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Information on EC 1.5.1.48 - 2-methyl-1-pyrroline reductase
for references in articles please use BRENDA:EC1.5.1.48
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EC Tree 1 Oxidoreductases
1.5 Acting on the CH-NH group of donors
1.5.1 With NAD+ or NADP+ as acceptor
1.5.1.48 2-methyl-1-pyrroline reductase
IUBMB Comments
The enzyme from the bacterium Streptomyces sp. GF3587 is highly specific for its substrate and forms only the (R) isomer.
The enzyme appears in viruses and cellular organisms
showSynonyms
(r)-imine reductase, (r)-ired, more
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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
LITERATURE
COMMENTARY
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
-
Substrates: -
Products: -
Products: -
?
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
-
Substrates: -
Products: -
Products: -
?
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
-
Substrates: -
Products: -
Products: -
?
1,2-dimethyl-3,4-dihydroisoquinolin-2-ium + NADPH + H+
(1R)-1,2-dimethyl-1,2,3,4-tetrahydroisoquinoline + NADP+
Substrates: -
Products: -
Products: -
?
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
-
Substrates: -
Products: -
Products: -
?
1-methyl-3,4-dihydroisoquinoline + NADPH + H+
(1R)-1-methyl-1,2,3,4-tetrahydroisoquinoline + NADP+
Substrates: over 98% enantiomeric excess
Products: -
Products: -
?
1-methyl-3,4-dihydroisoquinoline + NADPH + H+
(1S)-1-methyl-1,2,3,4-tetrahydroisoquinoline + NADP+
-
Substrates: -
Products: -
Products: -
?
2,3,3,5-tetramethyl-3H-indole + NADPH + H+
(2R)-2,3,3,5-tetramethyl-2,3-dihydro-1H-indole + NADP+
-
Substrates: -
Products: -
Products: -
?
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
-
Substrates: -
Products: -
Products: -
?
2,3,3-trimethyl-3H-indole + NADPH + H+
(2R)-2,3,3-trimethyl-2,3-dihydro-1H-indole + NADP+
-
Substrates: -
Products: -
Products: -
?
2,3,3-trimethyl-5-(trifluoromethyl)-3H-indole + NADH + H+
(2R)-2,3,3-trimethyl-5-(trifluoromethyl)-2,3-dihydro-1H-indole + NADP+
-
Substrates: -
Products: -
Products: -
?
2,3,3-trimethyl-5-nitro-3H-indole + NADPH + H+
(2R)-2,3,3-trimethyl-5-nitro-2,3-dihydro-1H-indole + NADP+
-
Substrates: -
Products: -
Products: -
?
2,3,3-trimethylindolenine + NADPH + H+
(R)-2,3,3-trimethylindoline + NADP+
-
Substrates: conversion rate of over 81% and enantiomeric excess of also over 96% for the (R)-isomer
Products: -
Products: -
?
2-cyclohexyl-1-pyrroline + NADPH + H+
(2S)-2-cyclohexylpyrrolidine + NADP+
Substrates: significant reduction in enantioselectivity is observed with this bulkier substituent compared to 2-methyl-1-pyrroline
Products: -
Products: -
?
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+
Substrates: -
Products: -
Products: -
?
3,4-dihydroisoquinoline + NADPH + H+
1,2,3,4-tetrahydroisoquinoline + NADP+
Substrates: -
Products: -
Products: -
?
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+
-
Substrates: -
Products: -
Products: -
?
5-(4-fluorophenyl)-3,4-dihydro-2H-pyrrole + NADPH + H+
(2S)-2-(4-fluorophenyl)pyrrolidine + NADP+
Substrates: -
Products: -
Products: -
?
5-(4-methoxyphenyl)-3,4-dihydro-2H-pyrrole + NADPH + H+
(2S)-2-(4-methoxyphenyl)pyrrolidine + NADP+
Substrates: -
Products: -
Products: -
?
5-bromo-2,3,3-trimethyl-3H-indole + NADPH + H+
(2R)-5-bromo-2,3,3-trimethyl-2,3-dihydro-1H-indole + NADP+
-
Substrates: -
Products: -
Products: -
?
5-chloro-2,3,3-trimethyl-3H-indole + NADPH + H+
(2R)-5-chloro-2,3,3-trimethyl-2,3-dihydro-1H-indole + NADP+
-
Substrates: -
Products: -
Products: -
?
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
-
Substrates: -
Products: -
Products: -
?
5-fluoro-2,3,3-trimethyl-3H-indole + NADPH + H+
(2S)-2-phenylpyrrolidine + NADP+
-
Substrates: -
Products: -
Products: -
?
5-methoxy-2,3,3-trimethyl-3H-indole + NADPH + H+
(2R)-5-methoxy-2,3,3-trimethyl-2,3-dihydro-1H-indole + NADP+
-
Substrates: -
Products: -
Products: -
?
5-methyl-3,4-dihydro-2H-pyrrole + NADPH + H+
(2R)-2-methylpyrrolidine + NADP+
Substrates: -
Products: -
Products: -
?
6-(2-methoxyphenyl)-2,3,4,5-tetrahydropyridine + NADPH + H+
(2S)-2-(2-methoxyphenyl)piperidine + NADP+
Substrates: -
Products: -
Products: -
?
6-(3-methoxyphenyl)-2,3,4,5-tetrahydropyridine + NADPH + H+
(2S)-2-(3-methoxyphenyl)piperidine + NADP+
Substrates: -
Products: -
Products: -
?
6-(4-fluorophenyl)-2,3,4,5-tetrahydropyridine + NADPH + H+
(2S)-2-(4-fluorophenyl)piperidine + NADP+
Substrates: -
Products: -
Products: -
?
6-(4-methoxyphenyl)-2,3,4,5-tetrahydropyridine + NADPH + H+
(2S)-2-(4-methoxyphenyl)piperidine + NADP+
Substrates: -
Products: -
Products: -
?
6-(4-methylphenyl)-2,3,4,5-tetrahydropyridine + NADPH + H+
(2S)-2-(4-methylphenyl)piperidine + NADP+
Substrates: -
Products: -
Products: -
?
6-(naphthalen-2-yl)-2,3,4,5-tetrahydropyridine + NADPH + H+
(-)-2-(naphthalen-2-yl)piperidine + NADP+
Substrates: -
Products: -
Products: -
?
6-(prop-1-en-2-yl)-2,3,4,5-tetrahydropyridine + NADPH + H+
(2S)-2-(prop-1-en-2-yl)piperidine + NADP+
Substrates: -
Products: -
Products: -
?
6-(propan-2-yl)-2,3,4,5-tetrahydropyridine + NADPH + H+
(2S)-2-(propan-2-yl)piperidine + NADP+
Substrates: -
Products: -
Products: -
?
6-(thiophen-2-yl)-2,3,4,5-tetrahydropyridine + NADPH + H+
(-)-2-(thiophen-2-yl)piperidine + NADP+
Substrates: -
Products: -
Products: -
?
6-benzyl-2,3,4,5-tetrahydropyridine + NADPH + H+
(2S)-2-benzylpiperidine + NADP+
Substrates: -
Products: -
Products: -
?
6-cyclohexyl-2,3,4,5-tetrahydropyridine + NADPH + H+
(-)-2-cyclohexylpiperidine + NADP+
Substrates: -
Products: -
Products: -
?
6-methyl-2,3,4,5-tetrahydropyridine + NADPH + H+
(2R)-2-methylpiperidine + NADP+
Substrates: -
Products: -
Products: -
?
6-methyl-2,3,4,5-tetrahydropyridine + NADPH + H+
(2S)-2-methylpiperidine + NADP+
-
Substrates: -
Products: -
Products: -
?
6-phenyl-2,3,4,5-tetrahydropyridine + NADPH + H+
(2S)-2-phenylpiperidine + NADP+
Substrates: -
Products: -
Products: -
?
6-propyl-2,3,4,5-tetrahydropyridine + NADPH + H+
(2R)-2-propylpiperidine + NADP+
Substrates: -
Products: -
Products: -
?
2-methyl-1-pyrroline + NADPH + H+
(R)-2-methylpyrrolidine + (S)-2-methylpyrrolidine + NADP+
-
Substrates: -
Products: 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
Products: 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
?
2-methyl-1-pyrroline + NADPH + H+
(R)-2-methylpyrrolidine + (S)-2-methylpyrrolidine + NADP+
-
Substrates: -
Products: 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 91Ā92% conversion in the presence of 2% (w/v) L-glucose, respectively, after 84 h incubation
Products: 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 91Ā92% 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+
-
Substrates: -
Products: 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
Products: 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
?
2-methyl-1-pyrroline + NADPH + H+
(R)-2-methylpyrrolidine + (S)-2-methylpyrrolidine + NADP+
-
Substrates: -
Products: 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 91Ā92% conversion in the presence of 2% (w/v) L-glucose, respectively, after 84 h incubation
Products: 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 91Ā92% 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+
-
Substrates: -
Products: -
Products: -
?
2-methyl-1-pyrroline + NADPH + H+
(R)-2-methylpyrrolidine + NADP+
-
Substrates: -
Products: -
Products: -
r
2-methyl-1-pyrroline + NADPH + H+
(R)-2-methylpyrrolidine + NADP+
-
Substrates: 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
Products: -
Products: -
r
2-methyl-1-pyrroline + NADPH + H+
(R)-2-methylpyrrolidine + NADP+
Substrates: -
Products: -
Products: -
?
2-methyl-1-pyrroline + NADPH + H+
(R)-2-methylpyrrolidine + NADP+
Substrates: enantioselective reaction, the enzyme produces only the (R)-isomer, conversion rate of over 98% and enantiomeric excess of also over 98%
Products: -
Products: -
?
2-phenyl-1-pyrroline + NADPH + H+
(2S)-2-phenylpyrrolidine + NADP+
Substrates: -
Products: -
Products: -
?
2-phenyl-1-pyrroline + NADPH + H+
(2S)-2-phenylpyrrolidine + NADP+
Substrates: significant reduction in enantioselectivity is observed with this bulkier substituent compared to 2-methyl-1-pyrroline
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
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+
-
Substrates: -
Products: 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
Products: 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
?
2-methyl-1-pyrroline + NADPH + H+
(R)-2-methylpyrrolidine + (S)-2-methylpyrrolidine + NADP+
-
Substrates: -
Products: 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 91Ā92% conversion in the presence of 2% (w/v) L-glucose, respectively, after 84 h incubation
Products: 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 91Ā92% 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+
-
Substrates: -
Products: 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
Products: 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
?
2-methyl-1-pyrroline + NADPH + H+
(R)-2-methylpyrrolidine + (S)-2-methylpyrrolidine + NADP+
-
Substrates: -
Products: 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 91Ā92% conversion in the presence of 2% (w/v) L-glucose, respectively, after 84 h incubation
Products: 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 91Ā92% 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+
-
Substrates: -
Products: -
Products: -
r
2-methyl-1-pyrroline + NADPH + H+
(R)-2-methylpyrrolidine + NADP+
Substrates: -
Products: -
Products: -
?
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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
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
EXTERNAL LINKS (specific for EC-Number 1.5.1.48)
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Release 2023.1 (January 2023)
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