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Information on EC 1.5.1.48 - 2-methyl-1-pyrroline reductase
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1.5.1.48 2-methyl-1-pyrroline reductaseIUBMB Comments
The enzyme from the bacterium Streptomyces sp. GF3587 is highly specific for its substrate and forms only the (R) isomer.
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The enzyme appears in viruses and cellular organisms
Synonyms
(r)-imine reductase, (r)-ired, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(R)-imine reductase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(R)-2-methylpyrrolidine + NADP+ = 2-methyl-1-pyrroline + NADPH + H+
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
(R)-2-methylpyrrolidine:NADP+ 2-oxidoreductase
The enzyme from the bacterium Streptomyces sp. GF3587 is highly specific for its substrate and forms only the (R) isomer.
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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
1,1,2,3-tetramethyl-1H-benzo[e]indol-3-ium iodide + NADPH + H+
(-)-1,1,2,3-tetramethyl-2,3-dihydro-1H-benzo[e]indole + NADP+ + hydrogen iodide
-
-
-
-
?
1,2,3,3,5-pentamethyl-3H-indol-1-ium iodide + NADPH + H+
(2S)-1,2,3,3,5-pentamethyl-2,3-dihydro-1H-indole + NADP+ + hydrogen iodide
-
-
-
-
?
1,2,3,3-tetramethyl-3H-indol-1-ium iodide + NADPH + H+
(2S)-1,2,3,3-tetramethyl-2,3-dihydro-1H-indole + NADP+ + hydrogen iodide
-
-
-
-
?
1,2-dimethyl-3,4-dihydroisoquinolin-2-ium + NADPH + H+
(1R)-1,2-dimethyl-1,2,3,4-tetrahydroisoquinoline + NADP+
-
-
-
?
1-ethyl-2,3,3-trimethyl-3H-indol-1-ium iodide + NADPH + H+
(2S)-1-ethyl-2,3,3-trimethyl-2,3-dihydro-1H-indole + NADP+ + hydrogen iodide
-
-
-
-
?
1-methyl-3,4-dihydroisoquinoline + NADPH + H+
(1R)-1-methyl-1,2,3,4-tetrahydroisoquinoline + NADP+
over 98% enantiomeric excess
-
-
?
1-methyl-3,4-dihydroisoquinoline + NADPH + H+
(1S)-1-methyl-1,2,3,4-tetrahydroisoquinoline + NADP+
-
-
-
-
?
2,3,3,5-tetramethyl-3H-indole + NADPH + H+
(2R)-2,3,3,5-tetramethyl-2,3-dihydro-1H-indole + NADP+
-
-
-
-
?
2,3,3-trimethyl-1-propyl-3H-indol-1-ium iodide + NADPH + H+
(2S)-2,3,3-trimethyl-1-propyl-2,3-dihydro-1H-indole + NADP+ + hydrogen iodide
-
-
-
-
?
2,3,3-trimethyl-3H-indole + NADPH + H+
(2R)-2,3,3-trimethyl-2,3-dihydro-1H-indole + NADP+
-
-
-
-
?
2,3,3-trimethyl-5-(trifluoromethyl)-3H-indole + NADH + H+
(2R)-2,3,3-trimethyl-5-(trifluoromethyl)-2,3-dihydro-1H-indole + NADP+
-
-
-
-
?
2,3,3-trimethyl-5-nitro-3H-indole + NADPH + H+
(2R)-2,3,3-trimethyl-5-nitro-2,3-dihydro-1H-indole + NADP+
-
-
-
-
?
2,3,3-trimethylindolenine + NADPH + H+
(R)-2,3,3-trimethylindoline + NADP+
-
conversion rate of over 81% and enantiomeric excess of also over 96% for the (R)-isomer
-
-
?
2-cyclohexyl-1-pyrroline + NADPH + H+
(2S)-2-cyclohexylpyrrolidine + NADP+
significant reduction in enantioselectivity is observed with this bulkier substituent compared to 2-methyl-1-pyrroline
-
-
?
2-methyl-1-pyrroline + NADPH + H+
(R)-2-methylpyrrolidine + (S)-2-methylpyrrolidine + NADP+
2-methyl-3,4-dihydroisoquinolin-2-ium + NADPH + H+
2-methyl-1,2,3,4-tetrahydroisoquinoline + NADP+
-
-
-
?
3,4-dihydroisoquinoline + NADPH + H+
1,2,3,4-tetrahydroisoquinoline + NADP+
-
-
-
?
4,6-difluoro-2,3,3-trimethyl-3H-indole + NADPH + H+
(2R)-4,6-difluoro-2,3,3-trimethyl-2,3-dihydro-1H-indole + NADP+
-
-
-
-
?
5-(4-fluorophenyl)-3,4-dihydro-2H-pyrrole + NADPH + H+
(2S)-2-(4-fluorophenyl)pyrrolidine + NADP+
-
-
-
?
5-(4-methoxyphenyl)-3,4-dihydro-2H-pyrrole + NADPH + H+
(2S)-2-(4-methoxyphenyl)pyrrolidine + NADP+
-
-
-
?
5-bromo-2,3,3-trimethyl-3H-indole + NADPH + H+
(2R)-5-bromo-2,3,3-trimethyl-2,3-dihydro-1H-indole + NADP+
-
-
-
-
?
5-chloro-2,3,3-trimethyl-3H-indole + NADPH + H+
(2R)-5-chloro-2,3,3-trimethyl-2,3-dihydro-1H-indole + NADP+
-
-
-
-
?
5-fluoro-1,2,3,3-tetramethyl-3H-indol-1-ium iodide + NADPH + H+
(2S)-5-fluoro-1,2,3,3-tetramethyl-2,3-dihydro-1H-indole + NADP+ + hydrogen iodide
-
-
-
-
?
5-fluoro-2,3,3-trimethyl-3H-indole + NADPH + H+
(2S)-2-phenylpyrrolidine + NADP+
-
-
-
-
?
5-methoxy-2,3,3-trimethyl-3H-indole + NADPH + H+
(2R)-5-methoxy-2,3,3-trimethyl-2,3-dihydro-1H-indole + NADP+
-
-
-
-
?
5-methyl-3,4-dihydro-2H-pyrrole + NADPH + H+
(2R)-2-methylpyrrolidine + NADP+
-
-
-
?
6-(2-methoxyphenyl)-2,3,4,5-tetrahydropyridine + NADPH + H+
(2S)-2-(2-methoxyphenyl)piperidine + NADP+
-
-
-
?
6-(3-methoxyphenyl)-2,3,4,5-tetrahydropyridine + NADPH + H+
(2S)-2-(3-methoxyphenyl)piperidine + NADP+
-
-
-
?
6-(4-fluorophenyl)-2,3,4,5-tetrahydropyridine + NADPH + H+
(2S)-2-(4-fluorophenyl)piperidine + NADP+
-
-
-
?
6-(4-methoxyphenyl)-2,3,4,5-tetrahydropyridine + NADPH + H+
(2S)-2-(4-methoxyphenyl)piperidine + NADP+
-
-
-
?
6-(4-methylphenyl)-2,3,4,5-tetrahydropyridine + NADPH + H+
(2S)-2-(4-methylphenyl)piperidine + NADP+
-
-
-
?
6-(naphthalen-2-yl)-2,3,4,5-tetrahydropyridine + NADPH + H+
(-)-2-(naphthalen-2-yl)piperidine + NADP+
-
-
-
?
6-(prop-1-en-2-yl)-2,3,4,5-tetrahydropyridine + NADPH + H+
(2S)-2-(prop-1-en-2-yl)piperidine + NADP+
-
-
-
?
6-(propan-2-yl)-2,3,4,5-tetrahydropyridine + NADPH + H+
(2S)-2-(propan-2-yl)piperidine + NADP+
-
-
-
?
6-(thiophen-2-yl)-2,3,4,5-tetrahydropyridine + NADPH + H+
(-)-2-(thiophen-2-yl)piperidine + NADP+
-
-
-
?
6-benzyl-2,3,4,5-tetrahydropyridine + NADPH + H+
(2S)-2-benzylpiperidine + NADP+
-
-
-
?
6-cyclohexyl-2,3,4,5-tetrahydropyridine + NADPH + H+
(-)-2-cyclohexylpiperidine + NADP+
-
-
-
?
6-methyl-2,3,4,5-tetrahydropyridine + NADPH + H+
(2R)-2-methylpiperidine + NADP+
-
-
-
?
6-methyl-2,3,4,5-tetrahydropyridine + NADPH + H+
(2S)-2-methylpiperidine + NADP+
-
-
-
-
?
6-phenyl-2,3,4,5-tetrahydropyridine + NADPH + H+
(2S)-2-phenylpiperidine + NADP+
-
-
-
?
6-propyl-2,3,4,5-tetrahydropyridine + NADPH + H+
(2R)-2-propylpiperidine + NADP+
-
-
-
?
2-methyl-1-pyrroline + NADPH + H+
(R)-2-methylpyrrolidine + (S)-2-methylpyrrolidine + NADP+
-
-
the enzyme produces 27.5 mM (S)-2-methylpyrrolidine (92.3% e.e.) from 30 mM 2-methyl-1-pyrroline at 92.3% conversion in the presence of 2% (w/v) L-glucose after 72 h incubation, the enzyme produces 91 mM (R)-2-methylpyrrolidine with 99.2% e.e. and 27.5 mM (S)-2-methylpyrrolidine (92.3% e.e.) from 100 mM 2-methyl-1-pyrroline at 9192% conversion in the presence of 2% (w/v) L-glucose, respectively, after 84 h incubation
-
?
2-methyl-1-pyrroline + NADPH + H+
(R)-2-methylpyrrolidine + (S)-2-methylpyrrolidine + NADP+
-
-
the enzyme produces 27.5 mM (S)-2-methylpyrrolidine (92.3% e.e.) from 30 mM 2-methyl-1-pyrroline at 92.3% conversion in the presence of 2% (w/v) L-glucose after 72 h incubation, the enzyme produces 91 mM (R)-2-methylpyrrolidine with 99.2% e.e. and 27.5 mM (S)-2-methylpyrrolidine (92.3% e.e.) from 100 mM 2-methyl-1-pyrroline at 9192% conversion in the presence of 2% (w/v) L-glucose, respectively, after 84 h incubation
-
?
2-methyl-1-pyrroline + NADPH + H+
(R)-2-methylpyrrolidine + NADP+
-
-
-
-
?
2-methyl-1-pyrroline + NADPH + H+
(R)-2-methylpyrrolidine + NADP+
-
the enzyme is very specific for 2-methyl-1-pyrroline as substrate. The purified enzyme catalyzes the formation of (R)-2-methylpyrrolidine with 99% enantiomeric excess. The enzyme shows also oxidation activity for (R)-2-methyl-1-pyrroline under alkaline pH (10-11.5) conditions. No activity with (S)-2-methylpyrrolidine. No activity with NADH
-
-
r
2-methyl-1-pyrroline + NADPH + H+
(R)-2-methylpyrrolidine + NADP+
-
-
-
?
2-methyl-1-pyrroline + NADPH + H+
(R)-2-methylpyrrolidine + NADP+
enantioselective reaction, the enzyme produces only the (R)-isomer, conversion rate of over 98% and enantiomeric excess of also over 98%
-
-
?
2-phenyl-1-pyrroline + NADPH + H+
(2S)-2-phenylpyrrolidine + NADP+
-
-
-
?
2-phenyl-1-pyrroline + NADPH + H+
(2S)-2-phenylpyrrolidine + NADP+
significant reduction in enantioselectivity is observed with this bulkier substituent compared to 2-methyl-1-pyrroline
-
-
?
additional information
?
-
-
the purified recombinant enzyme PlRIR exhibits relatively high catalytic efficiency towards 2,3,3-trimethylindolenine. A panel of 3H-indoles and 3H-indole iodides are reduced by PlRIR to yield the corresponding products with high enantioselectivity of 66-98% enantiomeric excess. In addition, enzyme PlRIR also possesses good activities toward other types of imines such as pyrroline, tetrahydropyridine, and dihydroisoquinoline, indicating a reasonably broad substrate acceptance
-
-
?
additional information
?
-
-
no activity with DELTA1-pyrroline-2-carboxylate, methyl-DELTA1-pyrroline-2-carboxylate, dihydrofolate, DELTA1-piperidine-2-carboxylate, 1-methyl-3,4-dihydroisoquinoline, 1-methyl-6,7-dimethoxy-3,4-dihydroisoquinoline, N-benzylidenebenzylamine, (E)-N-(1-phenylethylidene)benzeneamine ketone, 4-hydroxy-2-butanone, ethyl-3-oxobutanoate, ethyl 4-chloro-3-oxobutanoate, 3-2,2,6-trimethyl-2-cyclohexen-1,4-dione, 2-methylfuran, 2-methylimidazole, 2-methylthiazole, 2-methylpyrimidine, 2-methylpyrazine, 1,4,5,6-tetrahydropyrimidine
-
-
?
additional information
?
-
analysis of the enzyme substrate specificity, overview. Enzyme (R)-IRED catalyzes the reduction of pyrrolines containing both aliphatic and aromatic substituents at C-2. When a para-methoxy substituent is introduced on the benzene ring, conversion falls to 20% but the reaction proceeds with excellent selectivity to give (S)-2c in over 98% enantiomeric excess
-
-
?
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NATURAL SUBSTRATE
NATURAL 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
2-methyl-1-pyrroline + NADPH + H+
(R)-2-methylpyrrolidine + (S)-2-methylpyrrolidine + NADP+
2-methyl-1-pyrroline + NADPH + H+
(R)-2-methylpyrrolidine + (S)-2-methylpyrrolidine + NADP+
-
-
the enzyme produces 27.5 mM (S)-2-methylpyrrolidine (92.3% e.e.) from 30 mM 2-methyl-1-pyrroline at 92.3% conversion in the presence of 2% (w/v) L-glucose after 72 h incubation, the enzyme produces 91 mM (R)-2-methylpyrrolidine with 99.2% e.e. and 27.5 mM (S)-2-methylpyrrolidine (92.3% e.e.) from 100 mM 2-methyl-1-pyrroline at 9192% conversion in the presence of 2% (w/v) L-glucose, respectively, after 84 h incubation
-
?
2-methyl-1-pyrroline + NADPH + H+
(R)-2-methylpyrrolidine + (S)-2-methylpyrrolidine + NADP+
-
-
the enzyme produces 27.5 mM (S)-2-methylpyrrolidine (92.3% e.e.) from 30 mM 2-methyl-1-pyrroline at 92.3% conversion in the presence of 2% (w/v) L-glucose after 72 h incubation, the enzyme produces 91 mM (R)-2-methylpyrrolidine with 99.2% e.e. and 27.5 mM (S)-2-methylpyrrolidine (92.3% e.e.) from 100 mM 2-methyl-1-pyrroline at 9192% conversion in the presence of 2% (w/v) L-glucose, respectively, after 84 h incubation
-
?
2-methyl-1-pyrroline + NADPH + H+
(R)-2-methylpyrrolidine + NADP+
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
no inhibition: EDTA, Tiron, CaCl2, CdCl2, CoCl2, FeCl3, LiOH, MgCl2, NiCl2, ZnSO4, semicarbazide, diethylamine cysteamine, 3-(aminomethyl)pyridine, iodoacetate, (R)-(+)-cycloserine, diethyldithiocarbamiate, N-ethylmaleimide
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
not activated by glycerol, sorbitol, or 2-propanal
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.155
1-methyl-3,4-dihydroisoquinoline
recombinant enzyme, pH and temperature not specified in the publication
0.481
2-methyl-3,4-dihydroisoquinolin-2-ium
recombinant enzyme, pH and temperature not specified in the publication
0.317
3,4-dihydroisoquinoline
recombinant enzyme, pH and temperature not specified in the publication
1.05
6-(4-methoxyphenyl)-2,3,4,5-tetrahydropyridine
recombinant enzyme, pH and temperature not specified in the publication
1.77
6-(prop-1-en-2-yl)-2,3,4,5-tetrahydropyridine
recombinant enzyme, pH and temperature not specified in the publication
0.244
6-(thiophen-2-yl)-2,3,4,5-tetrahydropyridine
recombinant enzyme, pH and temperature not specified in the publication
1.55
6-cyclohexyl-2,3,4,5-tetrahydropyridine
recombinant enzyme, pH and temperature not specified in the publication
0.371
6-methyl-2,3,4,5-tetrahydropyridine
recombinant enzyme, pH and temperature not specified in the publication
5.22
6-phenyl-2,3,4,5-tetrahydropyridine
recombinant enzyme, pH and temperature not specified in the publication
0.804
6-propyl-2,3,4,5-tetrahydropyridine
recombinant enzyme, pH and temperature not specified in the publication
1.88
2-methyl-1-pyrroline
recombinant enzyme, pH and temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.189
1-methyl-3,4-dihydroisoquinoline
recombinant enzyme, pH and temperature not specified in the publication
0.351
2-methyl-1-pyrroline
recombinant enzyme, pH and temperature not specified in the publication
1.057
2-methyl-3,4-dihydroisoquinolin-2-ium
recombinant enzyme, pH and temperature not specified in the publication
0.141
3,4-dihydroisoquinoline
recombinant enzyme, pH and temperature not specified in the publication
0.263
6-(4-methoxyphenyl)-2,3,4,5-tetrahydropyridine
recombinant enzyme, pH and temperature not specified in the publication
2.35
6-(prop-1-en-2-yl)-2,3,4,5-tetrahydropyridine
recombinant enzyme, pH and temperature not specified in the publication
0.643
6-(thiophen-2-yl)-2,3,4,5-tetrahydropyridine
recombinant enzyme, pH and temperature not specified in the publication
0.0215
6-cyclohexyl-2,3,4,5-tetrahydropyridine
recombinant enzyme, pH and temperature not specified in the publication
4.21
6-methyl-2,3,4,5-tetrahydropyridine
recombinant enzyme, pH and temperature not specified in the publication
3.64
6-phenyl-2,3,4,5-tetrahydropyridine
recombinant enzyme, pH and temperature not specified in the publication
4.63
6-propyl-2,3,4,5-tetrahydropyridine
recombinant enzyme, pH and temperature not specified in the publication
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.22
1-methyl-3,4-dihydroisoquinoline
recombinant enzyme, pH and temperature not specified in the publication
0.187
2-methyl-1-pyrroline
recombinant enzyme, pH and temperature not specified in the publication
2.195
2-methyl-3,4-dihydroisoquinolin-2-ium
recombinant enzyme, pH and temperature not specified in the publication
0.447
3,4-dihydroisoquinoline
recombinant enzyme, pH and temperature not specified in the publication
0.25
6-(4-methoxyphenyl)-2,3,4,5-tetrahydropyridine
recombinant enzyme, pH and temperature not specified in the publication
1.33
6-(prop-1-en-2-yl)-2,3,4,5-tetrahydropyridine
recombinant enzyme, pH and temperature not specified in the publication
2.64
6-(thiophen-2-yl)-2,3,4,5-tetrahydropyridine
recombinant enzyme, pH and temperature not specified in the publication
0.0139
6-cyclohexyl-2,3,4,5-tetrahydropyridine
recombinant enzyme, pH and temperature not specified in the publication
11.4
6-methyl-2,3,4,5-tetrahydropyridine
recombinant enzyme, pH and temperature not specified in the publication
0.698
6-phenyl-2,3,4,5-tetrahydropyridine
recombinant enzyme, pH and temperature not specified in the publication
5.76
6-propyl-2,3,4,5-tetrahydropyridine
recombinant enzyme, pH and temperature not specified in the publication
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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
10.2 - 11.7
-
pH 6.2: about 60% of maximal activity, pH 8.7: about 60% of maximal activity, oxidation of (R)-2-methylpyrrolidine
6.2 - 8.7
-
pH 6.2: about 35% of maximal activity, pH 8.7: about 55% of maximal activity, reduction of 2-methyl-1-pyrroline
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
construction of a homology model of the enzyme active site, based on the structure of a closely related (R)-IRED from Streptomyces kanamyceticus
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). REDAM_ASPOR
Aspergillus oryzae (strain ATCC 42149 / RIB 40)
295
0
31155
Swiss-Prot
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
construction of a homology model of the enzyme active site, based on the structure of a closely related (R)-IRED from Streptomyces kanamyceticus
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D172A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme and also reduced enantioselectivity depending on the substrate, overview
D172K
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme and also reduced enantioselectivity depending on the substrate, overview
additional information
creation of a recombinant whole-cell biocatalyst for the asymmetric reduction of prochiral imines by recombinant overexpression of the (R)-imine reductase from Streptomyces sp. GF3587 in Escherichia coli
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant N-terminally His-tagged enzyme from Escherichia coli strain BL21(DE3)
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant overexpression of N-terminally His-tagged enzyme in Escherichia coli strain BL21(DE3)
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
(R)-imine reductase is a biocatalyst for the asymmetric reduction of cyclic imines
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mitsukura, K.; Suzuki, M.; Shinoda, S.; Kuramoto, T.; Yoshida, T.; Nagasawa, T.
Purification and characterization of a novel (R)-imine reductase from Streptomyces sp. GF3587
Biosci. Biotechnol. Biochem.
75
1778-1782
2011
Streptomyces sp.
brenda
Mitsukura, K.; Suzuki, M.; Tada, K.; Yoshida, T.; Nagasawa, T.
Asymmetric synthesis of chiral cyclic amine from cyclic imine by bacterial whole-cell catalyst of enantioselective imine reductase
Org. Biomol. Chem.
8
4533-4535
2010
Streptomyces sp., Streptomyces sp. 3546
brenda
Hussain, S.; Leipold, F.; Man, H.; Wells, E.; France, S.P.; Mulholland, K.R.; Grogan, G.; Turner, N.J.
An (R)-imine reductase biocatalyst for the asymmetric reduction of cyclic imines
ChemCatChem
7
579-583
2015
Streptomyces sp. GF3587 (M4ZRJ3)
brenda
Li, H.; Zhang, G.; Li, L.; Ou, Y.; Wang, M.; Li, C.; Zheng, G.; Xu, J.
A novel (R)-imine reductase from Paenibacillus lactis for asymmetric reduction of 3H-indoles
ChemCatChem
8
724-727
2016
Paenibacillus lactis
-
brenda
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Release 2023.1 (January 2023)
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