BRENDA - Enzyme Database show
show all sequences of 1.3.98.3

Lactococcus lactis HemW (HemN) is a haem-binding protein with a putative role in haem trafficking

Abicht, H.K.; Martinez, J.; Layer, G.; Jahn, D.; Solioz, M.; Biochem. J. 442, 335-343 (2012)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
gene hemW or hemN, recombinant expression in the hemN-deficient Escherichia coli mutant strain JW3838 and in strain BL21(DE3) as His-tagged protein. Lactococcus lactis HemW at high levels does not complement the growth deficit of the Escherichia coli DELTAhemN mutant
Lactococcus lactis
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
cytosol
in vivo, HemW occurs as a heme-free cytosolic form, as well as a heme-containing membrane-associated form
Lactococcus lactis
5829
-
membrane
in vivo, HemW occurs as a heme-free cytosolic form, as well as a heme-containing membrane-associated form
Lactococcus lactis
16020
-
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Fe2+
a heme containing enzyme, HemN contains a [4Fe-4S] cluster
Lactococcus lactis
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Lactococcus lactis
HemW shows no coproporphyrinogen III oxidase activity in vivo or in vitro
?
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Lactococcus lactis
-
gene hemW or hemN
-
Purification (Commentary)
Commentary
Organism
recombinant His-tagged HemN from Escherichia coli strain BL21(DE3) membranes by nickel affinity chromatography and gel filtration
Lactococcus lactis
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
HemW shows no coproporphyrinogen III oxidase activity in vivo or in vitro
724235
Lactococcus lactis
?
-
-
-
-
Cofactor
Cofactor
Commentary
Organism
Structure
heme
in vivo, HemW occurs as a heme-free cytosolic form, as well as a heme-containing membrane-associated form
Lactococcus lactis
S-adenosyl-L-methionine
-
Lactococcus lactis
Cloned(Commentary) (protein specific)
Commentary
Organism
gene hemW or hemN, recombinant expression in the hemN-deficient Escherichia coli mutant strain JW3838 and in strain BL21(DE3) as His-tagged protein. Lactococcus lactis HemW at high levels does not complement the growth deficit of the Escherichia coli DELTAhemN mutant
Lactococcus lactis
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
heme
in vivo, HemW occurs as a heme-free cytosolic form, as well as a heme-containing membrane-associated form
Lactococcus lactis
S-adenosyl-L-methionine
-
Lactococcus lactis
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
cytosol
in vivo, HemW occurs as a heme-free cytosolic form, as well as a heme-containing membrane-associated form
Lactococcus lactis
5829
-
membrane
in vivo, HemW occurs as a heme-free cytosolic form, as well as a heme-containing membrane-associated form
Lactococcus lactis
16020
-
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Fe2+
a heme containing enzyme, HemN contains a [4Fe-4S] cluster
Lactococcus lactis
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Lactococcus lactis
HemW shows no coproporphyrinogen III oxidase activity in vivo or in vitro
?
-
-
-
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant His-tagged HemN from Escherichia coli strain BL21(DE3) membranes by nickel affinity chromatography and gel filtration
Lactococcus lactis
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
HemW shows no coproporphyrinogen III oxidase activity in vivo or in vitro
724235
Lactococcus lactis
?
-
-
-
-
General Information
General Information
Commentary
Organism
evolution
HemW-like proteins form a distinct phylogenetic clade. It contains the four cysteine residues of the radical S-adenosyl-L-methionine enzyme motif of CPDH enzymes, structure comparisons, overview. The fourth cysteine residue of the Fe-S cluster motif of Escherichia coli HemN, CX3CX2CXC, is replaced by phenylalanine in HemW and related proteins
Lactococcus lactis
metabolism
genes hemH and hemW (hemN) show conjectured functions in heme metabolism
Lactococcus lactis
physiological function
addition of Lactococcus lactis membranes to heme-containing HemW triggers the release of heme from HemW in vitro. Role of HemW in heme trafficking
Lactococcus lactis
General Information (protein specific)
General Information
Commentary
Organism
evolution
HemW-like proteins form a distinct phylogenetic clade. It contains the four cysteine residues of the radical S-adenosyl-L-methionine enzyme motif of CPDH enzymes, structure comparisons, overview. The fourth cysteine residue of the Fe-S cluster motif of Escherichia coli HemN, CX3CX2CXC, is replaced by phenylalanine in HemW and related proteins
Lactococcus lactis
metabolism
genes hemH and hemW (hemN) show conjectured functions in heme metabolism
Lactococcus lactis
physiological function
addition of Lactococcus lactis membranes to heme-containing HemW triggers the release of heme from HemW in vitro. Role of HemW in heme trafficking
Lactococcus lactis
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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724235
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Lactococcus lactis HemW (HemN) ...
Lactococcus lactis
Biochem. J.
442
335-343
2012
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674567
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The substrate radical of Esche ...
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281
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386
971-980
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674462
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Radical S-adenosylmethionine e ...
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280
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Structure and function of radi ...
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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
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