BRENDA - Enzyme Database show
show all sequences of 1.3.98.3

Functional differentiation of two analogous coproporphyrinogen III oxidases for heme and chlorophyll biosynthesis pathways in the cyanobacterium Synechocystis sp. PCC 6803

Goto, T.; Aoki, R.; Minamizaki, K.; Fujita, Y.; Plant Cell Physiol. 51, 650-663 (2010)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
DTT
added to the assay at 2 mM
Synechocystis sp.
NADH
added to the assay at 0.5 mM
Synechocystis sp.
Cloned(Commentary)
Commentary
Organism
genes sll1876 and sll1917, overexpression of N-terminally Strep-tagged HemNs in Escherichia coli
Synechocystis sp.
Engineering
Amino acid exchange
Commentary
Organism
additional information
construction of deletion mutants of the HemN genes, growth of the mutant DELTAsll1876 is significantly slower than that of the wild-type under microoxic conditions, while it grows normally under aerobic conditions. Coproporphyrin III is accumulated at a low but significant level in the DELTAsll1876 mutant grown under micro-oxic conditions. No detectable phenotype in DELTAsll1917 under the conditions, phenotypes, overview
Synechocystis sp.
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
coproporphyrinogen III + 2 S-adenosyl-L-methionine
Synechocystis sp.
sll1876 encodes HemN operating under micro-oxic conditions
protoporphyrinogen IX + 2 CO2 + 2 L-methionine + 2 5'-deoxyadenosine
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Synechocystis sp.
-
two hemN genes, sll1876 and sll1917
-
Purification (Commentary)
Commentary
Organism
recombinant terminally Strep-tagged HemNs from Escherichia coli to homogeneity
Synechocystis sp.
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
coproporphyrinogen III + 2 S-adenosyl-L-methionine
sll1876 encodes HemN operating under micro-oxic conditions
713258
Synechocystis sp.
protoporphyrinogen IX + 2 CO2 + 2 L-methionine + 2 5'-deoxyadenosine
-
-
-
?
coproporphyrinogen III + 2 S-adenosyl-L-methionine
only Sll1876 shows CPO activity under anaerobic conditions, Sll1917 is inactive
713258
Synechocystis sp.
protoporphyrinogen IX + 2 CO2 + 2 L-methionine + 2 5'-deoxyadenosine
-
-
-
?
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
37
-
assay at
Synechocystis sp.
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
assay at
Synechocystis sp.
Cofactor
Cofactor
Commentary
Organism
Structure
iron-sulfur centre
in Sll1876 and Sll1917
Synechocystis sp.
S-adenosyl-L-methionine
-
Synechocystis sp.
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
DTT
added to the assay at 2 mM
Synechocystis sp.
NADH
added to the assay at 0.5 mM
Synechocystis sp.
Cloned(Commentary) (protein specific)
Commentary
Organism
genes sll1876 and sll1917, overexpression of N-terminally Strep-tagged HemNs in Escherichia coli
Synechocystis sp.
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
iron-sulfur centre
in Sll1876 and Sll1917
Synechocystis sp.
S-adenosyl-L-methionine
-
Synechocystis sp.
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
additional information
construction of deletion mutants of the HemN genes, growth of the mutant DELTAsll1876 is significantly slower than that of the wild-type under microoxic conditions, while it grows normally under aerobic conditions. Coproporphyrin III is accumulated at a low but significant level in the DELTAsll1876 mutant grown under micro-oxic conditions. No detectable phenotype in DELTAsll1917 under the conditions, phenotypes, overview
Synechocystis sp.
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
coproporphyrinogen III + 2 S-adenosyl-L-methionine
Synechocystis sp.
sll1876 encodes HemN operating under micro-oxic conditions
protoporphyrinogen IX + 2 CO2 + 2 L-methionine + 2 5'-deoxyadenosine
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant terminally Strep-tagged HemNs from Escherichia coli to homogeneity
Synechocystis sp.
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
coproporphyrinogen III + 2 S-adenosyl-L-methionine
sll1876 encodes HemN operating under micro-oxic conditions
713258
Synechocystis sp.
protoporphyrinogen IX + 2 CO2 + 2 L-methionine + 2 5'-deoxyadenosine
-
-
-
?
coproporphyrinogen III + 2 S-adenosyl-L-methionine
only Sll1876 shows CPO activity under anaerobic conditions, Sll1917 is inactive
713258
Synechocystis sp.
protoporphyrinogen IX + 2 CO2 + 2 L-methionine + 2 5'-deoxyadenosine
-
-
-
?
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
37
-
assay at
Synechocystis sp.
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
assay at
Synechocystis sp.
General Information
General Information
Commentary
Organism
physiological function
catalyzes the decarboxylation of coproporphyrinogen III to form protoporphyrinogen IX in heme biosynthesis and is shared in chlorophyll biosynthesis in photosynthetic organisms
Synechocystis sp.
General Information (protein specific)
General Information
Commentary
Organism
physiological function
catalyzes the decarboxylation of coproporphyrinogen III to form protoporphyrinogen IX in heme biosynthesis and is shared in chlorophyll biosynthesis in photosynthetic organisms
Synechocystis sp.
Other publictions for EC 1.3.98.3
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)
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Pratibha
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739104
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Role of HemF and HemN in the h ...
Vibrio vulnificus, Vibrio vulnificus ATCC 29307
Mol. Microbiol.
96
497-512
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1
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1
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4
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726009
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Coproporphyrin III excretion i ...
Rubrivivax gelatinosus
Mol. Microbiol.
88
339-351
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2
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4
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745799
Azzouzi
Coproporphyrin III excretion ...
Rubrivivax gelatinosus
Mol. Microbiol.
88
339-351
2013
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1
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724235
Abicht
Lactococcus lactis HemW (HemN) ...
Lactococcus lactis
Biochem. J.
442
335-343
2012
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3
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711084
Shaveta
Structural characterization re ...
Homo sapiens
Biochem. Biophys. Res. Commun.
391
1390-1395
2010
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711348
Rand
The oxygen-independent copropo ...
Escherichia coli
Biol. Chem.
391
55-63
2010
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1
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712016
Duschene
The antiviral protein viperin ...
Homo sapiens
FEBS Lett.
584
1263-1267
2010
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713258
Goto
Functional differentiation of ...
Synechocystis sp.
Plant Cell Physiol.
51
650-663
2010
2
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1
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1
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685280
Yokoyama
Mechanistic study on the react ...
Bacillus circulans
Biochemistry
47
8950-8960
2008
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686237
Frey
The radical SAM superfamily ...
Homo sapiens
Crit. Rev. Biochem. Mol. Biol.
43
63-88
2008
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687282
Yokoyama
Characterization and mechanist ...
Bacillus circulans
J. Am. Chem. Soc.
129
15147-15155
2007
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674567
Layer
The substrate radical of Esche ...
Escherichia coli
J. Biol. Chem.
281
15727-15734
2006
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672473
Layer
Structural and functional comp ...
Bacillus subtilis, Cupriavidus necator, Escherichia coli, Rhodobacter sphaeroides, Salmonella enterica subsp. enterica serovar Typhimurium
Biol. Chem.
386
971-980
2005
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674462
Layer
Radical S-adenosylmethionine e ...
Escherichia coli
J. Biol. Chem.
280
29038-29046
2005
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658501
Layer
Structure and function of radi ...
Escherichia coli
Curr. Opin. Chem. Biol.
8
468-476
2004
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655340
Layer
Crystal structure of coproporp ...
Escherichia coli
EMBO J.
22
6214-6224
2003
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656073
Layer
Oxygen-independent coproporphy ...
Escherichia coli
J. Biol. Chem.
277
34136-34142
2002
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