BRENDA - Enzyme Database show
show all sequences of 3.5.5.7

Transformation of aliphatic and aromatic nitriles by a nitrilase from Pseudomonas sp.

Dhillon, J.; Chhatre, S.; Shanker, R.; Shivaraman, N.; Can. J. Microbiol. 45, 811-815 (1999)
No PubMed abstract available

Data extracted from this reference:

KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
kinetics
Pseudomonas sp.
0.75
-
potassium cyanide
pH 7.0, 37C, partially purified enzyme
Pseudomonas sp.
5.88
-
acrylonitrile
pH 7.0, 37C, partially purified enzyme
Pseudomonas sp.
10.28
-
adiponitrile
pH 7.0, 37C, partially purified enzyme
Pseudomonas sp.
11.26
-
acetonitrile
pH 7.0, 37C, partially purified enzyme
Pseudomonas sp.
12.27
-
Benzonitrile
pH 7.0, 37C, partially purified enzyme
Pseudomonas sp.
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
41000
-
native PAGE
Pseudomonas sp.
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Pseudomonas sp.
-
from soil
-
Pseudomonas sp. S1
-
from soil
-
Purification (Commentary)
Commentary
Organism
3-step procedure, partially, 10.9fold
Pseudomonas sp.
Reaction
Reaction
Commentary
Organism
R-CN + 2 H2O = R-COOH + NH3
preferentially hydrolyses aliphatic nitriles, some of which are apparently not substrates for other known nitrilases, EC 3.5.5.1. Substrates include crotonitrile, acrylnitrile and glutaronitrile
Pseudomonas sp.
Specific Activity [micromol/min/mg]
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
17.53
-
partially purified enzyme
Pseudomonas sp.
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
acetonitrile + H2O
-
209747
Pseudomonas sp.
acetate + NH3
-
-
-
?
acetonitrile + H2O
-
209747
Pseudomonas sp. S1
acetate + NH3
-
-
-
?
acrylonitrile + H2O
most effective substrate
209747
Pseudomonas sp.
acrylate + NH3
-
-
-
?
acrylonitrile + H2O
most effective substrate
209747
Pseudomonas sp. S1
acrylate + NH3
-
-
-
?
adiponitrile + H2O
-
209747
Pseudomonas sp.
adipate + NH3
-
-
-
?
benzonitrile + H2O
-
209747
Pseudomonas sp.
benzoic acid + NH3
-
-
-
?
benzonitrile + H2O
-
209747
Pseudomonas sp. S1
benzoic acid + NH3
-
-
-
?
butyronitrile + H2O
-
209747
Pseudomonas sp.
butyrate + NH3
-
-
-
?
butyronitrile + H2O
-
209747
Pseudomonas sp. S1
butyrate + NH3
-
-
-
?
glutaronitrile + H2O
-
209747
Pseudomonas sp.
glutarate + NH3
-
-
-
?
glutaronitrile + H2O
-
209747
Pseudomonas sp. S1
glutarate + NH3
-
-
-
?
phenylacetonitrile + H2O
-
209747
Pseudomonas sp.
phenylacetic acid + NH3
-
-
-
?
potassium cyanide + H2O
-
209747
Pseudomonas sp.
?
-
-
-
?
R-CN + H2O
enzyme uses both aliphatic and aromatic nitriles, no formation of amide intermediate
209747
Pseudomonas sp.
R-COOH + NH3
-
-
-
?
succinodinitrile + H2O
-
209747
Pseudomonas sp.
?
-
-
-
?
Subunits
Subunits
Commentary
Organism
monomer
1 * 41000, SDS-PAGE
Pseudomonas sp.
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
37
-
assay at
Pseudomonas sp.
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
assay at
Pseudomonas sp.
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
kinetics
Pseudomonas sp.
0.75
-
potassium cyanide
pH 7.0, 37C, partially purified enzyme
Pseudomonas sp.
5.88
-
acrylonitrile
pH 7.0, 37C, partially purified enzyme
Pseudomonas sp.
10.28
-
adiponitrile
pH 7.0, 37C, partially purified enzyme
Pseudomonas sp.
11.26
-
acetonitrile
pH 7.0, 37C, partially purified enzyme
Pseudomonas sp.
12.27
-
Benzonitrile
pH 7.0, 37C, partially purified enzyme
Pseudomonas sp.
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
41000
-
native PAGE
Pseudomonas sp.
Purification (Commentary) (protein specific)
Commentary
Organism
3-step procedure, partially, 10.9fold
Pseudomonas sp.
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
17.53
-
partially purified enzyme
Pseudomonas sp.
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
acetonitrile + H2O
-
209747
Pseudomonas sp.
acetate + NH3
-
-
-
?
acetonitrile + H2O
-
209747
Pseudomonas sp. S1
acetate + NH3
-
-
-
?
acrylonitrile + H2O
most effective substrate
209747
Pseudomonas sp.
acrylate + NH3
-
-
-
?
acrylonitrile + H2O
most effective substrate
209747
Pseudomonas sp. S1
acrylate + NH3
-
-
-
?
adiponitrile + H2O
-
209747
Pseudomonas sp.
adipate + NH3
-
-
-
?
benzonitrile + H2O
-
209747
Pseudomonas sp.
benzoic acid + NH3
-
-
-
?
benzonitrile + H2O
-
209747
Pseudomonas sp. S1
benzoic acid + NH3
-
-
-
?
butyronitrile + H2O
-
209747
Pseudomonas sp.
butyrate + NH3
-
-
-
?
butyronitrile + H2O
-
209747
Pseudomonas sp. S1
butyrate + NH3
-
-
-
?
glutaronitrile + H2O
-
209747
Pseudomonas sp.
glutarate + NH3
-
-
-
?
glutaronitrile + H2O
-
209747
Pseudomonas sp. S1
glutarate + NH3
-
-
-
?
phenylacetonitrile + H2O
-
209747
Pseudomonas sp.
phenylacetic acid + NH3
-
-
-
?
potassium cyanide + H2O
-
209747
Pseudomonas sp.
?
-
-
-
?
R-CN + H2O
enzyme uses both aliphatic and aromatic nitriles, no formation of amide intermediate
209747
Pseudomonas sp.
R-COOH + NH3
-
-
-
?
succinodinitrile + H2O
-
209747
Pseudomonas sp.
?
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
monomer
1 * 41000, SDS-PAGE
Pseudomonas sp.
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
37
-
assay at
Pseudomonas sp.
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
assay at
Pseudomonas sp.
Other publictions for EC 3.5.5.7
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)
733526
Fang
Enzymatic degradation of aliph ...
Rhodococcus rhodochrous, Rhodococcus rhodochrous BX2
Biores. Technol.
185
28-34
2015
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
8
-
-
-
-
-
-
-
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-
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-
-
8
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
733919
Yusuf
Cloning and functional charact ...
Fusarium proliferatum, Fusarium proliferatum AUF-2
Funct. Integr. Genomics
15
413-424
2015
1
-
1
-
-
-
12
1
-
6
1
-
-
2
-
-
1
-
-
-
-
-
22
1
1
1
-
-
1
-
-
-
-
-
-
1
-
1
-
-
-
-
-
12
-
1
-
6
1
-
-
-
-
1
-
-
-
-
22
1
1
1
-
-
1
-
-
-
-
-
-
-
-
-
734577
Zhang
Structural insights into enzym ...
Synechocystis sp.
J. Struct. Biol.
188
93-101
2014
-
-
1
1
25
-
-
18
-
-
-
-
-
1
-
-
1
-
-
-
18
-
5
-
-
-
-
18
-
-
-
-
-
-
-
-
-
1
-
1
25
-
-
-
-
18
-
-
-
-
-
-
-
1
-
-
18
-
5
-
-
-
-
18
-
-
-
-
-
-
-
-
18
18
735340
Wang
A novel nitrilase from Rhodoba ...
Rhodobacter sphaeroides, Rhodobacter sphaeroides LHS-305
World J. Microbiol. Biotechnol.
30
245-252
2014
-
-
1
-
-
-
9
1
-
-
2
-
-
2
-
-
1
-
-
-
-
-
19
1
1
1
-
-
1
1
-
-
-
-
-
-
-
1
-
-
-
-
-
9
-
1
-
-
2
-
-
-
-
1
-
-
-
-
19
1
1
1
-
-
1
1
-
-
-
-
-
-
-
-
710984
Bayer
A nitrilase from a metagenomic ...
uncultured bacterium
Appl. Microbiol. Biotechnol.
89
91-98
2011
-
-
1
-
-
-
4
1
-
-
2
-
-
2
-
-
1
-
-
-
-
-
13
1
1
-
1
-
1
1
-
-
-
-
-
-
-
1
-
-
-
-
-
4
-
1
-
-
2
-
-
-
-
1
-
-
-
-
13
1
1
-
1
-
1
1
-
-
-
-
-
-
1
1
718661
He
A high-throughput screening st ...
Alcaligenes sp., Alcaligenes sp. ECU0401, Rhodococcus erythropolis, Rhodococcus erythropolis CGMCC 1.2362
Appl. Microbiol. Biotechnol.
89
817-823
2011
-
-
-
-
-
-
-
-
-
-
-
-
-
5
-
-
-
-
-
-
2
-
12
-
2
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
12
-
2
-
-
-
2
-
-
-
-
-
-
-
-
-
695831
Kim
Identification and characteriz ...
Pseudomonas fluorescens, Pseudomonas fluorescens Pf-5
Appl. Microbiol. Biotechnol.
83
273-283
2009
-
-
1
-
-
-
6
7
-
-
2
-
-
5
-
-
-
-
-
-
2
-
13
1
1
-
5
7
1
-
-
-
-
1
-
-
-
1
-
-
-
-
-
6
-
7
-
-
2
-
-
-
-
-
-
-
2
-
13
1
1
-
5
7
1
-
-
1
-
-
-
-
-
-
699065
Nigam
Nitrilase-catalysed conversion ...
Streptomyces sp.
J. Biosci.
34
21-26
2009
-
1
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
712260
Thuku
Microbial nitrilases: Versatil ...
Acidovorax facilis, Acidovorax facilis 72W, Acinetobacter sp., Acinetobacter sp. AK226, Comamonas testosteroni, Pseudomonas sp., Pseudomonas sp. S1, Pyrococcus abyssi, Rhodococcus rhodochrous, Rhodococcus rhodochrous J1, Rhodococcus rhodochrous K22, Synechocystis sp.
J. Appl. Microbiol.
106
703-727
2009
1
2
-
-
3
-
-
-
-
-
14
-
-
22
-
-
-
-
-
-
-
-
29
8
7
-
-
-
7
-
-
-
-
-
-
1
2
-
-
-
3
-
-
-
-
-
-
-
14
-
-
-
-
-
-
-
-
-
29
8
7
-
-
-
7
-
-
-
-
-
-
-
-
-
712870
Sharma
-
In silico analysis of amino ac ...
Bradyrhizobium sp., Bradyrhizobium sp. ORS278, Methylibium petroleiphilum, Pseudomonas syringae pv. syringae, Rhodococcus rhodochrous, Rhodococcus rhodochrous J1, Rhodococcus rhodochrous K22, Synechococcus elongatus
J. Proteomics Bioinform.
2
185-192
2009
-
-
-
-
-
-
-
-
-
-
6
-
-
27
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
6
-
-
-
-
-
-
-
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-
-
-
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-
-
6
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
6
-
-
-
-
-
-
685014
Yeom
A determinant residue of subst ...
Rhodococcus rhodochrous
Biochem. J.
415
401-407
2008
-
-
1
1
16
-
-
31
-
-
1
-
1
2
-
-
1
1
-
-
13
-
9
1
-
-
-
32
-
-
-
-
-
-
-
-
-
1
-
1
25
-
-
-
-
32
-
-
1
-
1
-
-
1
-
-
13
-
9
1
-
-
-
32
-
-
-
-
-
-
-
-
-
-
695708
Luo
Gene cloning, overexpression, ...
Rhodococcus rhodochrous, Rhodococcus rhodochrous tg1-A6
Appl. Biochem. Biotechnol.
160
393-400
2008
-
-
1
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
10
-
1
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
10
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
687941
Khandelwal
-
Optimization of nitrilase prod ...
Streptomyces sp., Streptomyces sp. MTCC 7546
J. Chem. Technol. Biotechnol.
82
646-651
2007
2
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
20
-
1
1
-
-
1
1
1
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
20
-
1
1
-
-
1
1
1
-
-
-
-
-
-
-
670463
Bergeron
-
Nitrilase-catalyzed desymmetri ...
Pseudomonas fluorescens
Org. Proc. Res. Dev.
10
661-665
2006
-
1
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
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-
-
-
-
-
-
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-
1
-
-
-
-
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
670792
Mueller
Cloning, overexpression, and c ...
no activity in Aeropyrum pernix, no activity in Pyrococcus furiosus, no activity in Pyrococcus horikoshii, Pyrococcus abyssi, Pyrococcus abyssi GE5 / CNCM I-1302 / DSM 25543
Protein Expr. Purif.
47
672-681
2006
4
-
1
-
-
-
24
2
1
-
4
-
-
6
-
-
1
-
-
-
3
-
10
2
1
1
6
-
1
1
-
-
-
1
-
4
-
1
-
-
-
-
-
24
-
2
1
-
4
-
-
-
-
1
-
-
3
-
10
2
1
1
6
-
1
1
-
1
-
-
-
-
-
-
685425
Holtze
Transformation of the herbicid ...
Pseudomonas fluorescens 11387, Pseudomonas fluorescens, Pseudomonas putida 11388, Pseudomonas putida, Rhizobium sp. 11401, Rhizobium sp.
Biodegradation
17
503-510
2006
-
-
-
-
-
-
-
-
-
-
-
-
-
6
-
-
-
-
-
-
-
-
6
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
6
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
686545
Mukherjee
-
Exploring the synthetic applic ...
Synechocystis sp.
Eur. J. Org. Chem.
23
5238-5242
2006
-
-
1
-
-
-
-
-
-
-
-
-
-
1
-
-
1
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8
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1
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1
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8
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670922
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8
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2
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2
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1
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2
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1
1
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1
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2
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3
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3
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1
20
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26
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1
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1
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1
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1
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2
1
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1
1
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1
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1
20
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26
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1
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1
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1
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1
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15
1
1
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1
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6
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1
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15
1
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1
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32507
Levy-Schil
Aliphatic nitrilase from a soi ...
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1
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5
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1
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6
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1
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1
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1
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6
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32505
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Primary structure of an alipha ...
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10
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1
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1
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2
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1
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1
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6
1
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3
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6
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1
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1
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63
2
1
1
7
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1
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2
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-
-
-
-
-
-
-
-
-
3
-
2
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1
3
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1
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1
-
63
2
1
1
7
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1
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2
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-
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-