BRENDA - Enzyme Database show
show all sequences of 1.14.99.57

A new way to degrade heme: the Mycobacterium tuberculosis enzyme MhuD catalyzes heme degradation without generating CO

Nambu, S.; Matsui, T.; Goulding, C.W.; Takahashi, S.; Ikeda-Saito, M.; J. Biol. Chem. 288, 10101-10109 (2013)

Data extracted from this reference:

Crystallization (Commentary)
Crystallization
Organism
the catalytically active 1:1 heme-MhuD complex has an active site structure similar to those of heme degrading enzymes IsdG and IsdI, including the nonplanarity (ruffling) of the heme group bound to the enzyme
Mycobacterium tuberculosis
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Mycobacterium tuberculosis
MhuD catalysis does not generate CO. MhuD cleaves heme at the alpha-meso position but retains the meso-carbon atom at the cleavage site. The tetrapyrrole product of MhuD, mycobilin, has an aldehyde group at the cleavage site and a carbonyl group at either the beta-meso or the delta-meso position. MhuD catalysis does not involve verdoheme
?
-
-
-
additional information
Mycobacterium tuberculosis H37Rv
MhuD catalysis does not generate CO. MhuD cleaves heme at the alpha-meso position but retains the meso-carbon atom at the cleavage site. The tetrapyrrole product of MhuD, mycobilin, has an aldehyde group at the cleavage site and a carbonyl group at either the beta-meso or the delta-meso position. MhuD catalysis does not involve verdoheme
?
-
-
-
protoheme + 3 reduced acceptor + 3 O2
Mycobacterium tuberculosis
-
mycobilin a + Fe2+ + 3 acceptor + 3 H2O
-
-
?
protoheme + 3 reduced acceptor + 3 O2
Mycobacterium tuberculosis
-
mycobilin b + Fe2+ + 3 acceptor + 3 H2O
-
-
?
protoheme + 3 reduced acceptor + 3 O2
Mycobacterium tuberculosis H37Rv
-
mycobilin a + Fe2+ + 3 acceptor + 3 H2O
-
-
?
protoheme + 3 reduced acceptor + 3 O2
Mycobacterium tuberculosis H37Rv
-
mycobilin b + Fe2+ + 3 acceptor + 3 H2O
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Mycobacterium tuberculosis
P9WKH3
-
-
Mycobacterium tuberculosis H37Rv
P9WKH3
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
MhuD catalysis does not generate CO. MhuD cleaves heme at the alpha-meso position but retains the meso-carbon atom at the cleavage site. The tetrapyrrole product of MhuD, mycobilin, has an aldehyde group at the cleavage site and a carbonyl group at either the beta-meso or the delta-meso position. MhuD catalysis does not involve verdoheme
740706
Mycobacterium tuberculosis
?
-
-
-
-
additional information
MhuD catalysis does not generate CO. MhuD cleaves heme at the alpha-meso position but retains the meso-carbon atom at the cleavage site. The tetrapyrrole product of MhuD, mycobilin, has an aldehyde group at the cleavage site and a carbonyl group at either the beta-meso or the delta-meso position. MhuD catalysis does not involve verdoheme
740706
Mycobacterium tuberculosis H37Rv
?
-
-
-
-
protoheme + 3 reduced acceptor + 3 O2
-
740706
Mycobacterium tuberculosis
mycobilin a + Fe2+ + 3 acceptor + 3 H2O
-
-
-
?
protoheme + 3 reduced acceptor + 3 O2
-
740706
Mycobacterium tuberculosis H37Rv
mycobilin a + Fe2+ + 3 acceptor + 3 H2O
-
-
-
?
protoheme + 3 reduced acceptor + 3 O2
-
740706
Mycobacterium tuberculosis
mycobilin b + Fe2+ + 3 acceptor + 3 H2O
-
-
-
?
protoheme + 3 reduced acceptor + 3 O2
-
740706
Mycobacterium tuberculosis H37Rv
mycobilin b + Fe2+ + 3 acceptor + 3 H2O
-
-
-
?
Cofactor
Cofactor
Commentary
Organism
Structure
heme
-
Mycobacterium tuberculosis
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
heme
-
Mycobacterium tuberculosis
Crystallization (Commentary) (protein specific)
Crystallization
Organism
the catalytically active 1:1 heme-MhuD complex has an active site structure similar to those of heme degrading enzymes IsdG and IsdI, including the nonplanarity (ruffling) of the heme group bound to the enzyme
Mycobacterium tuberculosis
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Mycobacterium tuberculosis
MhuD catalysis does not generate CO. MhuD cleaves heme at the alpha-meso position but retains the meso-carbon atom at the cleavage site. The tetrapyrrole product of MhuD, mycobilin, has an aldehyde group at the cleavage site and a carbonyl group at either the beta-meso or the delta-meso position. MhuD catalysis does not involve verdoheme
?
-
-
-
additional information
Mycobacterium tuberculosis H37Rv
MhuD catalysis does not generate CO. MhuD cleaves heme at the alpha-meso position but retains the meso-carbon atom at the cleavage site. The tetrapyrrole product of MhuD, mycobilin, has an aldehyde group at the cleavage site and a carbonyl group at either the beta-meso or the delta-meso position. MhuD catalysis does not involve verdoheme
?
-
-
-
protoheme + 3 reduced acceptor + 3 O2
Mycobacterium tuberculosis
-
mycobilin a + Fe2+ + 3 acceptor + 3 H2O
-
-
?
protoheme + 3 reduced acceptor + 3 O2
Mycobacterium tuberculosis
-
mycobilin b + Fe2+ + 3 acceptor + 3 H2O
-
-
?
protoheme + 3 reduced acceptor + 3 O2
Mycobacterium tuberculosis H37Rv
-
mycobilin a + Fe2+ + 3 acceptor + 3 H2O
-
-
?
protoheme + 3 reduced acceptor + 3 O2
Mycobacterium tuberculosis H37Rv
-
mycobilin b + Fe2+ + 3 acceptor + 3 H2O
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
MhuD catalysis does not generate CO. MhuD cleaves heme at the alpha-meso position but retains the meso-carbon atom at the cleavage site. The tetrapyrrole product of MhuD, mycobilin, has an aldehyde group at the cleavage site and a carbonyl group at either the beta-meso or the delta-meso position. MhuD catalysis does not involve verdoheme
740706
Mycobacterium tuberculosis
?
-
-
-
-
additional information
MhuD catalysis does not generate CO. MhuD cleaves heme at the alpha-meso position but retains the meso-carbon atom at the cleavage site. The tetrapyrrole product of MhuD, mycobilin, has an aldehyde group at the cleavage site and a carbonyl group at either the beta-meso or the delta-meso position. MhuD catalysis does not involve verdoheme
740706
Mycobacterium tuberculosis H37Rv
?
-
-
-
-
protoheme + 3 reduced acceptor + 3 O2
-
740706
Mycobacterium tuberculosis
mycobilin a + Fe2+ + 3 acceptor + 3 H2O
-
-
-
?
protoheme + 3 reduced acceptor + 3 O2
-
740706
Mycobacterium tuberculosis H37Rv
mycobilin a + Fe2+ + 3 acceptor + 3 H2O
-
-
-
?
protoheme + 3 reduced acceptor + 3 O2
-
740706
Mycobacterium tuberculosis
mycobilin b + Fe2+ + 3 acceptor + 3 H2O
-
-
-
?
protoheme + 3 reduced acceptor + 3 O2
-
740706
Mycobacterium tuberculosis H37Rv
mycobilin b + Fe2+ + 3 acceptor + 3 H2O
-
-
-
?
Other publictions for EC 1.14.99.57
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)
740897
Graves
Measurement of heme ruffling c ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis ATCC 25618
J. Phys. Chem. B
120
3844-3853
2016
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740528
Graves
Crystallographic and spectrosc ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis ATCC 25618
Inorg. Chem.
53
5931-5940
2014
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1
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1
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4
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1
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740706
Nambu
A new way to degrade heme: the ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
J. Biol. Chem.
288
10101-10109
2013
-
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1
-
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6
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2
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6
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1
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1
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6
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6
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740865
Chim
Unusual diheme conformation of ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis ATCC 25618
J. Mol. Biol.
395
595-608
2010
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1
1
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7
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1
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1
1
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