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Enzyme Nomenclature
Information on EC 3.11.1.1 - phosphonoacetaldehyde hydrolase
for references in articles please use BRENDA:EC3.11.1.1
Word Map on EC 3.11.1.1
- 3.11.1.1
- phosphorus
- phosphonates
-
carbon-phosphorus
-
dehalogenase
-
schiff
- phosphonoacetate
- 2-aminoethylphosphonate
- aerogenes
-
schiff-base
-
phosphomutase
- phosphonopyruvate
-
organophosphonate
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
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EC NUMBER 
COMMENTARY 
3.11.1.1
-
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RECOMMENDED NAME
GeneOntology No.
phosphonoacetaldehyde hydrolase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
phosphonoacetaldehyde + H2O = acetaldehyde + phosphate
Schiff base mechanism
-
phosphonoacetaldehyde + H2O = acetaldehyde + phosphate
imine formation between the enzyme and its substrate
-
phosphonoacetaldehyde + H2O = acetaldehyde + phosphate
double displacement mechanism proceeding via protonated Schiff base and phosphoenzyme intermediates. The mechanism involves P-C bond cleavage in a protonated Schiff base intermediate by in-line displacement by an enzyme nucleophile. Subsequent hydrolysis of the resultant acetaldehyde enamine and phosphoenzyme groups then yield acetaldehyde and phosphate
-
phosphonoacetaldehyde + H2O = acetaldehyde + phosphate
mechanism involves Schiff base formation with Lys53 followed by phosphoryl transfer to Asp12 and at last hydrolysis at the imine and acyl phosphate phosphorus
-
phosphonoacetaldehyde + H2O = acetaldehyde + phosphate
mechanism involves Schiff base formation with Lys53 followed by phosphoryl transfer to Asp11 and at last hydrolysis at the imine and acyl phosphate phosphorus
-
phosphonoacetaldehyde + H2O = acetaldehyde + phosphate
Schiff base formation with catalytic Lys and phosphonoacetaldehyde, PC-bond cleavage in the Schiff base takes place during the second partial reaction and liberation of the acetaldehyde from the resulting enamine occurs during the third partial reaction
-
phosphonoacetaldehyde + H2O = acetaldehyde + phosphate
bicovalent catalytic mechanism in which an active site nucleophile abstracts the phosphoryl group from the Schiff-base intermediate formed from Lys53 and phosphonoacetaldehyde
-
phosphonoacetaldehyde + H2O = acetaldehyde + phosphate
mechanism, active site conformation during catalysis, Lys53 is involved
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phosphonoacetaldehyde + H2O = acetaldehyde + phosphate
active site structure
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phosphonoacetaldehyde + H2O = acetaldehyde + phosphate
mechanism, reaction pathway, Schiff base formation between an amine and a ketone in aqueous solution, active site model
-
phosphonoacetaldehyde + H2O = acetaldehyde + phosphate
quantum chemical study of the imine formation reaction, which precedes P-C bond cleavage. The barrier of this reaction can be significantly lowered if the reaction is assisted by a water molecule and the substrate is protonated
-
phosphonoacetaldehyde + H2O = acetaldehyde + phosphate
alternative catalytic mechanism, involving proton transfer that triggers P-C bond cleavage, transition states, TSd1, TSm1, TSd2, TSm2, and theoretical QM/MM study using crystal structure of an inhibitor-bound enzyme, overview. The bond breaking process is facilitated by proton transfer from catalytic lysine residue to the substrate. The common catalytic mechanism involves formation of a Schiff base, overview
-
phosphonoacetaldehyde + H2O = acetaldehyde + phosphate
Schiff base formation with catalytic Lys and phosphonoacetaldehyde, PC-bond cleavage in the Schiff base takes place during the second partial reaction and liberation of the acetaldehyde from the resulting enamine occurs during the third partial reaction
-
-
phosphonoacetaldehyde + H2O = acetaldehyde + phosphate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of carbon-phosphorus bond
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
2-oxoethylphosphonate phosphonohydrolase
This enzyme destabilizes the C-P bond, by forming an imine between one of its lysine residues and the carbonyl group of the substrate, thus allowing this, normally stable, bond to be broken. The mechanism is similar to that used by EC 4.1.2.13, fructose-bisphosphate aldolase, to break a C-C bond. Belongs to the haloacetate dehalogenase family.
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CAS REGISTRY NUMBER
COMMENTARY
37289-42-2
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
2-aminoethylphosphonic acid:pyruvate aminotransferase and phosphonoacetaldehyde hydrolase activities are induced when cells are both phosphate limited and supplied with 2-aminoethylphosphonic acid as sole source of phosphorus in the culture medium. Neither enzyme is induced in phosphate-replete medium, or in medium where both 2-aminoethylphosphoonic acid and phosphate are supplied
-
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i.e. Geomyces pannorum strain P11, a psychrophilic fungal strain
UniProt
i.e. Geomyces pannorum strain P11, a psychrophilic fungal strain
UniProt
2-aminoethylphosphonic acid:pyruvate aminotransferase and phosphonoacetaldehyde hydrolase activities are induced when cells are both phosphate limited and supplied with 2-aminoethylphosphonic acid as sole source of phosphorus in the culture medium. Neither enzyme is induced in phosphate-replete medium, or in medium where both 2-aminoethylphosphoonic acid and phosphate are supplied
-
-
strain NG2 can utilize 2-aminoethylphosphonic acid as sole carbon and energy, nitrogen and phosphorus source. Both 2-aminoethylphosphonic acid:pyruvate aminotransferase and phosphonoacetaldehyde hydrolase activities are inducible by the presence of 2-aminoethylphosphonic acid in the culture medium
-
-
strain NG2 can utilize 2-aminoethylphosphonic acid as sole carbon and energy, nitrogen and phosphorus source. Both 2-aminoethylphosphonic acid:pyruvate aminotransferase and phosphonoacetaldehyde hydrolase activities are inducible by the presence of 2-aminoethylphosphonic acid in the culture medium
-
-
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
physiological function
additional information
evolution
-
the enzyme is a member of the halo acid dehalogenase superfamily. Distribution of phnX homologs within sequenced bacterial genomes, overview
evolution
the enzyme is a member of the halo acid dehalogenase superfamily. Distribution of phnX homologs within sequenced bacterial genomes, overview
evolution
the enzyme is a member of the halo acid dehalogenase superfamily. Distribution of phnX homologs within sequenced bacterial genomes, overview
evolution
the enzyme is a member of the halo acid dehalogenase superfamily. Distribution of phnX homologs within sequenced bacterial genomes, overview
evolution
-
the enzyme is a member of the halo acid dehalogenase superfamily. Distribution of phnX homologs within sequenced bacterial genomes, overview
-
metabolism
-
the enzyme is involved in the phosphonatase pathway of 2-aminoethylphosphonic acid degradation, overview
metabolism
the enzyme is involved in biodegradation pathway of ciliatine or 2-aminoethylphosphonic acid, a two-step process. The first reaction reported as transamination is carried out by 2-aminoethylphosphonic acid transaminase and leads to the formation of phosphonoacetaldehyde and corresponding amino acid. The next step includes hydrolytic cleavage of the C-P bond within the phosphonoacetaldehyde molecule and results in formation of inorganic phosphate and acetaldehyde, carried out by the phosphonoacetaldehyde hydrolase. The phophonoacetaldehyde hydrolase hydrolyzes
metabolism
-
the enzyme is involved in the phosphonatase pathway of 2-aminoethyl phosphonate degradation also including a 2-AEP:pyruvate aminotransferase (EC 2.6.1.37), encoded by gene phnW, whose products are phosphonoacetaldehyde and alanine. Phosphate-starvation-inducible expression of this pathway as a part of the Pho regulon
metabolism
the enzyme is involved in the phosphonatase pathway of 2-aminoethyl phosphonate degradation also including a 2-AEP:pyruvate aminotransferase (EC 2.6.1.37), encoded by gene phnW, whose products are phosphonoacetaldehyde and alanine. Expression of the operon is substrate-inducible, mediated by the product of an adjacent gene that encodes a LysR-like transcriptional activator, LTTR
metabolism
the enzyme is involved in the phosphonatase pathway of 2-aminoethyl phosphonate degradation also including a 2-AEP:pyruvate aminotransferase (EC 2.6.1.37), encoded by gene phnW, whose products are phosphonoacetaldehyde and alanine. Expression of the operon is substrate-inducible, mediated by the product of an adjacent gene that encodes a LysR-like transcriptional activator, LTTR
metabolism
the enzyme is involved in the phosphonatase pathway of 2-aminoethyl phosphonate degradation also including a 2-AEP:pyruvate aminotransferase (EC 2.6.1.37), encoded by gene phnW, whose products are phosphonoacetaldehyde and alanine. Phosphate-starvation-inducible expression of this pathway as a part of the Pho regulon
metabolism
-
the enzyme is involved in biodegradation pathway of ciliatine or 2-aminoethylphosphonic acid, a two-step process. The first reaction reported as transamination is carried out by 2-aminoethylphosphonic acid transaminase and leads to the formation of phosphonoacetaldehyde and corresponding amino acid. The next step includes hydrolytic cleavage of the C-P bond within the phosphonoacetaldehyde molecule and results in formation of inorganic phosphate and acetaldehyde, carried out by the phosphonoacetaldehyde hydrolase. The phophonoacetaldehyde hydrolase hydrolyzes
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metabolism
-
the enzyme is involved in the phosphonatase pathway of 2-aminoethyl phosphonate degradation also including a 2-AEP:pyruvate aminotransferase (EC 2.6.1.37), encoded by gene phnW, whose products are phosphonoacetaldehyde and alanine. Expression of the operon is substrate-inducible, mediated by the product of an adjacent gene that encodes a LysR-like transcriptional activator, LTTR
-
physiological function
the enzyme is involved in biodegradation pathway of ciliatine or 2-aminoethylphosphonic acid
physiological function
-
the enzyme is involved in biodegradation pathway of ciliatine or 2-aminoethylphosphonic acid
-
additional information
-
the mechanism of C-P bond cleavage by phosphonatase involves the formation of a Schiff base intermediate between a lysine residue at the active site of the enzyme and the phosphonoacetaldehyde carbonyl group, this activates the phosphonate group for attack by an active site nucleophile
additional information
the mechanism of C-P bond cleavage by phosphonatase involves the formation of a Schiff base intermediate between a lysine residue at the active site of the enzyme and the phosphonoacetaldehyde carbonyl group, this activates the phosphonate group for attack by an active site nucleophile
additional information
the mechanism of C-P bond cleavage by phosphonatase involves the formation of a Schiff base intermediate between a lysine residue at the active site of the enzyme and the phosphonoacetaldehyde carbonyl group, this activates the phosphonate group for attack by an active site nucleophile
additional information
the mechanism of C-P bond cleavage by phosphonatase involves the formation of a Schiff base intermediate between a lysine residue at the active site of the enzyme and the phosphonoacetaldehyde carbonyl group, this activates the phosphonate group for attack by an active site nucleophile
additional information
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the mechanism of C-P bond cleavage by phosphonatase involves the formation of a Schiff base intermediate between a lysine residue at the active site of the enzyme and the phosphonoacetaldehyde carbonyl group, this activates the phosphonate group for attack by an active site nucleophile
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
p-nitrophenylphosphate + H2O
p-nitrophenol + phosphate
-
hydrolyzed at considerable lower rate than phosphonoacetaldehyde
-
-
?
phosphonoacetaldehyde + H2O
acetaldehyde + phosphate
i.e. Pald, cleavage via Schiff base intermediate formed with Lys53, bound substrate stabilizes the closed conformation of the active site, thus facilitating catalysis
-
?
phosphonoacetaldehyde + H2O
acetaldehyde + phosphate
-
catalysis within the core domain of phosphonatase requires the participation of loop 5 of the corresponding cap domain. Gly is an indispensable component
-
-
?
phosphonoacetaldehyde + H2O
acetaldehyde + phosphate
-
-
-
?
phosphonoacetaldehyde + H2O
acetaldehyde + phosphate
-
-
-
?
phosphonoacetaldehyde + H2O
acetaldehyde + phosphate
-
-
-
?
phosphonoacetylaldehyde + H2O
acetaldehyde + phosphate
-
2-phosphonoacetaldehyde
-
?
phosphonoacetylaldehyde + H2O
acetaldehyde + phosphate
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second step in the pathway by which Bacillus cereus metabolizes 2-aminoethylphosphonic acid
-
?
phosphonoacetylaldehyde + H2O
acetaldehyde + phosphate
-
second step in the pathway by which Bacillus cereus metabolizes 2-aminoethylphosphonic acid
-
?
phosphonoacetylaldehyde + H2O
acetaldehyde + phosphate
-
second step in the pathway by which Bacillus cereus metabolizes 2-aminoethylphosphonic acid
-
?
phosphonoacetylaldehyde + H2O
acetaldehyde + phosphate
-
-
-
?
phosphonoacetylaldehyde + H2O
acetaldehyde + phosphate
-
-
-
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
phosphonoacetaldehyde + H2O
acetaldehyde + phosphate
A0A093YC30
-
-
-
?
phosphonoacetaldehyde + H2O
acetaldehyde + phosphate
A0A093YC30
-
-
-
?
phosphonoacetaldehyde + H2O
acetaldehyde + phosphate
Q7ZAP3
-
-
-
?
phosphonoacetylaldehyde + H2O
acetaldehyde + phosphate
-
second step in the pathway by which Bacillus cereus metabolizes 2-aminoethylphosphonic acid
-
?
phosphonoacetylaldehyde + H2O
acetaldehyde + phosphate
-
second step in the pathway by which Bacillus cereus metabolizes 2-aminoethylphosphonic acid
-
?
phosphonoacetylaldehyde + H2O
acetaldehyde + phosphate
-
second step in the pathway by which Bacillus cereus metabolizes 2-aminoethylphosphonic acid
-
?
phosphonoacetylaldehyde + H2O
acetaldehyde + phosphate
-
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mg2+
-
activates, required for catalysis, serves as a cofactor, binds via ligation to the loop 1 Asp12 carboxylate and Thr 14 backbone carbonyl and to the loop 4 Asp186carboxylate, the loop 4 Asp190 forms a hydrogen bond to the Mg(II) water ligand, Asp186 is essential while Asp190 simply enhances cofactor binding
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2,4-Dinitrophenylacetate
-
loss of activity due to acetylation of Ls53 with the inert compound, pH profile of inactivation
n-butylphosphonic acid
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activates at low concentrations, inhibits at high concentrations. Allosteric model involving two different classes of sites for n-butylphosphonic acid
NaBH4
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in presence of phosphonoacetaldehyde or acetaldehyde; no effect in absence of substrate or product
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
n-butylphosphonic acid
-
activates at low concentrations, inhibits at high concentrations. Allosteric model involving two different classes of sites for n-butylphosphonic acid
2-Aminoethylphosphonic acid
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both 2-aminoethylphosphonic acid:pyruvate aminotransferase and phosphonoacetaldehyde hydrolase activities are inducible by the presence of 2-aminoethylphosphonic acid in the culture medium
2-Aminoethylphosphonic acid
-
both 2-aminoethylphosphonic acid:pyruvate aminotransferase and phosphonoacetaldehyde hydrolase activities are inducible by the presence of 2-aminoethylphosphonic acid in the culture medium
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.033
phosphonoacetaldehyde
-
wild-type enzyme, mutant C22S, and mutant Y128F/C22S, pH 7.5, 25°C
additional information
additional information
-
kinetics, activity of mutant D186A is too low to measure Km accurately
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.94
phosphonoacetaldehyde
-
mutant C22S, pH 7.5, 25°C; mutant Y128F/C22S, pH 7.5, 25°C; mutant Y128F, pH 7.5, 25°C
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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
6.5 - 10
-
pH 6.5: about 35% of maximal activity, pH 10.0: about 30% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 55
-
30°C: about 50% of maximal activity, 55°C: about 45% of maximal activity
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
-
the organism is not capable of utilizing 2-aminoethyl phosphonate as sole carbon and energy source
additional information
the organism is able to mineralize 2-aminoethyl phosphonate as sole C, N, and P source
additional information
the organism is able to mineralize 2-aminoethyl phosphonate as sole C, N, and P source
additional information
-
the organism is able to mineralize 2-aminoethyl phosphonate as sole C, N, and P source
-
additional information
the organism is not capable of utilizing 2-aminoethyl phosphonate as sole carbon and energy source
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Bacillus cereus;
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
10 mg/ml purified recombinant wild-type and mutant enzymes, complexed with Mg2+ only or with Mg2+ and inhibitor vinyl sulfonate, in 1 mM HEPES, 10 mM MgCl2, 0.1 mM DTT, pH 7.5, 4°C, hanging drop vapour diffusion method, equal volume of protein and reservoir solution, the latter containing 30% PEG 4000, 100 mM Tris-HCl, pH 7.4, 100 mM MgCl2, 1 week, against the reservoir well solution additionally with 20% glycerol before data collection, X-ray diffraction structure determination and analysis at 2.4-2.8 A resolution
-
10 mg/ml wild-type and mutant D12A enzymes complexed with Mg2+ only or with Mg2+ and substrate, in 1 mM HEPES, 10 mM MgCl2, 0.1 mM DTT, pH 7.5, 4°C, hanging drop vapour diffusion method, equal volume of protein and reservoir solution, the latter containing 30% PEG 4000, 100 mM Tris-HCl, pH 7.4, 100 mM MgCl2, 1 week, against the reservoir well solution additionally with 20% glycerol before data collection, X-ray diffraction structure determination and analysis at 2.3-2.55 A
-
crystal structure of the homodimeric enzyme complexed with the phosphate analogue tungstate and Mg2+
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8
-
deprotonation of the active site Cys may be the cause for the loss of enzyme activity
246535
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
inactivation in absence of Mg2+ is aggravated at higher pH or when either EDTA or Ca2+ is added
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene phnX, the gene is encoded within a degradative operon for the mineralization of 2-aminoethylphosphonic acid (2-AEP, ciliatine)
gene phnX, the gene is encoded within a degradative operon for the mineralization of 2-aminoethylphosphonic acid (2-AEP, ciliatine)
-
gene phnX, the gene is encoded within a degradative operon for the mineralization of 2-aminoethylphosphonic acid (2-AEP, ciliatine)
gene phnX, the gene is encoded within a degradative operon for the mineralization of 2-aminoethylphosphonic acid (2-AEP, ciliatine)
gene phnX, the gene is encoded within a degradative operon for the mineralization of 2-aminoethylphosphonic acid (2-AEP, ciliatine)
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C22A
-
site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme
C22S
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
H56A
-
site-directed mutagenesis, very highly reduced activity compared to the wild-type enzyme
K121R/K146R/K192R
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
K183A
-
site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme, Lys183 is probably important in maintaining the active site environment
K183L
-
site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme, Lys183 is probably important in maintaining the active site environment
M49L
Y128A
-
site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme
Y128F
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
Y128F/C22S
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
M49L
-
site-directed mutagenesis, very highly reduced activity compared to the wild-type enzyme
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Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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LINKS TO OTHER DATABASES (specific for EC-Number 3.11.1.1)
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