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1.3.98.5

Accepted name:

hydrogen peroxide-dependent heme synthase

Reaction:

Fe-coproporphyrin III + 2 H₂O₂ = protoheme + 2 CO₂ + 4 H₂O (overall reaction)
(1a) Fe-coproporphyrin III + H₂O₂ = harderoheme III + CO₂ + 2 H₂O
(1b) harderoheme III + H₂O₂ = protoheme + CO₂ + 2 H₂O

Other name(s):

coproheme III oxidative decarboxylase; hemQ (gene name)

Systematic name:

Fe-coproporphyrin III:hydrogen peroxide oxidoreductase (decarboxylating)

Comments:

The enzyme participates in a heme biosynthesis pathway found in Gram-positive bacteria. The initial decarboxylation step is fast and yields the three-propanoate harderoheme isomer III. The second decarboxylation is much slower. cf. EC 1.3.98.6, SAM-dependent heme synthase.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	Dailey, T.A., Boynton, T.O., Albetel, A.N., Gerdes, S., Johnson, M.K. and Dailey, H.A. Discovery and characterization of HemQ: an essential heme biosynthetic pathway component. J. Biol. Chem. 285 (2010) 25978–25986. [PMID: 20543190]
2.	Celis, A.I., Streit, B.R., Moraski, G.C., Kant, R., Lash, T.D., Lukat-Rodgers, G.S., Rodgers, K.R. and DuBois, J.L. Unusual peroxide-dependent, heme-transforming reaction catalyzed by HemQ. Biochemistry 54 (2015) 4022–4032. [PMID: 26083961]
3.	Hofbauer, S., Mlynek, G., Milazzo, L., Puhringer, D., Maresch, D., Schaffner, I., Furtmuller, P.G., Smulevich, G., Djinovic-Carugo, K. and Obinger, C. Hydrogen peroxide-mediated conversion of coproheme to heme b by HemQ-lessons from the first crystal structure and kinetic studies. FEBS J. 283 (2016) 4386–4401. [PMID: 27758026]
4.	Celis, A.I., Gauss, G.H., Streit, B.R., Shisler, K., Moraski, G.C., Rodgers, K.R., Lukat-Rodgers, G.S., Peters, J.W. and DuBois, J.L. Structure-based mechanism for oxidative decarboxylation reactions mediated by amino acids and heme propionates in coproheme decarboxylase (HemQ). J. Am. Chem. Soc. 139 (2017) 1900–1911. [PMID: 27936663]

[EC 1.3.98.5 created 2019]

1.3.98.6

Accepted name:

AdoMet-dependent heme synthase

Reaction:

Fe-coproporphyrin III + 2 S-adenosyl-L-methionine = protoheme + 2 CO₂ + 2 5′-deoxyadenosine + 2 L-methionine

Other name(s):

ahbD (gene name); SAM-dependent heme synthase

Systematic name:

Fe-coproporphyrin III:S-adenosyl-L-methionine oxidoreductase (decarboxylating)

Comments:

This radical AdoMet enzyme participates in a heme biosynthesis pathway found in archaea and sulfur-reducing bacteria. cf. EC 1.3.98.5, hydrogen peroxide-dependent heme synthase.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Bali, S., Lawrence, A.D., Lobo, S.A., Saraiva, L.M., Golding, B.T., Palmer, D.J., Howard, M.J., Ferguson, S.J. and Warren, M.J. Molecular hijacking of siroheme for the synthesis of heme and d1 heme. Proc. Natl. Acad. Sci. USA 108 (2011) 18260–18265. [DOI] [PMID: 21969545]
2.	Kuhner, M., Haufschildt, K., Neumann, A., Storbeck, S., Streif, J. and Layer, G. The alternative route to heme in the methanogenic archaeon Methanosarcina barkeri. Archaea 2014:327637 (2014). [DOI] [PMID: 24669201]

[EC 1.3.98.6 created 2019]

4.99.1.9

Accepted name:

coproporphyrin ferrochelatase

Reaction:

Fe-coproporphyrin III + 2 H⁺ = coproporphyrin III + Fe²⁺

Glossary:

Fe-coproporphyrin III = coproheme III

Other name(s):

hemH (gene name)

Systematic name:

protoheme ferro-lyase (protoporphyrin-forming)

Comments:

The enzyme, present in Gram-positive bacteria, participates in heme biosynthesis. It can also catalyse the reaction of EC 4.99.1.1, protoporphyrin IX ferrochelatase, at a much lower level.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	Hansson, M. and Hederstedt, L. Purification and characterisation of a water-soluble ferrochelatase from Bacillus subtilis. Eur. J. Biochem. 220 (1994) 201–208. [DOI] [PMID: 8119288]
2.	Al-Karadaghi, S., Hansson, M., Nikonov, S., Jonsson, B. and Hederstedt, L. Crystal structure of ferrochelatase: the terminal enzyme in heme biosynthesis. Structure 5 (1997) 1501–1510. [DOI] [PMID: 9384565]
3.	Hansson, M.D., Karlberg, T., Soderberg, C.A., Rajan, S., Warren, M.J., Al-Karadaghi, S., Rigby, S.E. and Hansson, M. Bacterial ferrochelatase turns human: Tyr¹³ determines the apparent metal specificity of Bacillus subtilis ferrochelatase. J. Biol. Inorg. Chem. 16 (2011) 235–242. [DOI] [PMID: 21052751]
4.	Dailey, H.A., Gerdes, S., Dailey, T.A., Burch, J.S. and Phillips, J.D. Noncanonical coproporphyrin-dependent bacterial heme biosynthesis pathway that does not use protoporphyrin. Proc. Natl. Acad. Sci. USA 112 (2015) 2210–2215. [DOI] [PMID: 25646457]

[EC 4.99.1.9 created 2016]