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Literature summary extracted from

  • Nambu, S.; Matsui, T.; Goulding, C.W.; Takahashi, S.; Ikeda-Saito, M.
    A new way to degrade heme: the Mycobacterium tuberculosis enzyme MhuD catalyzes heme degradation without generating CO (2013), J. Biol. Chem., 288, 10101-10109.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.14.99.57 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)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.14.99.57 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 ?
-
?
1.14.99.57 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 ?
-
?
1.14.99.57 protoheme + 3 reduced acceptor + 3 O2 Mycobacterium tuberculosis
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mycobilin a + Fe2+ + 3 acceptor + 3 H2O
-
?
1.14.99.57 protoheme + 3 reduced acceptor + 3 O2 Mycobacterium tuberculosis
-
mycobilin b + Fe2+ + 3 acceptor + 3 H2O
-
?
1.14.99.57 protoheme + 3 reduced acceptor + 3 O2 Mycobacterium tuberculosis H37Rv
-
mycobilin a + Fe2+ + 3 acceptor + 3 H2O
-
?
1.14.99.57 protoheme + 3 reduced acceptor + 3 O2 Mycobacterium tuberculosis H37Rv
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mycobilin b + Fe2+ + 3 acceptor + 3 H2O
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.14.99.57 Mycobacterium tuberculosis P9WKH3
-
-
1.14.99.57 Mycobacterium tuberculosis H37Rv P9WKH3
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-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.99.57 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 Mycobacterium tuberculosis ?
-
?
1.14.99.57 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 Mycobacterium tuberculosis H37Rv ?
-
?
1.14.99.57 protoheme + 3 reduced acceptor + 3 O2
-
Mycobacterium tuberculosis mycobilin a + Fe2+ + 3 acceptor + 3 H2O
-
?
1.14.99.57 protoheme + 3 reduced acceptor + 3 O2
-
Mycobacterium tuberculosis H37Rv mycobilin a + Fe2+ + 3 acceptor + 3 H2O
-
?
1.14.99.57 protoheme + 3 reduced acceptor + 3 O2
-
Mycobacterium tuberculosis mycobilin b + Fe2+ + 3 acceptor + 3 H2O
-
?
1.14.99.57 protoheme + 3 reduced acceptor + 3 O2
-
Mycobacterium tuberculosis H37Rv mycobilin b + Fe2+ + 3 acceptor + 3 H2O
-
?

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.99.57 heme
-
Mycobacterium tuberculosis