DB code: D00483
| CATH domain | 1.-.-.- : | Catalytic domain |
|---|---|---|
| 1.10.640.10 : Myeloperoxidase, subunit C | Catalytic domain | |
| E.C. | 1.11.1.7 | |
| CSA | 1mhl | |
| M-CSA | 1mhl | |
| MACiE | ||
| CATH domain | Related DB codes (homologues) |
|---|
| Uniprot Enzyme Name | UniprotKB | Protein name | Synonyms | Contains | RefSeq | Pfam |
|---|---|---|---|---|---|
| P05164 |
Myeloperoxidase
|
MPO
EC 1.11.1.7 |
89 kDa myeloperoxidase
84 kDa myeloperoxidase Myeloperoxidase light chain Myeloperoxidase heavy chain |
NP_000241.1
(Protein)
NM_000250.1 (DNA/RNA sequence) |
PF03098
(An_peroxidase)
[Graphical View] |
| KEGG enzyme name |
|---|
|
peroxidase
myeloperoxidase lactoperoxidase verdoperoxidase guaiacol peroxidase thiocyanate peroxidase eosinophil peroxidase Japanese radish peroxidase horseradish peroxidase (HRP) extensin peroxidase heme peroxidase MPO oxyperoxidase protoheme peroxidase pyrocatechol peroxidase scopoletin peroxidase |
| UniprotKB: Accession Number | Entry name | Activity | Subunit | Subcellular location | Cofactor |
|---|---|---|---|---|---|
| P05164 | PERM_HUMAN | Donor + H(2)O(2) = oxidized donor + 2 H(2)O. Cl(-) + H(2)O(2) = HOCl + 2 H(2)O. | Tetramer of two light chains and two heavy chains. | Lysosome. | Binds 1 calcium ion per heterodimer. Binds 1 heme B (iron-protoporphyrin IX) group covalently per heterodimer. |
| KEGG Pathways | Map code | Pathways | E.C. |
|---|---|---|
| MAP00360 | Phenylalanine metabolism | |
| MAP00680 | Methane metabolism | |
| MAP00940 | Phenylpropanoid biosynthesis |
| Compound table | ||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Cofactors | Substrates | Products | Intermediates | |||||||||||
| KEGG-id | C00032 | C00076 | C01351 | C00027 | C00115 | C02177 | C00001 | C99999 | ||||||
| E.C. | ||||||||||||||
| Compound | Heme | Calcium | Donor | H2O2 | Chloride | Oxidized donor | H2O | Hypochlorite | ||||||
| Type | aromatic ring (with nitrogen atoms),carboxyl group,heavy metal | divalent metal (Ca2+, Mg2+) | others | others | halide | others | H2O | halide | ||||||
| ChEBI |
17627 26355 17627 26355 |
29108 29108 |
16240 16240 |
15377 15377 |
||||||||||
| PubChem |
271 271 |
22326046 784 22326046 784 |
22247451 962 22247451 962 |
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| 1cxpA |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1cxpB |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1d2vA |
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Unbound | Unbound | Unbound | Unbound | Analogue:_BR_843 | Unbound | Unbound | ||
| 1d2vB |
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Unbound | Unbound | Unbound | Unbound | Analogue:_BR_843 | Unbound | Unbound | ||
| 1d5lA |
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Unbound | Unbound | Analogue:CYN_1844 | Unbound | Unbound | Unbound | Unbound | ||
| 1d5lB |
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Unbound | Unbound | Analogue:CYN_1844 | Unbound | Unbound | Unbound | Unbound | ||
| 1d7wA |
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Unbound | Unbound | Analogue:CYN | Unbound | Analogue:_BR_957 | Unbound | Unbound | ||
| 1d7wB |
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Unbound | Unbound | Analogue:CYN | Unbound | Analogue:_BR_957 | Unbound | Unbound | ||
| 1dnuA |
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Unbound | Unbound | Analogue:SCN_5 | Unbound | Unbound | Unbound | Unbound | ||
| 1dnuB |
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Unbound | Unbound | Analogue:SCN_4 | Unbound | Unbound | Unbound | Unbound | ||
| 1dnwA |
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Unbound | Unbound | Analogue:CYN_3 | Unbound | Unbound | Unbound | Unbound | ||
| 1dnwB |
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Unbound | Unbound | Analogue:CYN_4 | Unbound | Unbound | Unbound | Unbound | ||
| 1mhlA |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1mhlB |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1mypA |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1mypB |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1cxpC |
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Bound:HEM | Bound:_CA | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1cxpD |
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Bound:HEM | Bound:_CA | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1d2vC |
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Bound:HEM | Bound:_CA | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1d2vD |
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Bound:HEM | Bound:_CA | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1d5lC |
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Bound:HEM | Bound:_CA | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1d5lD |
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Bound:HEM | Bound:_CA | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1d7wC |
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Bound:HEM | Bound:_CA | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1d7wD |
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Bound:HEM | Bound:_CA | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1dnuC |
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Bound:HEM | Bound:_CA | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1dnuD |
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Bound:HEM | Bound:_CA | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1dnwC |
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Bound:HEM | Bound:_CA | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1dnwD |
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Bound:HEM | Bound:_CA | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1mhlC |
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Bound:HEM | Bound:_CA | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1mhlD |
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Bound:HEM | Bound:_CA | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1mypC |
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Bound:HEM | Bound:_CA | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1mypD |
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Bound:HEM | Bound:_CA | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| Reference for Active-site residues | ||
|---|---|---|
| resource | references | E.C. |
| Swiss-prot;P05164 & literature [5], [10], [11] | ||
| Active-site residues | ||||||||||
|---|---|---|---|---|---|---|---|---|---|---|
| PDB | Catalytic residues | Cofactor-binding residues | Modified residues | Main-chain involved in catalysis | Comment | |||||
| 1cxpA |
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GLN 91;HIS 95 | ASP 94(Heme);ASP 96(Calcium) | |||
| 1cxpB |
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GLN 91;HIS 95 | ASP 94(Heme);ASP 96(Calcium) | |||
| 1d2vA |
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GLN 91;HIS 95 | ASP 94(Heme);ASP 96(Calcium) | |||
| 1d2vB |
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GLN 91;HIS 95 | ASP 94(Heme);ASP 96(Calcium) | |||
| 1d5lA |
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GLN 91;HIS 95 | ASP 94(Heme);ASP 96(Calcium) | |||
| 1d5lB |
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GLN 91;HIS 95 | ASP 94(Heme);ASP 96(Calcium) | |||
| 1d7wA |
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GLN 91;HIS 95 | ASP 94(Heme);ASP 96(Calcium) | |||
| 1d7wB |
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GLN 91;HIS 95 | ASP 94(Heme);ASP 96(Calcium) | |||
| 1dnuA |
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GLN 91;HIS 95 | ASP 94(Heme);ASP 96(Calcium) | |||
| 1dnuB |
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GLN 91;HIS 95 | ASP 94(Heme);ASP 96(Calcium) | |||
| 1dnwA |
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GLN 91;HIS 95 | ASP 94(Heme);ASP 96(Calcium) | |||
| 1dnwB |
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GLN 91;HIS 95 | ASP 94(Heme);ASP 96(Calcium) | |||
| 1mhlA |
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GLN 91;HIS 95 | ASP 94(Heme);ASP 96(Calcium) | |||
| 1mhlB |
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GLN 91;HIS 95 | ASP 94(Heme);ASP 96(Calcium) | |||
| 1mypA |
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GLN 91;HIS 95 | ASP 94(Heme);ASP 96(Calcium) | |||
| 1mypB |
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GLN 91;HIS 95 | ASP 94(Heme);ASP 96(Calcium) | |||
| 1cxpC |
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ARG 239 | GLU 242;MET 243(Heme);HIS 336(Heme iron);THR 168;PHE 170;ASP 172;SER 174(Calcium) | CSO 150(Cysteine sulfenic acid) | ||
| 1cxpD |
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ARG 239 | GLU 242;MET 243(Heme);HIS 336(Heme iron);THR 168;PHE 170;ASP 172;SER 174(Calcium) | CSO 150(Cysteine sulfenic acid) | ||
| 1d2vC |
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ARG 239 | GLU 242;MET 243(Heme);HIS 336(Heme iron);THR 168;PHE 170;ASP 172;SER 174(Calcium) | CSO 150(Cysteine sulfenic acid) | ||
| 1d2vD |
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ARG 239 | GLU 242;MET 243(Heme);HIS 336(Heme iron);THR 168;PHE 170;ASP 172;SER 174(Calcium) | CSO 150(Cysteine sulfenic acid) | ||
| 1d5lC |
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ARG 239 | GLU 242;MET 243(Heme);HIS 336(Heme iron);THR 168;PHE 170;ASP 172;SER 174(Calcium) | CSO 150(Cysteine sulfenic acid) | ||
| 1d5lD |
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ARG 239 | GLU 242;MET 243(Heme);HIS 336(Heme iron);THR 168;PHE 170;ASP 172;SER 174(Calcium) | CSO 150(Cysteine sulfenic acid) | ||
| 1d7wC |
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ARG 239 | GLU 242;MET 243(Heme);HIS 336(Heme iron);THR 168;PHE 170;ASP 172;SER 174(Calcium) | CSO 150(Cysteine sulfenic acid) | ||
| 1d7wD |
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ARG 239 | GLU 242;MET 243(Heme);HIS 336(Heme iron);THR 168;PHE 170;ASP 172;SER 174(Calcium) | CSO 150(Cysteine sulfenic acid) | ||
| 1dnuC |
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ARG 239 | GLU 242;MET 243(Heme);HIS 336(Heme iron);THR 168;PHE 170;ASP 172;SER 174(Calcium) | CSO 150(Cysteine sulfenic acid) | ||
| 1dnuD |
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ARG 239 | GLU 242;MET 243(Heme);HIS 336(Heme iron);THR 168;PHE 170;ASP 172;SER 174(Calcium) | CSO 150(Cysteine sulfenic acid) | ||
| 1dnwC |
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ARG 239 | GLU 242;MET 243(Heme);HIS 336(Heme iron);THR 168;PHE 170;ASP 172;SER 174(Calcium) | CSO 150(Cysteine sulfenic acid) | ||
| 1dnwD |
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ARG 239 | GLU 242;MET 243(Heme);HIS 336(Heme iron);THR 168;PHE 170;ASP 172;SER 174(Calcium) | CSO 150(Cysteine sulfenic acid) | ||
| 1mhlC |
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ARG 239 | GLU 242;MET 243(Heme);HIS 336(Heme iron);THR 168;PHE 170;ASP 172;SER 174(Calcium) | CYS 150(Cysteine sulfenic acid) | ||
| 1mhlD |
|
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ARG 239 | GLU 242;MET 243(Heme);HIS 336(Heme iron);THR 168;PHE 170;ASP 172;SER 174(Calcium) | CYS 150(Cysteine sulfenic acid) | ||
| 1mypC |
|
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|
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ARG 239 | GLU 242;MET 243(Heme);HIS 336(Heme iron);THR 168;PHE 170;ASP 172;SER 174(Calcium) | CYS 150(Cysteine sulfenic acid) | ||
| 1mypD |
|
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ARG 239 | GLU 242;MET 243(Heme);HIS 336(Heme iron);THR 168;PHE 170;ASP 172;SER 174(Calcium) | CYS 150(Cysteine sulfenic acid) | ||
| References for Catalytic Mechanism | ||
|---|---|---|
| References | Sections | No. of steps in catalysis |
|
[5]
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||
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[6]
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||
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[10]
|
Fig.3 | |
|
[11]
|
p.10970-10973 | |
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[12]
|
SCHEME IV, p.5004 | |
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[17]
|
Scheme 1, p.1178 | |
|
[18]
|
p.11964 | |
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[22]
|
||
| References | |
|---|---|
| [1] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 2824790 |
| Journal | J Mol Biol |
| Year | 1987 |
| Volume | 196 |
| Pages | 919-25 |
| Authors | Fenna RE |
| Title | Crystallization and subunit structure of canine myeloperoxidase. |
| Related PDB | |
| Related UniProtKB | |
| [2] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 2832613 |
| Journal | J Mol Biol |
| Year | 1988 |
| Volume | 199 |
| Pages | 395-6 |
| Authors | Sutton BJ, Little C, Olsen RL, Willassen NP |
| Title | Preliminary crystallographic analysis of human myeloperoxidase. |
| Related PDB | |
| Related UniProtKB | |
| [3] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 2559209 |
| Journal | J Mol Biol |
| Year | 1989 |
| Volume | 210 |
| Pages | 681-3 |
| Authors | Zeng J, Fenna RE |
| Title | Tetragonal crystals of canine myeloperoxidase suitable for X-ray structural analysis. |
| Related PDB | |
| Related UniProtKB | |
| [4] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 1321726 |
| Journal | FEBS Lett |
| Year | 1992 |
| Volume | 302 |
| Pages | 189-91 |
| Authors | Jacquet A, Deleersnyder V, Garcia-Quintana L, Bollen A, Moguilevsky N |
| Title |
Site-directed mutants of human myeloperoxidase. |
| Related PDB | |
| Related UniProtKB | |
| [5] | |
| Resource | |
| Comments | X-ray crystallography |
| Medline ID | |
| PubMed ID | 1320128 |
| Journal | J Mol Biol |
| Year | 1992 |
| Volume | 226 |
| Pages | 185-207 |
| Authors | Zeng J, Fenna RE |
| Title | X-ray crystal structure of canine myeloperoxidase at 3 A resolution. |
| Related PDB | 1myp |
| Related UniProtKB | |
| [6] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 8037771 |
| Journal | Biochem Biophys Res Commun |
| Year | 1994 |
| Volume | 202 |
| Pages | 73-81 |
| Authors | Jacquet A, Garcia-Quintana L, Deleersnyder V, Fenna R, Bollen A, Moguilevsky N |
| Title | Site-directed mutagenesis of human myeloperoxidase: further identification of residues involved in catalytic activity and heme interaction. |
| Related PDB | |
| Related UniProtKB | |
| [7] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 8062820 |
| Journal | EMBO J |
| Year | 1994 |
| Volume | 13 |
| Pages | 3438-47 |
| Authors | Nelson RE, Fessler LI, Takagi Y, Blumberg B, Keene DR, Olson PF, Parker CG, Fessler JH |
| Title | Peroxidasin: a novel enzyme-matrix protein of Drosophila development. |
| Related PDB | |
| Related UniProtKB | |
| [8] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 8020506 |
| Journal | Eur J Biochem |
| Year | 1994 |
| Volume | 222 |
| Pages | 677-85 |
| Authors | Floris R, Kim Y, Babcock GT, Wever R |
| Title |
Optical spectrum of myeloperoxidase. |
| Related PDB | |
| Related UniProtKB | |
| [9] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 8132563 |
| Journal | J Biol Chem |
| Year | 1994 |
| Volume | 269 |
| Pages | 8388-92 |
| Authors | Hori H, Fenna RE, Kimura S, Ikeda-Saito M |
| Title | Aromatic substrate molecules bind at the distal heme pocket of myeloperoxidase. |
| Related PDB | |
| Related UniProtKB | |
| [10] | |
| Resource | |
| Comments | X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 167-744 |
| Medline ID | 95142692 |
| PubMed ID | 7840679 |
| Journal | Arch Biochem Biophys |
| Year | 1995 |
| Volume | 316 |
| Pages | 653-6 |
| Authors | Fenna R, Zeng J, Davey C |
| Title | Structure of the green heme in myeloperoxidase. |
| Related PDB | 1mhl |
| Related UniProtKB | P05164 |
| [11] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 8718890 |
| Journal | Biochemistry |
| Year | 1996 |
| Volume | 35 |
| Pages | 10967-73 |
| Authors | Davey CA, Fenna RE |
| Title | 2.3 A resolution X-ray crystal structure of the bisubstrate analogue inhibitor salicylhydroxamic acid bound to human myeloperoxidase: a model for a prereaction complex with hydrogen peroxide. |
| Related PDB | |
| Related UniProtKB | |
| [12] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 9478947 |
| Journal | J Biol Chem |
| Year | 1998 |
| Volume | 273 |
| Pages | 4997-5005 |
| Authors | Hazen SL, d'Avignon A, Anderson MM, Hsu FF, Heinecke JW |
| Title |
Human neutrophils employ the myeloperoxidase-hydrogen peroxide-chloride system to oxidize alpha-amino acids to a family of reactive aldehydes. |
| Related PDB | |
| Related UniProtKB | |
| [13] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 10395733 |
| Journal | Arch Biochem Biophys |
| Year | 1999 |
| Volume | 367 |
| Pages | 173-84 |
| Authors | Nomura K, Hoshino K, Suzuki N |
| Title | The primary and higher order structures of sea urchin ovoperoxidase as determined by cDNA cloning and predicted by homology modeling. |
| Related PDB | |
| Related UniProtKB | |
| [14] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 10585414 |
| Journal | J Biol Chem |
| Year | 1999 |
| Volume | 274 |
| Pages | 35441-8 |
| Authors | Lardinois OM, Medzihradszky KF, Ortiz de Montellano PR |
| Title | Spin trapping and protein cross-linking of the lactoperoxidase protein radical. |
| Related PDB | |
| Related UniProtKB | |
| [15] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 10069970 |
| Journal | J Exp Biol |
| Year | 1999 |
| Volume | 202 |
| Pages | 809-16 |
| Authors | Ribeiro JM, Valenzuela JG |
| Title | Purification and cloning of the salivary peroxidase/catechol oxidase of the mosquito Anopheles albimanus. |
| Related PDB | |
| Related UniProtKB | |
| [16] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 10805914 |
| Journal | Biopolymers |
| Year | 2000 |
| Volume | 57 |
| Pages | 169-78 |
| Authors | Araki K, Takeuchi H |
| Title | Effects of pH and chloride concentration on resonance Raman spectra of human myeloperoxidase and Raman microspectroscopic analysis of enzyme state in azurophilic granules. |
| Related PDB | |
| Related UniProtKB | |
| [17] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 11087440 |
| Journal | Chem Res Toxicol |
| Year | 2000 |
| Volume | 13 |
| Pages | 1174-80 |
| Authors | Stansbury KH, Noll DM, Groopman JD, Trush MA |
| Title | Enzyme-mediated dialdehyde formation: an alternative pathway for benzo[a]pyrene 7,8-dihydrodiol bioactivation. |
| Related PDB | |
| Related UniProtKB | |
| [18] | |
| Resource | |
| Comments | X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 167-744 |
| Medline ID | 20229799 |
| PubMed ID | 10766826 |
| Journal | J Biol Chem |
| Year | 2000 |
| Volume | 275 |
| Pages | 11964-71 |
| Authors | Fiedler TJ, Davey CA, Fenna RE |
| Title | X-ray crystal structure and characterization of halide-binding sites of human myeloperoxidase at 1.8 A resolution. |
| Related PDB | 1cxp 1d2v |
| Related UniProtKB | P05164 |
| [19] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 10994874 |
| Journal | Redox Rep |
| Year | 2000 |
| Volume | 5 |
| Pages | 197-206 |
| Authors | Nauseef WM, McCormick S, Goedken M |
| Title | Impact of missense mutations on biosynthesis of myeloperoxidase. |
| Related PDB | |
| Related UniProtKB | |
| [20] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 11159195 |
| Journal | Am J Pathol |
| Year | 2001 |
| Volume | 158 |
| Pages | 581-92 |
| Authors | Yang JJ, Preston GA, Pendergraft WF, Segelmark M, Heeringa P, Hogan SL, Jennette JC, Falk RJ |
| Title | Internalization of proteinase 3 is concomitant with endothelial cell apoptosis and internalization of myeloperoxidase with generation of intracellular oxidants. |
| Related PDB | |
| Related UniProtKB | |
| [21] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 11237766 |
| Journal | Biochem Biophys Res Commun |
| Year | 2001 |
| Volume | 281 |
| Pages | 1024-9 |
| Authors | Shin K, Hayasawa H, Lonnerdal B |
| Title | Mutations affecting the calcium-binding site of myeloperoxidase and lactoperoxidase. |
| Related PDB | |
| Related UniProtKB | |
| [22] | |
| Resource | |
| Comments | X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 167-744 |
| Medline ID | 21562373 |
| PubMed ID | 11705390 |
| Journal | Biochemistry |
| Year | 2001 |
| Volume | 40 |
| Pages | 13990-7 |
| Authors | Blair-Johnson M, Fiedler T, Fenna R |
| Title | Human myeloperoxidase: structure of a cyanide complex and its interaction with bromide and thiocyanate substrates at 1.9 A resolution. |
| Related PDB | 1d5l 1d7w 1dnu 1dnw |
| Related UniProtKB | P05164 |
| [23] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 11513872 |
| Journal | FEBS Lett |
| Year | 2001 |
| Volume | 503 |
| Pages | 147-50 |
| Authors | Furtmuller PG, Jantschko W, Regelsberger G, Jakopitsch C, Moguilevsky N, Obinger C |
| Title | A transient kinetic study on the reactivity of recombinant unprocessed monomeric myeloperoxidase. |
| Related PDB | |
| Related UniProtKB | |
| Comments |
|---|
|
This enzyme is composed of light chain (chain A or B in PDB) and heavy chain (chain C or D in PDB).
Although this enzyme binds a calcium ion, |
| Created | Updated |
|---|---|
| 2005-04-04 | 2009-02-26 |