BRENDA - Enzyme Database
show all sequences of 1.5.5.2

High yields of active Thermus thermophilus proline dehydrogenase are obtained using maltose-binding protein as a solubility tag

Huijbers, M.M.; van Berkel, W.J.; Biotechnol. J. 10, 395-403 (2015)

Data extracted from this reference:

Application
Application
Commentary
Organism
synthesis
ProDH is of interest for practical applications because the proline imino acid can serve as a building block for a wide range of peptides and antibiotics
Thermus thermophilus
Cloned(Commentary)
Cloned (Commentary)
Organism
gene TT_C1214, recombinant expression of functional and soluble MBP-tagged enzyme in Escherichia coli TOP10 cells. The MBP tag inhibits the self-association of TtProDH, preventing to a large extent the formation of insoluble protein aggregates
Thermus thermophilus
Inhibitors
Inhibitors
Commentary
Organism
Structure
GuHCl
enzyme unfolding at 1 M, 0.5 M is not enough for proper unfolding. The fusion protein forms visible aggregates due to unfolding of MBP
Thermus thermophilus
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
mitochondrial membrane
a membrane-associated protein
Thermus thermophilus
31966
-
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
additional information
-
the MBP tag inhibits the self-association of TtProDH, preventing to a large extent the formation of insoluble protein aggregates
Thermus thermophilus
78675
-
recombinant MBP-tagged enzyme, sequence calculation
Thermus thermophilus
78677
-
recombinant MBP-tagged enzyme, mass spectrometry
Thermus thermophilus
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
L-proline + a quinone
Thermus thermophilus
-
(S)-1-pyrroline-5-carboxylate + a quinol
-
-
?
L-proline + a quinone
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
-
(S)-1-pyrroline-5-carboxylate + a quinol
-
-
?
Organism
Organism
UniProt
Commentary
Textmining
Thermus thermophilus
Q72IB8
-
-
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
Q72IB8
-
-
Purification (Commentary)
Purification (Commentary)
Organism
recombinant MBP-tagged enzyme from Escherichia coli, gel filtration, and tag cleavage by trypsin, followed by ultrafiltration
Thermus thermophilus
Specific Activity [micromol/min/mg]
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
4
-
purified recombinant MBP-tagged enzyme, pH 8.0, 25C
Thermus thermophilus
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
L-proline + 2,6-dichlorphenol-indophenol
-
742162
Thermus thermophilus
(S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorphenol-indophenol
-
-
-
?
L-proline + 2,6-dichlorphenol-indophenol
-
742162
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
(S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorphenol-indophenol
-
-
-
?
L-proline + a quinone
-
742162
Thermus thermophilus
(S)-1-pyrroline-5-carboxylate + a quinol
-
-
-
?
L-proline + a quinone
a FAD-dependent reaction
742162
Thermus thermophilus
(S)-1-pyrroline-5-carboxylate + a quinol
-
-
-
?
L-proline + a quinone
-
742162
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
(S)-1-pyrroline-5-carboxylate + a quinol
-
-
-
?
L-proline + a quinone
a FAD-dependent reaction
742162
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
(S)-1-pyrroline-5-carboxylate + a quinol
-
-
-
?
Subunits
Subunits
Commentary
Organism
More
recombinant wild-type detagged enzyme and recombinant wild-type MBP-tagged enzyme both form oligomers. Peptide mapping
Thermus thermophilus
Synonyms
Synonyms
Commentary
Organism
PRODH
-
Thermus thermophilus
TtProDH
-
Thermus thermophilus
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
25
-
assay at
Thermus thermophilus
Temperature Stability [C]
Temperature Stability Minimum [C]
Temperature Stability Maximum [C]
Commentary
Organism
additional information
-
enzyme unfolding experiments using recombinant MBP-tagged enzyme in 20 mM Hepes, pH 8.0, at 60-95C, the MBP-tagged enzyme unfolds at lower temperature around 56C due to unfolding of the MBP tag
Thermus thermophilus
90
-
with the native enzyme, rapid loss of activity only occurs at temperatures above 90C
Thermus thermophilus
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
assay at
Thermus thermophilus
Cofactor
Cofactor
Commentary
Organism
Structure
FAD
enzyme-bound, dependent on. Addition of excess FAD hardly improves the enzyme activity, confirming that the enzyme is fully saturated with FAD
Thermus thermophilus
Application (protein specific)
Application
Commentary
Organism
synthesis
ProDH is of interest for practical applications because the proline imino acid can serve as a building block for a wide range of peptides and antibiotics
Thermus thermophilus
Cloned(Commentary) (protein specific)
Commentary
Organism
gene TT_C1214, recombinant expression of functional and soluble MBP-tagged enzyme in Escherichia coli TOP10 cells. The MBP tag inhibits the self-association of TtProDH, preventing to a large extent the formation of insoluble protein aggregates
Thermus thermophilus
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
FAD
enzyme-bound, dependent on. Addition of excess FAD hardly improves the enzyme activity, confirming that the enzyme is fully saturated with FAD
Thermus thermophilus
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
GuHCl
enzyme unfolding at 1 M, 0.5 M is not enough for proper unfolding. The fusion protein forms visible aggregates due to unfolding of MBP
Thermus thermophilus
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
mitochondrial membrane
a membrane-associated protein
Thermus thermophilus
31966
-
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
additional information
-
the MBP tag inhibits the self-association of TtProDH, preventing to a large extent the formation of insoluble protein aggregates
Thermus thermophilus
78675
-
recombinant MBP-tagged enzyme, sequence calculation
Thermus thermophilus
78677
-
recombinant MBP-tagged enzyme, mass spectrometry
Thermus thermophilus
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
L-proline + a quinone
Thermus thermophilus
-
(S)-1-pyrroline-5-carboxylate + a quinol
-
-
?
L-proline + a quinone
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
-
(S)-1-pyrroline-5-carboxylate + a quinol
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant MBP-tagged enzyme from Escherichia coli, gel filtration, and tag cleavage by trypsin, followed by ultrafiltration
Thermus thermophilus
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
4
-
purified recombinant MBP-tagged enzyme, pH 8.0, 25C
Thermus thermophilus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
L-proline + 2,6-dichlorphenol-indophenol
-
742162
Thermus thermophilus
(S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorphenol-indophenol
-
-
-
?
L-proline + 2,6-dichlorphenol-indophenol
-
742162
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
(S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorphenol-indophenol
-
-
-
?
L-proline + a quinone
-
742162
Thermus thermophilus
(S)-1-pyrroline-5-carboxylate + a quinol
-
-
-
?
L-proline + a quinone
a FAD-dependent reaction
742162
Thermus thermophilus
(S)-1-pyrroline-5-carboxylate + a quinol
-
-
-
?
L-proline + a quinone
-
742162
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
(S)-1-pyrroline-5-carboxylate + a quinol
-
-
-
?
L-proline + a quinone
a FAD-dependent reaction
742162
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
(S)-1-pyrroline-5-carboxylate + a quinol
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
More
recombinant wild-type detagged enzyme and recombinant wild-type MBP-tagged enzyme both form oligomers. Peptide mapping
Thermus thermophilus
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
25
-
assay at
Thermus thermophilus
Temperature Stability [C] (protein specific)
Temperature Stability Minimum [C]
Temperature Stability Maximum [C]
Commentary
Organism
additional information
-
enzyme unfolding experiments using recombinant MBP-tagged enzyme in 20 mM Hepes, pH 8.0, at 60-95C, the MBP-tagged enzyme unfolds at lower temperature around 56C due to unfolding of the MBP tag
Thermus thermophilus
90
-
with the native enzyme, rapid loss of activity only occurs at temperatures above 90C
Thermus thermophilus
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
assay at
Thermus thermophilus
General Information
General Information
Commentary
Organism
metabolism
proline dehydrogenase (ProDH) catalyzes the FAD-dependent oxidation of proline to DELTA1-pyrroline-5-carboxylate, the first step of proline catabolism in many organisms
Thermus thermophilus
General Information (protein specific)
General Information
Commentary
Organism
metabolism
proline dehydrogenase (ProDH) catalyzes the FAD-dependent oxidation of proline to DELTA1-pyrroline-5-carboxylate, the first step of proline catabolism in many organisms
Thermus thermophilus
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
Synonyms
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)
743834
Huijbers
Proline dehydrogenase from Th ...
Thermus thermophilus, Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
Sci. Rep.
7
43880
2017
-
-
1
1
1
-
-
3
-
-
-
2
-
6
-
-
-
-
-
-
4
-
4
1
1
1
-
-
3
1
-
-
3
-
-
-
-
-
1
3
1
1
-
-
-
-
3
-
-
-
2
-
-
-
-
-
-
4
-
4
1
1
-
-
3
1
-
-
-
-
-
-
-
3
3
741588
Hancock
Co-regulation of mitochondria ...
Homo sapiens, Mus musculus
Amino Acids
48
859-872
2016
-
-
2
-
1
-
12
-
2
-
-
-
-
4
-
-
1
-
-
-
-
-
-
-
4
2
-
-
-
2
-
-
2
-
-
-
-
-
2
2
-
1
-
-
12
-
-
2
-
-
-
-
-
-
1
-
-
-
-
-
-
2
-
-
-
2
-
-
-
-
6
6
-
-
-
741858
Cabassa-Hourton
Proteomic and functional anal ...
Arabidopsis thaliana
Biochem. J.
473
2623-2634
2016
-
-
-
-
1
-
-
-
3
-
-
-
-
5
-
-
1
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
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-
-
1
-
-
-
-
-
3
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
1
1
-
-
741642
Wang
Molecular cloning and express ...
Jatropha curcas
Appl. Biochem. Biotechnol.
175
2413-2426
2015
-
-
1
-
-
-
-
-
-
-
-
-
-
4
-
-
-
-
-
6
-
-
-
2
2
-
-
-
-
-
-
-
-
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
6
-
-
-
2
-
-
-
-
-
-
-
1
1
2
2
1
-
-
742162
Huijbers
High yields of active Thermus ...
Thermus thermophilus, Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
Biotechnol. J.
10
395-403
2015
-
1
1
-
-
-
1
-
1
-
3
2
-
5
-
-
1
-
-
-
1
-
6
1
2
1
-
2
-
1
-
-
1
-
-
-
-
1
1
1
-
-
-
-
1
-
-
1
-
3
2
-
-
-
1
-
-
1
-
6
1
1
-
2
-
1
-
-
-
-
1
1
-
-
-
740734
Moxley
Evidence for hysteretic substr ...
Escherichia coli
J. Biol. Chem.
289
3639-3651
2014
-
-
-
-
-
-
-
3
-
-
-
-
-
2
-
-
-
-
-
-
-
-
2
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
1
-
-
-
-
-
-
-
-
3
3
742487
Schertl
Biochemical characterization ...
Arabidopsis thaliana
FEBS J.
281
2794-2804
2014
-
-
-
-
-
-
2
-
2
-
-
1
-
4
-
-
-
-
-
-
-
-
2
1
1
-
-
-
-
-
-
-
2
-
-
-
-
-
-
2
-
-
-
-
2
-
-
2
-
-
1
-
-
-
-
-
-
-
-
2
1
-
-
-
-
-
-
-
-
1
2
2
1
-
-
724389
Serrano
Kinetic and isotopic character ...
Mycobacterium tuberculosis
Biochemistry
52
5009-5015
2013
-
-
-
-
2
-
-
3
-
-
1
-
-
2
-
-
1
-
-
-
-
-
1
1
3
-
-
-
2
-
-
-
1
-
-
-
-
-
-
1
-
2
-
-
-
-
3
-
-
1
-
-
-
-
1
-
-
-
-
1
1
-
-
-
2
-
-
-
-
-
-
-
-
2
2
741732
Kawakami
Comparative analysis of the c ...
Pyrococcus furiosus, Pyrococcus horikoshii, Pyrococcus horikoshii OT-3, Thermococcus kodakarensis, Thermococcus kodakarensis KOD1 JCM12380, Thermococcus profundus, Thermococcus profundus DSM 9503
Appl. Microbiol. Biotechnol.
97
3419-3427
2013
-
-
4
-
-
-
8
-
-
-
-
-
-
13
-
-
4
-
-
-
-
-
22
7
24
4
-
4
-
4
-
-
4
-
-
-
-
-
7
7
-
-
-
-
14
-
-
-
-
-
-
-
-
-
7
-
-
-
-
22
7
7
-
7
-
7
-
-
-
-
8
14
-
-
-
742641
Omidinia
Expression, purification and ...
Pseudomonas putida, Pseudomonas putida POS-F84
Indian J. Microbiol.
53
297-302
2013
-
-
1
-
1
-
-
-
-
-
-
-
-
5
-
-
1
-
-
-
-
-
2
2
3
1
1
-
-
1
1
-
1
-
-
-
-
-
1
1
-
1
-
-
-
-
-
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-
-
-
-
-
-
1
-
-
-
-
2
2
1
1
-
-
1
1
-
-
-
1
1
-
-
-
743635
Paes
Proline dehydrogenase regulat ...
Trypanosoma cruzi, Trypanosoma cruzi CL Brener
PLoS ONE
8
e69419
2013
-
-
1
-
-
-
-
1
1
-
-
2
-
5
-
-
1
-
-
1
-
-
10
1
4
1
-
-
-
1
-
-
2
-
-
-
-
-
1
2
-
-
-
-
-
-
1
1
-
-
2
-
-
-
1
-
1
-
-
10
1
1
-
-
-
1
-
-
-
1
2
2
1
-
-
724345
Moxley
Rapid reaction kinetics of pro ...
Escherichia coli
Biochemistry
51
511-520
2012
-
-
-
-
-
-
-
1
-
-
-
-
-
2
-
-
-
-
-
-
-
-
1
-
1
-
-
-
1
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
739932
Kawakami
L-proline dehydrogenases in hy ...
Pyrococcus horikoshii
Appl. Microbiol. Biotechnol.
93
83-93
2012
-
-
-
-
-
-
-
1
-
-
3
1
-
5
-
-
-
-
-
-
1
-
1
1
2
-
-
1
-
-
-
-
4
-
-
-
-
-
-
4
-
-
-
-
-
-
1
-
-
3
1
-
-
-
-
-
-
1
-
1
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
711252
Srivastava
The structure of the proline u ...
Escherichia coli
Biochemistry
49
560-569
2010
-
-
1
1
-
-
1
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
1
-
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-
-
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-
-
-
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-
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-
1
-
1
-
-
-
1
-
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-
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-
-
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-
-
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-
-
-
-
-
-
-
-
696361
Ostrander
A conserved active site tyrosi ...
Escherichia coli
Biochemistry
48
951-959
2009
-
-
1
1
2
-
1
6
-
-
-
-
-
3
-
-
1
-
-
-
-
-
2
-
1
-
-
-
6
-
-
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