Crystallization (Comment) | 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 | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
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 | UniProt | Comment | Textmining |
---|---|---|---|
Mycobacterium tuberculosis | P9WKH3 | - |
- |
Mycobacterium tuberculosis H37Rv | P9WKH3 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
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 | ? | - |
? | |
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 | ? | - |
? | |
protoheme + 3 reduced acceptor + 3 O2 | - |
Mycobacterium tuberculosis | mycobilin a + 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 | mycobilin b + Fe2+ + 3 acceptor + 3 H2O | - |
? | |
protoheme + 3 reduced acceptor + 3 O2 | - |
Mycobacterium tuberculosis H37Rv | mycobilin b + Fe2+ + 3 acceptor + 3 H2O | - |
? |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
heme | - |
Mycobacterium tuberculosis |