
12
-
-
-
-
-
-
-
-
-
-
-
-
-
-
6
-
-
-
1
-
-
-
1
-
6
1
-
7
-
2
1
3
6
-
-
12
-
-
-
-
-
-
-
654421
Huang
The role of metal on imide hyd ...
Sus scrofa
Biochem. Biophys. Res. Commun.
297
1027-1032
2002
-
-
-
-
-
-
-
-
-
5
-
-
-
1
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
5
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
209265
Ogawa
3-Carbamoyl-alpha-picolinic ac ...
Paenarthrobacter ureafaciens
Appl. Microbiol. Biotechnol.
54
331-334
2000
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
209266
Su
Identification, purification, ...
Sus scrofa
Protein Expr. Purif.
19
289-297
2000
-
-
-
-
-
-
-
3
-
-
2
2
-
2
-
-
1
-
-
2
1
-
4
1
1
1
1
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
3
-
-
2
2
-
-
-
1
-
2
1
-
4
1
1
1
1
-
1
-
1
-
-
-
-
-
-
-
209267
Ogawa
Imidase, a dihydropyrimidinase ...
Blastobacter sp. A17p-4
Eur. J. Biochem.
243
322-327
1997
-
-
-
-
-
-
2
10
-
-
2
2
-
2
-
-
1
-
-
-
1
-
10
1
1
-
1
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
2
-
10
-
-
2
2
-
-
-
1
-
-
1
-
10
1
1
-
1
-
1
-
1
-
-
-
-
-
-
-
209268
Yang
Rat liver imidase ...
Rattus norvegicus
J. Biol. Chem.
268
10870-10874
1993
-
-
-
-
-
-
1
5
-
1
2
3
-
2
-
-
1
-
-
2
1
-
4
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
5
-
1
2
3
-
-
-
1
-
2
1
-
4
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-