BRENDA - Enzyme Database
show all sequences of 1.3.1.70

Microsomal enzymes of cholesterol biosynthesis from lanosterol. Characterization, solubilization, and partial purification of NADPH-dependent DELTA8,14-steroid 14-reductase

Paik, Y.K.; Trzaskos, J.M.; Shafiee, A.; Gaylor, J.L.; J. Biol. Chem. 259, 13413-13423 (1984)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
phosphatidylcholine
liposomal phosphatidylcholine, egg yolk: 1.4fold activation
Rattus norvegicus
Phospholipids
partially purified enzyme: activation
Rattus norvegicus
Application
Application
Commentary
Organism
analysis
partial purified enzyme suitable for reconstitution studies, reconstitution of isolated, soluble enzymes involved in cholesterol biosynthesis from lanosterol
Rattus norvegicus
General Stability
General Stability
Organism
detergents such as Lubrol-WX, Emulgen 911, Triton X-100, Triton WR-1339, and their combinations with ionic detergents such as taurodeoxycholate, cholate, and Na+ salts destroy enzyme even at low concentration, 0.1-0.5%, w/v
Rattus norvegicus
enzyme in soluble form is very instable
Rattus norvegicus
stable against trypsin treatment
Rattus norvegicus
Inhibitors
Inhibitors
Commentary
Organism
Structure
Ca2+
4 mM: very slight, 3.5% inhibition
Rattus norvegicus
cyanide
cyanide ion, membrane-bound enzyme, modest inhibition at high concentrations, greater than 1 mM, partial purified enzyme, sodium cyanide, no or very poor inhibition, 10 mM: 3.5% inhibition
Rattus norvegicus
HgCl2
3 mM: more than 99% inhibition, inhibition negligible in the presence of 10 mM glutathione
Rattus norvegicus
Mg2+
4 mM: slight, 6% inhibition
Rattus norvegicus
additional information
no direct inhibition by 3beta-hydroxy-4,4-dimethyl-5alpha-cholest-8(14)-en-15-one, even when concentration is increased to level of Km for substrate; no inhibition by trypsin
Rattus norvegicus
N-ethylmaleimide
5 mM: 53% inhibition, inhibition negligible in the presence of 10 mM glutathione
Rattus norvegicus
O2
28% inhibition
Rattus norvegicus
Phospholipase A2
very high inhibition by very small concentrations, activity not restored by addition of phospholipids or any components presumed to be released from treated microsomes. Various concentration ranges of potential cofactors including FMN, FAD, AMP, ADP, ATP, coenzyme Q, Coenzyme A, and hemin, plus heat-treated microsomes, and lipid extracts of microsomes does not restore microsomal 14-reductase of phospholipase A2-treated microsomes
Rattus norvegicus
sulfhydryl-binding agents
-
Rattus norvegicus
trans-1,4-bis(2-chlorobenzylaminomethyl)cyclohexane dihydrochloride
AY-9944, strong inhibition, 0.0003 mM: 50% inhibition, 0.0005 mM: 65% inhibition
Rattus norvegicus
Triparanol
4-chloro-alpha-[4-[2-diethylaminoethoxy]phenyl]-alpha-(4-methylphenyl)benze-methanol, slight inhibition
Rattus norvegicus
Tris-HCl
Tris-HCl buffer, 28% inhibition, not restored by addition of KCl at various concentrations
Rattus norvegicus
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
kinetic data; kinetics
Rattus norvegicus
0.0294
-
4,4-dimethyl-5alpha-cholesta-7,14-dien-3beta-ol
membrane-bound enzyme, Lineweaver-Burk
Rattus norvegicus
0.0333
-
4,4-dimethyl-5alpha-cholesta-7,14-dien-3beta-ol
soluble enzyme
Rattus norvegicus
0.0345
-
4,4-dimethyl-5alpha-cholesta-7,14-dien-3beta-ol
microsomal-bound enzyme
Rattus norvegicus
0.6
-
NADPH
membrane-bound enzyme
Rattus norvegicus
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
endoplasmic reticulum
-
Rattus norvegicus
5783
-
membrane
membrane-bound
Rattus norvegicus
16020
-
microsome
microsomal-bound
Rattus norvegicus
-
-
additional information
distribution
Rattus norvegicus
-
-
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
additional information
no activation by Mg2+ or Ca2+, 0.5-20 mM, but slight inhibition
Rattus norvegicus
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + NADPH
Rattus norvegicus
presumably the natural substrate
4,4-dimethyl-5alpha-cholesta-8-en-3beta-ol + NADP+
-
-
?
additional information
Rattus norvegicus
catalyzes anaerobically NADPH-dependent reduction of 14-double bond of 8,14-diene or 7,14-diene sterols that are sterol intermediates formed during C-32 demethylation in cholesterol biosynthesis from lanosterol in mammals
?
-
-
-
additional information
Rattus norvegicus
reduction of 14-double bond of sterol-conjugated dienes
?
-
-
-
additional information
Rattus norvegicus
microsomal enzyme of cholesterol biosynthesis from lanosterol
?
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Rattus norvegicus
-
male sprague-dawley rats
-
Purification (Commentary)
Commentary
Organism
solubilization with combined octylglucoside and sodium taurodeoxycholate system and partial purification
Rattus norvegicus
Reaction
Reaction
Commentary
Organism
4,4-dimethyl-5alpha-cholesta-8,24-dien-3beta-ol + NADP+ = 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + NADPH + H+
reduction of 14-double bond of conjugated DELTA8,14-sterols and DELTA7,14-sterols
Rattus norvegicus
Source Tissue
Source Tissue
Commentary
Organism
Textmining
liver
-
Rattus norvegicus
-
Specific Activity [micromol/min/mg]
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
0.0555
-
partially purified enzyme
Rattus norvegicus
Storage Stability
Storage Stability
Organism
-80C, 1 week, stable
Rattus norvegicus
4C, overnight, 30% activity lost
Rattus norvegicus
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
4,4-dimethyl-5alpha-cholesta-7,14-dien-3beta-ol + NADPH
64% activity compared with 4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol
288490
Rattus norvegicus
4,4-dimethyl-5alpha-cholesta-7-en-3beta-ol + NADP+
-
-
-
?
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + NADPH
best substrate, probably natural substrate
288490
Rattus norvegicus
4,4-dimethyl-5alpha-cholesta-8-en-3beta-ol + NADP+
-
-
-
?
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + NADPH
presumably the natural substrate
288490
Rattus norvegicus
4,4-dimethyl-5alpha-cholesta-8-en-3beta-ol + NADP+
-
-
-
?
5alpha-cholesta-7,14-dien-3beta-ol + NADPH
43% activity compared with 4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol
288490
Rattus norvegicus
5alpha-cholesta-7-en-3beta-ol + NADP+
-
-
-
?
5alpha-cholesta-8,14-dien-3beta-ol + NADPH
DELTA8,14-cholestadien-3beta-ol
288490
Rattus norvegicus
5alpha-cholesta-8-en-3beta-ol + NADP+
-
-
-
?
5alpha-cholesta-8,14-dien-3beta-ol + NADPH
53% activity compared with 4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol
288490
Rattus norvegicus
5alpha-cholesta-8-en-3beta-ol + NADP+
-
-
-
?
additional information
substrate specificity
288490
Rattus norvegicus
?
-
-
-
-
additional information
enzyme acts on a range of steroids with a 14(15)-double bond
288490
Rattus norvegicus
?
-
-
-
-
additional information
reduction of 14-double bond of conjugated DELTA8,14-diene sterols and DELTA7,14-diene sterols
288490
Rattus norvegicus
?
-
-
-
-
additional information
sterol substrate specificity study
288490
Rattus norvegicus
?
-
-
-
-
additional information
anaerobic conditions yield maximal rates of reduction
288490
Rattus norvegicus
?
-
-
-
-
additional information
4-nor-methyldiene sterols, 5alpha-cholesta-8,14-dien-3beta-ol, and 5alpha-cholesta-7,14-dien-3beta-ol are reduced at about 50% of the rate of the corresponding 4-gem-dimethyldiene sterols, for both the C27-sterol and C29-sterol, the higher reaction rate of the 8,14-diene system is consistently observed over the isomeric 7,14-diene
288490
Rattus norvegicus
?
-
-
-
-
additional information
catalyzes anaerobically NADPH-dependent reduction of 14-double bond of 8,14-diene or 7,14-diene sterols that are sterol intermediates formed during C-32 demethylation in cholesterol biosynthesis from lanosterol in mammals
288490
Rattus norvegicus
?
-
-
-
-
additional information
reduction of 14-double bond of sterol-conjugated dienes
288490
Rattus norvegicus
?
-
-
-
-
additional information
microsomal enzyme of cholesterol biosynthesis from lanosterol
288490
Rattus norvegicus
?
-
-
-
-
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
37
-
assay at, anaerobically
Rattus norvegicus
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.4
-
pH-optimum and assay at, anaerobically
Rattus norvegicus
pH Range
pH Minimum
pH Maximum
Commentary
Organism
additional information
-
14-reductase has relatively broad pH profile in acidic region, activity drastically decreases with only moderate elevation of pH above 7.8
Rattus norvegicus
7.8
-
14-reductase has relatively broad pH profile in acidic region, activity drastically decreases with only moderate elevation of pH above 7.8
Rattus norvegicus
Cofactor
Cofactor
Commentary
Organism
Structure
additional information
NADH only poorly supports reduction
Rattus norvegicus
NADPH
NADPH-dependent; NADPH required, NADH has 4.5%, of the NADPH activity
Rattus norvegicus
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
phosphatidylcholine
liposomal phosphatidylcholine, egg yolk: 1.4fold activation
Rattus norvegicus
Phospholipids
partially purified enzyme: activation
Rattus norvegicus
Application (protein specific)
Application
Commentary
Organism
analysis
partial purified enzyme suitable for reconstitution studies, reconstitution of isolated, soluble enzymes involved in cholesterol biosynthesis from lanosterol
Rattus norvegicus
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
additional information
NADH only poorly supports reduction
Rattus norvegicus
NADPH
NADPH-dependent; NADPH required, NADH has 4.5%, of the NADPH activity
Rattus norvegicus
General Stability (protein specific)
General Stability
Organism
detergents such as Lubrol-WX, Emulgen 911, Triton X-100, Triton WR-1339, and their combinations with ionic detergents such as taurodeoxycholate, cholate, and Na+ salts destroy enzyme even at low concentration, 0.1-0.5%, w/v
Rattus norvegicus
enzyme in soluble form is very instable
Rattus norvegicus
stable against trypsin treatment
Rattus norvegicus
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
Ca2+
4 mM: very slight, 3.5% inhibition
Rattus norvegicus
cyanide
cyanide ion, membrane-bound enzyme, modest inhibition at high concentrations, greater than 1 mM, partial purified enzyme, sodium cyanide, no or very poor inhibition, 10 mM: 3.5% inhibition
Rattus norvegicus
HgCl2
3 mM: more than 99% inhibition, inhibition negligible in the presence of 10 mM glutathione
Rattus norvegicus
Mg2+
4 mM: slight, 6% inhibition
Rattus norvegicus
additional information
no direct inhibition by 3beta-hydroxy-4,4-dimethyl-5alpha-cholest-8(14)-en-15-one, even when concentration is increased to level of Km for substrate; no inhibition by trypsin
Rattus norvegicus
N-ethylmaleimide
5 mM: 53% inhibition, inhibition negligible in the presence of 10 mM glutathione
Rattus norvegicus
O2
28% inhibition
Rattus norvegicus
Phospholipase A2
very high inhibition by very small concentrations, activity not restored by addition of phospholipids or any components presumed to be released from treated microsomes. Various concentration ranges of potential cofactors including FMN, FAD, AMP, ADP, ATP, coenzyme Q, Coenzyme A, and hemin, plus heat-treated microsomes, and lipid extracts of microsomes does not restore microsomal 14-reductase of phospholipase A2-treated microsomes
Rattus norvegicus
sulfhydryl-binding agents
-
Rattus norvegicus
trans-1,4-bis(2-chlorobenzylaminomethyl)cyclohexane dihydrochloride
AY-9944, strong inhibition, 0.0003 mM: 50% inhibition, 0.0005 mM: 65% inhibition
Rattus norvegicus
Triparanol
4-chloro-alpha-[4-[2-diethylaminoethoxy]phenyl]-alpha-(4-methylphenyl)benze-methanol, slight inhibition
Rattus norvegicus
Tris-HCl
Tris-HCl buffer, 28% inhibition, not restored by addition of KCl at various concentrations
Rattus norvegicus
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
kinetic data; kinetics
Rattus norvegicus
0.0294
-
4,4-dimethyl-5alpha-cholesta-7,14-dien-3beta-ol
membrane-bound enzyme, Lineweaver-Burk
Rattus norvegicus
0.0333
-
4,4-dimethyl-5alpha-cholesta-7,14-dien-3beta-ol
soluble enzyme
Rattus norvegicus
0.0345
-
4,4-dimethyl-5alpha-cholesta-7,14-dien-3beta-ol
microsomal-bound enzyme
Rattus norvegicus
0.6
-
NADPH
membrane-bound enzyme
Rattus norvegicus
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
endoplasmic reticulum
-
Rattus norvegicus
5783
-
membrane
membrane-bound
Rattus norvegicus
16020
-
microsome
microsomal-bound
Rattus norvegicus
-
-
additional information
distribution
Rattus norvegicus
-
-
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
additional information
no activation by Mg2+ or Ca2+, 0.5-20 mM, but slight inhibition
Rattus norvegicus
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + NADPH
Rattus norvegicus
presumably the natural substrate
4,4-dimethyl-5alpha-cholesta-8-en-3beta-ol + NADP+
-
-
?
additional information
Rattus norvegicus
catalyzes anaerobically NADPH-dependent reduction of 14-double bond of 8,14-diene or 7,14-diene sterols that are sterol intermediates formed during C-32 demethylation in cholesterol biosynthesis from lanosterol in mammals
?
-
-
-
additional information
Rattus norvegicus
reduction of 14-double bond of sterol-conjugated dienes
?
-
-
-
additional information
Rattus norvegicus
microsomal enzyme of cholesterol biosynthesis from lanosterol
?
-
-
-
Purification (Commentary) (protein specific)
Commentary
Organism
solubilization with combined octylglucoside and sodium taurodeoxycholate system and partial purification
Rattus norvegicus
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
liver
-
Rattus norvegicus
-
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
0.0555
-
partially purified enzyme
Rattus norvegicus
Storage Stability (protein specific)
Storage Stability
Organism
-80C, 1 week, stable
Rattus norvegicus
4C, overnight, 30% activity lost
Rattus norvegicus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
4,4-dimethyl-5alpha-cholesta-7,14-dien-3beta-ol + NADPH
64% activity compared with 4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol
288490
Rattus norvegicus
4,4-dimethyl-5alpha-cholesta-7-en-3beta-ol + NADP+
-
-
-
?
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + NADPH
best substrate, probably natural substrate
288490
Rattus norvegicus
4,4-dimethyl-5alpha-cholesta-8-en-3beta-ol + NADP+
-
-
-
?
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + NADPH
presumably the natural substrate
288490
Rattus norvegicus
4,4-dimethyl-5alpha-cholesta-8-en-3beta-ol + NADP+
-
-
-
?
5alpha-cholesta-7,14-dien-3beta-ol + NADPH
43% activity compared with 4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol
288490
Rattus norvegicus
5alpha-cholesta-7-en-3beta-ol + NADP+
-
-
-
?
5alpha-cholesta-8,14-dien-3beta-ol + NADPH
DELTA8,14-cholestadien-3beta-ol
288490
Rattus norvegicus
5alpha-cholesta-8-en-3beta-ol + NADP+
-
-
-
?
5alpha-cholesta-8,14-dien-3beta-ol + NADPH
53% activity compared with 4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol
288490
Rattus norvegicus
5alpha-cholesta-8-en-3beta-ol + NADP+
-
-
-
?
additional information
substrate specificity
288490
Rattus norvegicus
?
-
-
-
-
additional information
enzyme acts on a range of steroids with a 14(15)-double bond
288490
Rattus norvegicus
?
-
-
-
-
additional information
reduction of 14-double bond of conjugated DELTA8,14-diene sterols and DELTA7,14-diene sterols
288490
Rattus norvegicus
?
-
-
-
-
additional information
sterol substrate specificity study
288490
Rattus norvegicus
?
-
-
-
-
additional information
anaerobic conditions yield maximal rates of reduction
288490
Rattus norvegicus
?
-
-
-
-
additional information
4-nor-methyldiene sterols, 5alpha-cholesta-8,14-dien-3beta-ol, and 5alpha-cholesta-7,14-dien-3beta-ol are reduced at about 50% of the rate of the corresponding 4-gem-dimethyldiene sterols, for both the C27-sterol and C29-sterol, the higher reaction rate of the 8,14-diene system is consistently observed over the isomeric 7,14-diene
288490
Rattus norvegicus
?
-
-
-
-
additional information
catalyzes anaerobically NADPH-dependent reduction of 14-double bond of 8,14-diene or 7,14-diene sterols that are sterol intermediates formed during C-32 demethylation in cholesterol biosynthesis from lanosterol in mammals
288490
Rattus norvegicus
?
-
-
-
-
additional information
reduction of 14-double bond of sterol-conjugated dienes
288490
Rattus norvegicus
?
-
-
-
-
additional information
microsomal enzyme of cholesterol biosynthesis from lanosterol
288490
Rattus norvegicus
?
-
-
-
-
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
37
-
assay at, anaerobically
Rattus norvegicus
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.4
-
pH-optimum and assay at, anaerobically
Rattus norvegicus
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
additional information
-
14-reductase has relatively broad pH profile in acidic region, activity drastically decreases with only moderate elevation of pH above 7.8
Rattus norvegicus
7.8
-
14-reductase has relatively broad pH profile in acidic region, activity drastically decreases with only moderate elevation of pH above 7.8
Rattus norvegicus
Other publictions for EC 1.3.1.70
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)
746161
Huang
Fackel interacts with gibbere ...
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3
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2
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1
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1
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-
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2
-
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744648
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Impaired cell proliferation i ...
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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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1
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1
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1
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2
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745882
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Structure of an integral memb ...
Methylomicrobium alcaliphilum 20Z, Methylomicrobium alcaliphilum
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6
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