Information on EC 1.1.1.88 - hydroxymethylglutaryl-CoA reductase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY
1.1.1.88
-
RECOMMENDED NAME
GeneOntology No.
hydroxymethylglutaryl-CoA reductase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
(R)-mevalonate + CoA + 2 NAD+ = 3-hydroxy-3-methylglutaryl-CoA + 2 NADH + 2 H+
show the reaction diagram
reaction mechanism purposal
-
(R)-mevalonate + CoA + 2 NAD+ = 3-hydroxy-3-methylglutaryl-CoA + 2 NADH + 2 H+
show the reaction diagram
There are two classes of enzyme, the third enzyme of the mevalonate pathway of isopentenyl diphosphate biosynthesis: the class I enzymes of eukaryotes and the class II enzymes of certain eubacteria
-
(R)-mevalonate + CoA + 2 NAD+ = 3-hydroxy-3-methylglutaryl-CoA + 2 NADH + 2 H+
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
-
-
-
-
oxidative acylation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
reductive deacylation
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
-
mevalonate degradation
-
Terpenoid backbone biosynthesis
-
SYSTEMATIC NAME
IUBMB Comments
(R)-mevalonate:NAD+ oxidoreductase (CoA-acylating)
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3-hydroxy-3-methylglutaryl CoA reductase 1
-
-
3-hydroxy-3-methylglutaryl coenzyme A reductase
-
-
-
-
beta-hydroxy-beta-methylglutaryl CoA-reductase
-
-
-
-
beta-hydroxy-beta-methylglutaryl coenzyme A reductase
-
-
-
-
HMG-CoA reductase
-
-
-
-
HMG-CoA reductase
-
-
HMG-CoA reductase
-
-
HMG-CoA reductase
-
-
hydroxymethylglutaryl coenzyme A reductase
-
-
-
-
NADH-dependent HMG-CoA reductase
-
-
CAS REGISTRY NUMBER
COMMENTARY
37250-24-1
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
chinese hamster
-
-
Manually annotated by BRENDA team
Mycobacterium sp. s4
S4
-
-
Manually annotated by BRENDA team
formerly Pseudomonas sp. M
-
-
Manually annotated by BRENDA team
a transgenic potato cell culture system expressing an epitope-tagged enzyme
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
physiological function
-
HMG-CoAR increase is crucial for muscle differentiation induction. p21waf, whose increase is a necessary requisite for differentiation to occur, rises downstream HMG-CoAR activation, while p38/MAPK has a role as key regulator also for HMG-CoAR
additional information
-
sequence comparisons of several species with class II and class I HMG-CoA reductases for analysis of cofactor binding, overview
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(R)-mevalonate + CoA + 2 NAD+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADH + 2 H+
show the reaction diagram
-
-
-
-
?
(R)-mevalonate + CoA + 2 NAD+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADH + 2 H+
show the reaction diagram
-
-
-
-
?
(R)-mevalonate + CoA + 2 NAD+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADH + 2 H+
show the reaction diagram
-
-
-
-
-
(R)-mevalonate + CoA + 2 NAD+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADH + 2 H+
show the reaction diagram
-
-
-
-
r
(R)-mevalonate + CoA + 2 NAD+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADH + 2 H+
show the reaction diagram
-
with mevalonate as sole source of carbon enzyme acts as a biodegradative enzyme
-
-
-
(R)-mevalonate + CoA + 2 NAD+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADH + 2 H+
show the reaction diagram
-
with mevalonate as sole source of carbon enzyme acts as a biodegradative enzyme
-
-
r
(R)-mevalonate + CoA + 2 NAD+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADH + 2 H+
show the reaction diagram
Mycobacterium sp. s4
-
-
-
-
?
(R)-mevalonate + CoA + 2 NAD+
3-hydroxy-3-methylglutaryl-CoA + 2 NADH + 2 H+
show the reaction diagram
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + NADH + H+
(R)-mevalonate + NAD+ + CoA
show the reaction diagram
-
-
-
-
-
(S)-3-hydroxy-3-methylglutaryl-CoA + NADH + H+
(R)-mevalonate + NAD+ + CoA
show the reaction diagram
-
mevalonate is required for cholesterol and isoprenoid synthesis
-
-
-
(S)-3-hydroxy-3-methylglutaryl-CoA + NADH + H+
(R)-mevalonate + NAD+ + CoA
show the reaction diagram
-
mevalonate is first commited intermediate in polyisoprenoid synthesis
-
-
-
3-hydroxy-3-methyl-glutaryl-CoA + NADH + H+
mevalonate + CoA + NAD+
show the reaction diagram
-
-
-
-
?
3-hydroxy-3-methyl-glutaryl-CoA + NADH + H+
mevalonate + CoA + NAD+
show the reaction diagram
-
-, mevalonate pathway
-
-
?
3-hydroxy-3-methylglutaryl-CoA + NADH + H+
mevalonate + CoA + NAD+
show the reaction diagram
-
-
-
-
-
3-hydroxy-3-methylglutaryl-CoA + NADH + H+
mevalonate + CoA + NAD+
show the reaction diagram
-
-
-
-
r
additional information
?
-
-
oxidative acylation of mevalonate: the carboxy-, 3-methyl-, and 3-hydroxy groups are essential for substrate binding to the enzyme
-
-
-
additional information
?
-
-
oxidative acylation of mevalonate: the carboxy-, 3-methyl-, and 3-hydroxy groups are essential for substrate binding to the enzyme
-
-
-
additional information
?
-
-
The biosynthetic pathway leading to plant cytosolic isoprenoids begins with the 3-hydroxy-3-methyl-glutaryl CoA reductase-mediated production of mevalonate
-
-
-
additional information
?
-
-
The enzyme can play a role in indole alkaloid biosynthesis and a possible cosuppression of both the endogenous and foreign enzyme genes in clone 236
-
-
-
additional information
?
-
Mycobacterium sp. s4
-
oxidative acylation of mevalonate: the carboxy-, 3-methyl-, and 3-hydroxy groups are essential for substrate binding to the enzyme
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(R)-mevalonate + CoA + 2 NAD+
3-hydroxy-3-methylglutaryl-CoA + 2 NADH + 2 H+
show the reaction diagram
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + NADH + H+
(R)-mevalonate + NAD+ + CoA
show the reaction diagram
-
-
-
-
-
(S)-3-hydroxy-3-methylglutaryl-CoA + NADH + H+
(R)-mevalonate + NAD+ + CoA
show the reaction diagram
-
mevalonate is required for cholesterol and isoprenoid synthesis
-
-
-
(S)-3-hydroxy-3-methylglutaryl-CoA + NADH + H+
(R)-mevalonate + NAD+ + CoA
show the reaction diagram
-
mevalonate is first commited intermediate in polyisoprenoid synthesis
-
-
-
3-hydroxy-3-methyl-glutaryl-CoA + NADH + H+
mevalonate + CoA + NAD+
show the reaction diagram
-
mevalonate pathway
-
-
?
additional information
?
-
-
The biosynthetic pathway leading to plant cytosolic isoprenoids begins with the 3-hydroxy-3-methyl-glutaryl CoA reductase-mediated production of mevalonate
-
-
-
additional information
?
-
-
The enzyme can play a role in indole alkaloid biosynthesis and a possible cosuppression of both the endogenous and foreign enzyme genes in clone 236
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
NAD+
-
four-electron pyridine oxidoreductase
NADP+
-
NAD+ is 600000fold more efficient than NADP+ in wild-type enzyme
additional information
-
very detailed kinetic studies of mutants concerning NAD+/NADP+-affinities, the best specificity improvement is achieved by the D146A/L148R-mutant
-
additional information
-
sequence comparisons of several species with class II (NAD(H)) and class I (NADP(H)) HMG-CoA reductases for analysis of cofactor binding, overview
-
additional information
-
sequence comparisons of several species with class II (NAD(H)) and class I (NADP(H)) HMG-CoA reductases for analysis of cofactor binding, specificity-determining residue of HMGR from Pseudomonas mevalonii is D646, overview
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(3S,6Z)-3-benzyl-1-(4-fluorobenzyl)-8-(4-methoxyphenyl)-4-(3-methylbutanoyl)-3,4,5,8-tetrahydro-1,4-diazocin-2(1H)-one
-
purified enzyme, 52.6% residual activity at 0.01 mM
(3S,6Z)-3-benzyl-1-(4-fluorobenzyl)-8-(4-methoxyphenyl)-4-(3-methylbutanoyl)-3,4,5,8-tetrahydro-1,4-diazocin-2(1H)-one
-
antiproliferative activity in L-1210 cell, IC50 0.00148 mM
(3S,6Z)-3-benzyl-1-(4-fluorobenzyl)-8-(4-methoxyphenyl)-4-[[(E)-2-phenylethenyl]sulfonyl]-3,4,5,8-tetrahydro-1,4-diazocin-2(1H)-one
-
purified enzyme, 32.3% residual activity at 0.01 mM
-
(3S,6Z)-3-benzyl-1-(4-fluorobenzyl)-8-(4-methoxyphenyl)-4-[[(E)-2-phenylethenyl]sulfonyl]-3,4,5,8-tetrahydro-1,4-diazocin-2(1H)-one
-
antiproliferative activity in L-1210 cell, IC50 0.0023 mM
-
(3S,6Z)-3-benzyl-4-(3,3-dimethylbutanoyl)-1-(4-fluorobenzyl)-8-(4-methoxyphenyl)-3,4,5,8-tetrahydro-1,4-diazocin-2(1H)-one
-
purified enzyme, 43.4% residual activity at 0.01 mM
(3S,6Z)-3-benzyl-4-(3,3-dimethylbutanoyl)-1-(4-fluorobenzyl)-8-(4-methoxyphenyl)-3,4,5,8-tetrahydro-1,4-diazocin-2(1H)-one
-
antiproliferative activity in L-1210 cell, IC50 0.00143 mM
(3S,6Z)-4-(biphenyl-4-ylsulfonyl)-1-(4-fluorobenzyl)-8-(4-methoxyphenyl)-3-methyl-3,4,5,8-tetrahydro-1,4-diazocin-2(1H)-one
-
purified enzyme, 54.4% residual activity at 0.01 mM
(3S,6Z)-4-(biphenyl-4-ylsulfonyl)-1-(4-fluorobenzyl)-8-(4-methoxyphenyl)-3-methyl-3,4,5,8-tetrahydro-1,4-diazocin-2(1H)-one
-
antiproliferative activity in L-1210 cell, IC50 0.00119 mM
3-Hydroxy-3-methylbutyrate
-
-
3-hydroxy-3-methylcarboxylic acid
-
competitive inhibitor
3-hydroxy-3-methylglutarate
-
-
3-hydroxy-3-methylglutarate
-
competitive inhibitor
3-hydroxy-3-methylglutarate
-
-
4-hydroxybutyrate
-
-
acetoacetate
-
competivive inhibitor vs. mevalonate, non inhibitory vs. NAD+
beta-hydroxybutyrate
-
-
Ca2+
-
the addition of Ca2+ leads to a decrease in protein accumulation
deoxycholate
-
competitive inhibitor
lovastatin
-
pharmacological inhibition of HMGR activities decreases nodule number and delays nodulation
mevalonate
-
the addition of reaction product results in a dramatic loss of immunoreactive enzyme
simvastatin
-
treatment prevents endotoxemic liver injury by inhibiting leukocyte infiltration and hepatocellular apoptosis. The protective effects are dependent on the 3-hydroxy-3-methylglutaryl-coenzyme A reductase pathway
additional information
-
no inhibition citrate, succinate, glutarate, 3,3-dimethylacrylate, 2,2-dimethylpropionate, acetoacetate
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
CoA
-
mevaldehyde reduction
docosahexaenoic acid ethyl ester
-
in 18-month-old aged mice but not in 8-month-old mice, HMG-CoA reductase activity is enhanced with dietary intake of docosahexaenoic acid ethyl ester (DHA-EE)
EGTA
-
EGTA causes an increase in levels of enzyme observed on immunoplots
mevastatin
-
The increased accumulation of the enzyme-FLAG using the open-ring form and the closed-ring form of mevastatin is observed. The mevastatin-induced enzyme increases are possibly explained by the inhibition of a feedback-regulated down-regulation due to lowered pools of mevalonate or its product
pantetheine
-
mevaldehyde reduction
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.27
-
(R,S)-mevalonate
-
H381A mutant, oxidative acylation of mevalonate
0.45
-
(R,S)-mevalonate
-
wild-type enyzme, oxidative acylation of mevalonate
0.71
-
(R,S)-mevalonate
-
H381Q mutant, oxidative acylation of mevalonate
0.75
-
(R,S)-mevalonate
-
H381K mutant, oxidative acylation of mevalonate
3.7
-
(R,S)-mevalonate
-
H381N mutant, oxidative acylation of mevalonate
0.039
-
CoA
-
oxidative acylation of mevalonate
0.046
-
CoA
-
mevaldate oxidation
0.1
-
CoA
-
oxidative acylation of mevalonate
0.03
-
CoASH
-
H381A mutant, oxidative acylation of mevalonate
0.05
-
CoASH
-
oxidative acylation of mevalonate
0.05
-
CoASH
-
wild-type enzyme, oxidative acylation of mevalonate
0.11
-
CoASH
-
H381Q mutant, oxidative acylation of mevalonate
0.2
-
CoASH
-
H381N mutant, oxidative acylation of mevalonate
0.5
-
CoASH
-
H381K mutant, oxidative acylation of mevalonate
0.05
-
DL-3-hydroxy-3-methylglutaryl-CoA
-
reductive deacylation to mevalonate
0.3
-
DL-3-hydroxy-3-methylglutaryl-CoA
-
reductive deacylation to mevalonate
0.61
-
DL-mevaldate
-
mevaldate oxidation
1.36
-
DL-mevaldate
-
mevaldate oxidation
9
-
DL-mevaldate
-
mevaldate reduction to mevalonate
36
-
DL-mevaldate
-
mevaldate reduction to mevalonate
0.35
-
DL-mevalonate
-
oxidative acylation of mevalonate
0.49
-
DL-mevalonate
-
oxidative acylation of mevalonate
0.22
-
mevalonate
-
oxidative acylation of mevalonate
0.3
-
mevalonate
-
oxidative acylation of mevalonate
0.06
-
NAD+
-
mevaldate oxidation
0.14
-
NAD+
-
H381A mutant, oxidative acylation of mevalonate
0.17
-
NAD+
-
mevaldate oxidation
0.21
-
NAD+
-
wild-type enzyme, oxidative acylation of mevalonate
0.22
-
NAD+
-
wild-type enzyme, oxidative acylation of mevalonate
0.27
-
NAD+
-
oxidative acylation of mevalonate
0.35
-
NAD+
-
oxidative acylation of mevalonate
0.37
-
NAD+
-
oxidative acylation of mevalonate
0.6
-
NAD+
-
oxidative acylation of mevalonate
0.62
-
NAD+
-
H381Q mutant, oxidative acylation of mevalonate
0.81
-
NAD+
-
H381N mutant, oxidative acylation of mevalonate
1.23
-
NAD+
-
H381K mutant, oxidative acylation of mevalonate
0.032
-
NADH
-
reductive deacylation to mevalonate
0.17
-
NADH
-
reductive deacylation to mevalonate
0.36
-
NADH
-
mevaldate reduction to mevalonate
52
-
NADP+
-
wild-type enzyme, oxidative acylation of mevalonate
0.15
-
R-mevalonate
-
oxidative acylation of mevalonate
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
4.5
-
3-hydroxy-3-methylglutarate
-
standard conditions, inhibition by substrate analog
35
-
4-hydroxybutyrate
-
standard conditions, inhibition by substrate analog
3
-
acetoacetate
-
standard conditions, inhibition by substrate analog
0.8
-
beta-hydroxybutyrate
-
standard conditions, inhibition by substrate analog
0.28
-
lovastin
-
competive inhibition with respect to mevanolate
0.53
-
lovastin
-
competive inhibition with respect to 3-hydroxy-3-methylglutaryl-CoA
16
-
lovastin
-
non-competive inhibition with respect to NADH
35
-
lovastin
-
non-competive inhibition with respect to NAD+
0.26
-
mevalonate
-
standard conditions, substrate inhibition
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.011
-
-
H381A-mutant, mevalonate acylation
0.029
-
-
H381N-mutant, mevalonate acylation
0.041
-
-
H381Q-mutant, mevalonate acylation
0.091
-
-
H381K-mutant, mevalonate acylation
0.163
-
-
mevalonate acylation
0.17
-
-
mevalonate acylation
0.922
-
-
wild-type enzyme, [14C]-mevalonate acylation
1.203
-
-
S871A [14C]-mevalonate acylation
2.7
-
-
reverse reaction, pH 7.9, 30C
2.73
-
-
forward reaction, pH 7.9, 30C
4.87
-
-
reverse reaction, pH 7.9, 30C
11.94
-
-
forward reaction, pH 7.9, 30C
18
-
-
mevalonate acylation pH 8.1
20.3
-
-
mevalonate acylation pH 11
54.2
-
-
cysteine-free mutant, mevalonate acylation
60.5
-
-
mevalonate acylation
65.6
-
-
C156A-mutant, mevalonate acylation
70.5
-
-
wild-type enzyme, mevalonate acylation
77.7
-
-
C296A-mutant, mevalonate acylation
additional information
-
-
after a dietary intake of docosahexaenoic acid ethyl ester (DHA-EE) brain HMG-CoA reductase activity and brain cholesterol content significantly increases with age. Hepatic HMG-CoA reductase activity and the cholesterol content of both adult and aged mice are reduced in DHA-EE diet groups compared with linoleic acid ethyl ester
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
-
-
oxidative acylation of mevalonate with NADP+ as cofactor
7.1
-
-
assay conditions
7.2
-
-
assay at
7.9
-
-
assay at, both reaction directions
8.1
-
-
oxidative acylation of mevalonate
9
-
-
oxidative acylation of mevalonate
9.2
9.6
-
oxidative acylation of mevalonate
9.5
-
-
H381N mutant, oxidative acylation of mevalonate
10
-
-
H381A mutant, oxidative acylation of mevalonate
10.5
-
-
H381Q mutant, oxidative acylation of mevalonate
11
-
-
H381K mutant, oxidative acylation of mevalonate
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
-
assay at, both reaction directions
37
-
-
assay at
40
-
-
oxidative acylation of mevalonate
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
results show that docosahexaenoic acid ethyl ester enhances brain HMG-CoA reductase activity in aged mice
Manually annotated by BRENDA team
-
primary and reccurent pterygium
Manually annotated by BRENDA team
-
human trophoblast cell line (JAR) infected with Chlamydia trachomatis reveal a decrease in cellular cholesterol and a down regulation of HMG-CoA reductase
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Mycobacterium sp. s4
-
-
-
Manually annotated by BRENDA team
additional information
-
found predominantly in vesicle-like structures
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
45540
-
-
amino acid composition
178000
-
-
gel filtration
270000
-
-
SDS-PAGE
270100
-
-
sedimentation equilibrium centrifugation
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hexamer
-
3alpha2, XSA
tetramer
-
alpha4, 4 * 43000, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
phosphoprotein
-
near the C-terminus
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
3 A resolution, 3 dimers packed along three-fold crystallographic axis, hexamer
-
wild-type and mutants, H381A, H381N, H381K, H381Q, 3 A resolution
-
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
stable to quick freezing and boiling
-
20 mM N-ethylmaleimide, 50 min, 12% activity
-
4-vinylpyridine, 20 min, 0C, 76% activity
-
5,5'-dithiobis(2-nitrobenzoic acid), 20 min, 0C, 20% activity
-
diethyl polycarbonate causes loss of activity
-
dithiothreitol causes loss of activity
-
EDTA causes loss of activity
-
N-ethylmaleimide, 20 min, 0C, 0% activity
-
p-hydroxymercuribenzoate, 20 min, 0C, 19% activity
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C unstable to repeated freezing and thawing
-
-180C, 400 mM KCl, 12 months
-
-180C, 400 mM KCl, 24 months
-
-20C stable to repeated freezing and thawing
-
0C, 10 hours, 5% loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in COS-M6a, monkey; expressed in UT-2, CHO-cells
-
expression in Catharanthus roseus, the hairy roots with higher levels of soluble enzyme, clone 19, have a lower alkaloid and higher sterol content. By contrast, the clone with nonsoluble enzyme activity, clone 236, has a higher alkaloid and lower sterol content
-
expressed in Escherichia coli
-
expressed in Escherichia coli BL21
-
expressed in Escherichia coli JM103
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
mRNA levels of HMG-CoA-R are increased significantly in both primary and recurrent pterygia by 4.2fold and 3.6fold respectively, compared with normal conjunctiva. Concomitantly, there is a significant increase of LDL-R mRNA levels of 4.1fold in primary pterygia and 2.7fold in recurrent pterygium, compared with the control normal conjunctiva
-
during myoblast differentiation, insulin-induced increase in protein levels is detected after 6 h, remains constant up to 16 h, and then decreases below control levels at 72 h after insulin addition
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
S871A
-
150% of wild-type activity in 50 mM KCl
C156/296 A
-
fully active, resistant to N-ethylmaleimide
C156A
-
fully active, resistant to N-ethylmaleimide
C296A
-
fully active
D146A
-
6670-fold more specific for NADP+ than wild-type
D146A/L148K
-
72200-fold more specific for NADP+ than wild-type
D146A/L148R
-
83300-fold more specific for NADP+ than wild-type
D146A/Q147K
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no activity with NADP+ as cofactor
D146A/T192K
-
no activity with NADP+ as cofactor
D146A/T192R
-
no activity with NADP+ as cofactor
D146G
-
1170-fold more specific for NADP+ than wild-type
D146G/L148K
-
55600-fold more specific for NADP+ than wild-type
D146G/L148R
-
no activity with NADP+ as cofactor
D146G/T192K
-
3170-fold more specific for NADP+ than wild-type
D146G/T192R
-
4500-fold more specific for NADP+ than wild-type
D146N
-
no activity with NADP+ as cofactor
D146S
-
no activity with NADP+ as cofactor
H381A
-
6% of wild-type activity
H381K
-
45% of wild-type activity at pH 11
H381N
-
16% of wild-type activity
H381Q
-
23% of wild-type activity
additional information
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decreasing HMGR1 expression in Medicago truncatula transgenic roots by RNA interference leads to a dramatic decrease in nodulation, confirming that HMGR1 is essential for nodule development; using Medicago truncatula NORK, a receptor-like kinase, as bait in a yeast two-hybrid assay, Mt HMGR1 is identified as a NORK interacting partner. Mutagenesis and deletion analysis show that this interaction requires the cytosolic active kinase domain of NORK and the cytosolic catalytic domain of HMGR1
Renatured/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
after inactivation with diethyl polycarbonate addition of hydroxylamine restores 50% of activity
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
medicine
-
pterygium has an altered metabolism of cholesterol, namely increased LDL-R and HMG-CoA-R mRNAs. Both genes may play important roles in the pathogenesis of pterygium
medicine
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in endotoxemic mice, leukocyte infiltration in the liver is significantly elevated. Simvastatin significantly reduces endotoxin-induced hepatocellular damage and apoptosis. Hepatic accumulation of leukocytes is attenuated by simvastatin. Co-administration of mevalonate abolishes the protective effects of simvastatin on endotoxin-provoked increases in serum alanine transferase and serum alanine transferase as well as leukocyte recruitment
medicine
-
target enzyme for chemotherapy of hypercholesterolemias