BRENDA - Enzyme Database show
show all sequences of 1.1.1.88

3-hydroxy-3-methylglutaryl coenzyme a reductase1 interacts with NORK and is crucial for nodulation in Medicago truncatula

Kevei, Z.; Lougnon, G.; Mergaert, P.; Horvath, G.V.; Kereszt, A.; Jayaraman, D.; Zaman, N.; Marcel, F.; Regulski, K.; Kiss, G.B.; Kondorosi, A.; Endre, G.; Kondorosi, E.; Ane, J.; Plant Cell 19, 3974-3989 (2007)

Data extracted from this reference:

Engineering
Amino acid exchange
Commentary
Organism
additional information
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
Medicago truncatula
Inhibitors
Inhibitors
Commentary
Organism
Structure
lovastatin
pharmacological inhibition of HMGR activities decreases nodule number and delays nodulation
Medicago truncatula
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
additional information
found predominantly in vesicle-like structures
Medicago truncatula
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Medicago truncatula
-
-
-
Source Tissue
Source Tissue
Commentary
Organism
Textmining
root
-
Medicago truncatula
-
root nodule
-
Medicago truncatula
-
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
additional information
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
Medicago truncatula
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
lovastatin
pharmacological inhibition of HMGR activities decreases nodule number and delays nodulation
Medicago truncatula
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
additional information
found predominantly in vesicle-like structures
Medicago truncatula
-
-
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
root
-
Medicago truncatula
-
root nodule
-
Medicago truncatula
-
Other publictions for EC 1.1.1.88
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)
723092
Ma
Optimization of a heterologous ...
Bordetella petrii, Delftia acidovorans, Pseudomonas mevalonii
Metab. Eng.
13
588-597
2011
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3
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712189
Perchellet
Novel synthetic inhibitors of ...
Homo sapiens, Mus musculus
Int. J. Mol. Med.
24
633-643
2009
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712196
Yu
-
Expression of low-density lipo ...
Homo sapiens
Int. J. Ophthal.
9
284-285
2009
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1
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712560
Martini
3-Hydroxy 3-methylglutaryl coe ...
Rattus norvegicus
J. Cell. Physiol.
220
524-530
2009
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712670
Slotta
Inhibition of 3-hydroxy-3-meth ...
Mus musculus
J. Investig. Med.
57
645-649
2009
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687173
Azenabor
Chlamydia trachomatis Infectio ...
Homo sapiens
Int. J. Med. Sci.
4
223-231
2007
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688564
Shirai
Effect of docosahexaenoic acid ...
Mus musculus
J. Nutr. Biochem.
18
488-494
2007
1
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689467
Kevei
3-hydroxy-3-methylglutaryl coe ...
Medicago truncatula
Plant Cell
19
3974-3989
2007
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1
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1
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5
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657303
Hedl
Inhibition of the Class II HMG ...
Pseudomonas mevalonii
Protein Sci.
13
1693-1697
2004
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6
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654225
Ayora-Talavera
Overexpression in Catharanthus ...
Mesocricetus auratus
Appl. Biochem. Biotechnol.
97
135-145
2002
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1
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656615
Crane
-
Regulated accumulation of 3-hy ...
Solanum tuberosum
J. Plant Physiol.
159
1301-1307
2002
2
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2
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287507
Tabernero
Substrate-induced closure of t ...
Pseudomonas mevalonii
Proc. Natl. Acad. Sci. USA
96
7167-7177
1999
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287508
Bochar
Aminoethylcysteine can replace ...
Pseudomonas mevalonii
Biochemistry
38
8879-8883
1999
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287506
Rogers
Active form of Pseudomonas mev ...
Pseudomonas mevalonii
Biochem. Mol. Med.
61
114-120
1997
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1
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1
3
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2
1
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2
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1
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1
2
1
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2
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3
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2
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287505
Friesen
Structural determinants of nuc ...
Pseudomonas mevalonii
Biochemistry
35
11945-11950
1996
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1
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13
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2
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2
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4
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1
4
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13
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2
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287504
Lawrence
Crystal structure of Pseudomon ...
Pseudomonas mevalonii
Science
268
1758-1762
1995
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1
1
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2
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287503
Sato
Replacement of serine-871 of h ...
Mesocricetus auratus
Proc. Natl. Acad. Sci. USA
90
9261-9265
1993
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1
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1
1
1
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287502
Darnay
Identification of the catalyti ...
Pseudomonas mevalonii
J. Biol. Chem.
267
15064-15070
1992
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15
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6
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5
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1
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15
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6
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2
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5
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287499
Jordan-Starck
Pseudomonas mevalonii 3-hydrox ...
Pseudomonas mevalonii
J. Biol. Chem.
264
17913-17918
1989
2
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287500
Jordan-Starck
Role of cysteine residues in P ...
Pseudomonas mevalonii
J. Biol. Chem.
264
17919-17923
1989
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287501
Beach
Cloning, sequencing, and overe ...
Pseudomonas mevalonii
J. Bacteriol.
171
2994 - 3001
1989
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287498
Gill
Mevalonate utilization in Pseu ...
Pseudomonas mevalonii
J. Biol. Chem.
260
9393-9398
1985
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4
1
1
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1
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1
1
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1
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2
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4
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1
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1
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2
1
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1
1
2
1
1
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1
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287497
Rodwell
S-3-Hydroxy-3-methylglutaryl-C ...
Pseudomonas mevalonii
Methods Enzymol.
71
480-486
1981
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1
10
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1
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1
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1
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3
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1
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2
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2
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2
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1
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10
-
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1
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1
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3
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1
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2
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287496
Bensch
Purification and properties of ...
Pseudomonas mevalonii
J. Biol. Chem.
245
3755-3762
1970
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2
1
10
1
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1
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2
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1
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2
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2
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2
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1
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10
1
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2
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1
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287495
Fimognari
-
Substrate-competitive inhibiti ...
Mycobacterium sp., Mycobacterium sp. s4, Pseudomonas mevalonii
Biochemistry
4
2086-2090
1965
-
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12
6
2
1
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3
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2
2
7
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2
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3
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3
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-
-
12
-
6
2
1
-
-
-
-
-
-
-
-
2
2
7
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-