BRENDA - Enzyme Database
show all sequences of 1.5.5.2

Evidence for hysteretic substrate channeling in the proline dehydrogenase and delta1-pyrroline-5-carboxylate dehydrogenase coupled reaction of proline utilization A (PutA)

Moxley, M.A.; Sanyal, N.; Krishnan, N.; Tanner, J.J.; Becker, D.F.; J. Biol. Chem. 289, 3639-3651 (2014)

Data extracted from this reference:

KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0235
-
NAD+
overall reaction of bifunctional enzyme, pH 7.5, 21°C
Escherichia coli
2
-
L-proline
pH 7.5, 21°C
Escherichia coli
42
-
NAD+
pH 7.5, 21°C
Escherichia coli
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Escherichia coli
P09546
bifunctional proline dehydrogenase and delta1-pyrroline-5-carboxylate dehydrogenase, reactions of EC 1.5.5.2 and EC 1.2.1.88, respectively
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-proline + NAD+ + H2O
-
740734
Escherichia coli
(S)-1-pyrroline-5-carboxylate + NADH
-
-
-
?
additional information
kinetic model for the overall PRODH-P5CDH reaction of bifunctional PutA enzyme. The intermediate is not released into the bulk medium, but the mechanism follows substrate channeling. The rate of NADH formation is 20fold slower than the steady-state turnover number for the overall reaction, The limiting rate constant observed for NADH formation in the first turnover increases by almost 40fold after multiple turnovers, achieving half of the steady-state value after 15 turnovers
740734
Escherichia coli
?
-
-
-
-
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
5.2
-
L-proline
pH 7.5, 21°C
Escherichia coli
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0235
-
NAD+
overall reaction of bifunctional enzyme, pH 7.5, 21°C
Escherichia coli
2
-
L-proline
pH 7.5, 21°C
Escherichia coli
42
-
NAD+
pH 7.5, 21°C
Escherichia coli
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-proline + NAD+ + H2O
-
740734
Escherichia coli
(S)-1-pyrroline-5-carboxylate + NADH
-
-
-
?
additional information
kinetic model for the overall PRODH-P5CDH reaction of bifunctional PutA enzyme. The intermediate is not released into the bulk medium, but the mechanism follows substrate channeling. The rate of NADH formation is 20fold slower than the steady-state turnover number for the overall reaction, The limiting rate constant observed for NADH formation in the first turnover increases by almost 40fold after multiple turnovers, achieving half of the steady-state value after 15 turnovers
740734
Escherichia coli
?
-
-
-
-
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
5.2
-
L-proline
pH 7.5, 21°C
Escherichia coli
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.124
-
L-proline
pH 7.5, 21°C
Escherichia coli
31
-
NAD+
overall reaction of bifunctional enzyme, pH 7.5, 21°C
Escherichia coli
235
-
NAD+
pH 7.5, 21°C
Escherichia coli
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.124
-
L-proline
pH 7.5, 21°C
Escherichia coli
31
-
NAD+
overall reaction of bifunctional enzyme, pH 7.5, 21°C
Escherichia coli
235
-
NAD+
pH 7.5, 21°C
Escherichia coli
Other publictions for EC 1.5.5.2
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)
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Moxley
Evidence for hysteretic substr ...
Escherichia coli
J. Biol. Chem.
289
3639-3651
2014
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-
-
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3
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2
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2
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1
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1
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1
1
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2
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2
2
741732
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13
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4
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22
7
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4
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4
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4
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7
7
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-
-
-
14
-
-
-
-
-
-
-
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-
7
-
-
-
-
22
7
7
-
7
-
7
-
-
-
-
8
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1
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1
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5
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1
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-
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-
2
2
1
1
-
-
1
1
-
1
-
-
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-
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1
1
-
1
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-
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-
-
-
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1
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-
-
2
2
1
1
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-
1
1
-
-
-
1
1
-
-
-
743635
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PLoS ONE
8
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1
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1
1
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2
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5
-
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1
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-
1
-
-
10
1
1
-
-
-
1
-
-
2
-
-
-
-
-
1
2
-
-
-
-
-
-
1
1
-
-
2
-
-
-
1
-
1
-
-
10
1
1
-
-
-
1
-
-
-
1
2
2
1
-
-
724345
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51
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2012
-
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-
-
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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
-
-
-
-
-
-
-
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-
-
-
-
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
739932
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Appl. Microbiol. Biotechnol.
93
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2012
-
-
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-
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-
1
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-
3
1
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5
-
-
-
-
-
-
1
-
1
1
-
-
1
-
-
-
-
4
-
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4
-
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1
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3
1
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1
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1
1
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1
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711252
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49
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2010
-
-
1
1
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1
-
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-
-
-
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2
-
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-
-
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1
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1
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1
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1
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1
6
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-
-
-
3
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1
-
-
-
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2
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6
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1
3
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1
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6
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671977
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-
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4
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4
1
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2
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1
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1
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4
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4
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4
1
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1
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4
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658033
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Biochemistry
43
12539-12548
2004
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1
1
1
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3
2
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1
1
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3
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1
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1
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1
2
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3
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1
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1
1
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3
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2
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1
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2
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658211
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1701
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2004
-
-
1
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3
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4
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2
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1
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4
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658668
Kawakami
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Thermococcus profundus
Extremophiles
8
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2004
-
-
1
-
-
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1
-
1
5
-
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10
-
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1
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1
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2
1
1
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1
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1
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1
1
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1
1
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1
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1
5
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1
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1
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2
1
1
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1
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1
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1
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659987
Lee
Structure of the proline dehyd ...
Escherichia coli
Nat. Struct. Biol.
10
109-114
2003
-
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1
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1
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3
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1
1
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1
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1
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1
1
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392565
Nadaraia
Crystallization and preliminar ...
Escherichia coli
Acta Crystallogr. Sect. D
57
1925-1927
2001
-
-
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1
-
-
-
-
-
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2
-
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1
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1
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1
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392570
Sakuraba
Purification, characterization ...
Thermococcus profundus
Appl. Environ. Microbiol.
67
1470-1475
2001
-
-
-
-
-
-
-
1
-
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3
-
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6
-
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1
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1
1
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2
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1
1
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1
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1
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3
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1
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1
1
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2
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1
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-
392572
Chaudhary
-
Proline dehydrogenase activity ...
Vigna radiata
Indian J. Exp. Biol.
37
1234-1240
1999
-
-
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1
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392571
Brown
Conformational change and memb ...
Escherichia coli
J. Biol. Chem.
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8972-8979
1993
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1
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392569
Deutch
-
Oxidation of L-thiazolidine-4- ...
Escherichia coli
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1593-1598
1992
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2
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722591
Brown
Redesigned purification yields ...
Escherichia coli
J. Biol. Chem.
267
13086-13092
1992
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2
1
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3
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1
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1
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1
1
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1
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392555
Wood
Membrane association of prolin ...
Escherichia coli
Proc. Natl. Acad. Sci. USA
84
373-377
1987
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1
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2
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392556
Graham
Proline dehydrogenase from Esc ...
Escherichia coli
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259
2656-2661
1984
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2
2
2
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4
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3
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3
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392560
Scarpulla
Membrane-bound proline dehydro ...
Escherichia coli
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253
5997-6001
1978
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5
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1
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4
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5
4
1
1
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1
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4
1
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