BRENDA - Enzyme Database
show all sequences of 1.3.1.8

Crystal structures of the substrate-bound forms of red chlorophyll catabolite reductase: implications for site-specific and stereospecific reaction

Sugishima, M.; Okamoto, Y.; Noguchi, M.; Kohchi, T.; Tamiaki, H.; Fukuyama, K.; J. Mol. Biol. 402, 879-891 (2010)

Data extracted from this reference:

Cloned(Commentary)
Cloned (Commentary)
Organism
expression of GST-tagged wild-type and F218V mutant RCCR lacking the chloroplast transit peptide, Met1 to Gln39
Arabidopsis thaliana
Crystallization (Commentary)
Crystallization (Commentary)
Organism
purified recombinant red chlorophyll catabolite-bound RCCRDELTA49, and red chlorophyll catabolite-bound or substrate-free F218V RCCRDELTA49, sitting drop vapor diffusion method, 20°C, protein solution is mixed with an equal volume of reservoir solution and equilibrated against reservoir solution containing 30% w/v PEG 2000 monomethyl ether, 0.1 M ammonium acetate, 3% v/v dioxane, and 0.1 M 4-morpholineethanesulfonic acid–NaOH, pH 6.5, 1 day, X-ray diffraction structure determination and analysis at 2.0-2.6 A resolution
Arabidopsis thaliana
Engineering
Protein Variants
Commentary
Organism
F218V
a mutant protein that produces the stereoisomer of primary fluorescent chlorophyll catabolites at the C1 position, the F218V mutation changes the stereospecificity in RCCR. Construction of wild-type and F218V mutant RCCR lacking the chloroplast transit peptide, Met1 to Gln39, i.e. RCCRDELTA49
Arabidopsis thaliana
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
primary fluorescent chlorophyll catabolite + NADP+
Arabidopsis thaliana
stereospecific reaction. RCCR catalyzes the ferredoxin-dependent and site-specific reduction of the C20/C1 double bond of red chlorophyll catabolite, RCC, the catabolic intermediate produced in chlorophyll degradation
red chlorophyll catabolite + NADPH + H+
-
-
r
Organism
Organism
UniProt
Commentary
Textmining
Arabidopsis thaliana
-
-
-
Purification (Commentary)
Purification (Commentary)
Organism
recombinant GST-tagged wild-type and F218V mutant RCCR lacking the chloroplast transit peptide, Met1 to Gln39, i.e. RCCRDELTA49
Arabidopsis thaliana
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
primary fluorescent chlorophyll catabolite + NADP+
stereospecific reaction
712769
Arabidopsis thaliana
red chlorophyll catabolite + NADPH + H+
red chlorophyll catabolite, RCC, binding does not drastically change the RCCR structure, binding structure and mechanism analysis, overview. Comparison of the RCC-binding pockets of wild-type RCCRDELTA49 and F218V RCCRDELTA49, overview
-
-
r
primary fluorescent chlorophyll catabolite + NADP+
stereospecific reaction. RCCR catalyzes the ferredoxin-dependent and site-specific reduction of the C20/C1 double bond of red chlorophyll catabolite, RCC, the catabolic intermediate produced in chlorophyll degradation
712769
Arabidopsis thaliana
red chlorophyll catabolite + NADPH + H+
-
-
-
r
Subunits
Subunits
Commentary
Organism
More
RCCR folds into a characteristic alpha/beta/alpha sandwich, similar to that observed in the ferredoxin-dependent bilin reductase family, structure comparisosns, overview
Arabidopsis thaliana
Synonyms
Synonyms
Commentary
Organism
RCCR
-
Arabidopsis thaliana
Cofactor
Cofactor
Commentary
Organism
Structure
NADP+
-
Arabidopsis thaliana
NADPH
-
Arabidopsis thaliana
Cloned(Commentary) (protein specific)
Commentary
Organism
expression of GST-tagged wild-type and F218V mutant RCCR lacking the chloroplast transit peptide, Met1 to Gln39
Arabidopsis thaliana
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADP+
-
Arabidopsis thaliana
NADPH
-
Arabidopsis thaliana
Crystallization (Commentary) (protein specific)
Crystallization
Organism
purified recombinant red chlorophyll catabolite-bound RCCRDELTA49, and red chlorophyll catabolite-bound or substrate-free F218V RCCRDELTA49, sitting drop vapor diffusion method, 20°C, protein solution is mixed with an equal volume of reservoir solution and equilibrated against reservoir solution containing 30% w/v PEG 2000 monomethyl ether, 0.1 M ammonium acetate, 3% v/v dioxane, and 0.1 M 4-morpholineethanesulfonic acid–NaOH, pH 6.5, 1 day, X-ray diffraction structure determination and analysis at 2.0-2.6 A resolution
Arabidopsis thaliana
Engineering (protein specific)
Protein Variants
Commentary
Organism
F218V
a mutant protein that produces the stereoisomer of primary fluorescent chlorophyll catabolites at the C1 position, the F218V mutation changes the stereospecificity in RCCR. Construction of wild-type and F218V mutant RCCR lacking the chloroplast transit peptide, Met1 to Gln39, i.e. RCCRDELTA49
Arabidopsis thaliana
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
primary fluorescent chlorophyll catabolite + NADP+
Arabidopsis thaliana
stereospecific reaction. RCCR catalyzes the ferredoxin-dependent and site-specific reduction of the C20/C1 double bond of red chlorophyll catabolite, RCC, the catabolic intermediate produced in chlorophyll degradation
red chlorophyll catabolite + NADPH + H+
-
-
r
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant GST-tagged wild-type and F218V mutant RCCR lacking the chloroplast transit peptide, Met1 to Gln39, i.e. RCCRDELTA49
Arabidopsis thaliana
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
primary fluorescent chlorophyll catabolite + NADP+
stereospecific reaction
712769
Arabidopsis thaliana
red chlorophyll catabolite + NADPH + H+
red chlorophyll catabolite, RCC, binding does not drastically change the RCCR structure, binding structure and mechanism analysis, overview. Comparison of the RCC-binding pockets of wild-type RCCRDELTA49 and F218V RCCRDELTA49, overview
-
-
r
primary fluorescent chlorophyll catabolite + NADP+
stereospecific reaction. RCCR catalyzes the ferredoxin-dependent and site-specific reduction of the C20/C1 double bond of red chlorophyll catabolite, RCC, the catabolic intermediate produced in chlorophyll degradation
712769
Arabidopsis thaliana
red chlorophyll catabolite + NADPH + H+
-
-
-
r
Subunits (protein specific)
Subunits
Commentary
Organism
More
RCCR folds into a characteristic alpha/beta/alpha sandwich, similar to that observed in the ferredoxin-dependent bilin reductase family, structure comparisosns, overview
Arabidopsis thaliana
Other publictions for EC 1.3.1.8
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
Synonyms
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)
712769
Sugishima
Crystal structures of the subs ...
Arabidopsis thaliana
J. Mol. Biol.
402
879-891
2010
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685980
Rennison
Enhanced acyl-CoA dehydrogenas ...
Rattus norvegicus
Cardiovasc. Res.
79
331-340
2008
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689745
Erb
Synthesis of C5-dicarboxylic a ...
Luteovulum sphaeroides
Proc. Natl. Acad. Sci. USA
104
10631-10636
2007
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673619
Park
Silencing of NbECR encoding a ...
Nicotiana benthamiana
FEBS Lett.
579
4459-4464
2005
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656737
Li
Crotonyl-coenzyme A reductase ...
Streptomyces collinus
Microbiology
150
3463-3472
2004
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2
1
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6
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390872
Sargueil
High metabolism and subsequent ...
Mus musculus
Neurosci. Lett.
273
29-32
1999
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390873
Lessire
Study of the 3-hydroxy-eicosan ...
Allium ampeloprasum
Plant Physiol.
119
1009-1015
1999
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390869
Mukherjee
Inactivation of enoyl-CoA redu ...
Columba sp.
J. Enzyme Inhib.
13
217-228
1998
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390868
Mukherjee
Evidence for the essential his ...
Columba sp.
J. Enzyme Inhib.
11
209-216
1997
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1
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390759
Laguna
Action of Ebselen on rat hepat ...
Rattus norvegicus
Arch. Biochem. Biophys.
269
272-283
1989
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1
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390758
Nagi
Dual action of 2-decynoyl coen ...
Rattus norvegicus
Arch. Biochem. Biophys.
267
1-12
1988
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390757
Nagi
Site of inhibition of rat live ...
Rattus norvegicus
J. Biol. Chem.
261
13598-13605
1986
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1
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390753
Prasad
Solubilization and purificatio ...
Rattus norvegicus
Arch. Biochem. Biophys.
237
535-544
1985
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1
4
1
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8
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390870
Cvetanovic
Purification and characterizat ...
Bos taurus
Biochem. J.
227
49-56
1985
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390810
Inui
Fatty acid synthesis in mitoch ...
Euglena gracilis
Eur. J. Biochem.
142
121-126
1984
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390849
Kikuchi
Purification of NADPH-dependen ...
Mycolicibacterium smegmatis
J. Biochem.
96
841-848
1984
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10
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390754
Nagi
Biochemical properties of shor ...
Rattus norvegicus
Arch. Biochem. Biophys.
226
50-64
1983
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390755
Prasad
Kinetic evidence for two separ ...
Rattus norvegicus
Biochem. Biophys. Res. Commun.
113
659-665
1983
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390756
Cinti
Evidence for a second microsom ...
Rattus norvegicus
J. Biol. Chem.
257
14333-14340
1982
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1
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390752
Bernert
The isolation of acyl-CoA deri ...
Rattus norvegicus
Biochim. Biophys. Acta
573
436-442
1979
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390850
Strom
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Activation and inhibition of c ...
Bos taurus
J. Biol. Chem.
254
8159-8162
1979
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9
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390851
Strom
Enoyl coenzyme A reduction by ...
Bos taurus
J. Biol. Chem.
254
8153-8158
1979
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2
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8
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390751
Bernert
An analysis of partial reactio ...
Rattus norvegicus
J. Biol. Chem.
252
6736-6744
1977
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2
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6
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1
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390852
Maitra
Crotonyl coenzyme A reductase ...
Bos taurus
J. Biol. Chem.
249
111-117
1974
1
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3
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390853
Ishidate
Induction of NADPH enoyl-coA r ...
Candida albicans
J. Biochem.
76
1139-1142
1974
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390854
Ishidate
Separation and some characteri ...
Candida albicans
Chem. Pharm. Bull.
22
2685-2691
1974
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6
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2
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1
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1
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2
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1
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390855
Mizugaki
Stereospecific hydrogen transf ...
Rattus norvegicus
J. Biochem.
74
691-696
1973
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390856
Mizugaki
Possible role of NADPH-depende ...
Rattus norvegicus
Biochem. Biophys. Res. Commun.
50
48-53
1973
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3
1
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390857
Podack
On the mechanism of malonyl-Co ...
Rattus norvegicus
Biochim. Biophys. Acta
280
235-247
1972
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1
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1
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390858
Seubert
On the mechanism of malonyl-Co ...
Rattus norvegicus
Biochim. Biophys. Acta
164
498-517
1968
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