EC Number | Crystallization (Comment) | Organism |
---|---|---|
1.13.11.72 | in vitro reconstitution of activity and determination of the crystal structure of Cd2+-substituted PhpD in complex with the 2-hydroxyethylphosphonate substrate | Streptomyces viridochromogenes |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.14.99.50 | Y377F | site-directed mutagenesis, the single point mutation in EgtB completely uncouples substrate consumption from sulfoxide synthase activity with the native substrates hercynine and gamma-glutamyl cysteine, with EgtB exclusively oxidizing gamma-glutamyl cysteine to the sulfinic acid. Tyr377 is hydrogen bonded to a water molecule that coordinates to the iron | Mycobacterium avium |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
1.13.11.72 | Fe2+ | a mononuclear non-heme iron-dependent enzyme | Streptomyces viridochromogenes | |
1.13.11.73 | Fe2+ | a mononuclear non-heme iron-dependent enzyme. MPnS contains iron-binding residues at only the two histidines, raising the specter that either MPnS is a 2-His only enzyme or that the third ligand is not well conserved in the alignment | Nitrosopumilus maritimus | |
1.14.99.50 | Fe2+ | non-heme iron, required for catalysis, the active site iron is coordinated by a 3-His facial triad rather than a 2-His-1-Glu ligand set | Mycobacterium avium | |
1.14.99.52 | Fe2+ | non-heme iron, required for catalysis,residues in the HX3HXE motif might be involved in iron binding | Erwinia tasmaniensis |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.13.11.72 | 2-hydroxyethylphosphonate + O2 | Streptomyces viridochromogenes | - |
hydroxymethylphosphonate + formate | - |
ir | |
1.13.11.72 | 2-hydroxyethylphosphonate + O2 | Streptomyces viridochromogenes DSM 40736 | - |
hydroxymethylphosphonate + formate | - |
ir | |
1.13.11.73 | 2-hydroxyethylphosphonate + O2 | Nitrosopumilus maritimus | - |
methylphosphonate + HCO3- | - |
ir | |
1.14.99.50 | hercynine + gamma-L-glutamyl-L-cysteine + O2 | Mycobacterium avium | - |
gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide + H2O | - |
? | |
1.14.99.52 | L-histidine + L-cysteine + O2 | Erwinia tasmaniensis | - |
S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.13.11.72 | Streptomyces viridochromogenes | Q5IW40 | - |
- |
1.13.11.72 | Streptomyces viridochromogenes DSM 40736 | Q5IW40 | - |
- |
1.13.11.73 | Nitrosopumilus maritimus | - |
- |
- |
1.14.99.50 | Mycobacterium avium | - |
- |
- |
1.14.99.52 | Erwinia tasmaniensis | - |
- |
- |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
1.13.11.72 | 2-hydroxyethylphosphonate + O2 = hydroxymethylphosphonate + formate | initial substrate oxidation by a ferric-superoxo-intermediate and a second oxidation by a ferryl species, catalytic mechanism, detailed overview | Streptomyces viridochromogenes | |
1.13.11.73 | 2-hydroxyethylphosphonate + O2 = methylphosphonate + HCO3- | initial substrate oxidation by a ferric-superoxo-intermediate and a second oxidation by a ferryl species, catalytic mechanism, detailed overview | Nitrosopumilus maritimus |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.13.11.72 | 2-hydroxyethylphosphonate + O2 | - |
Streptomyces viridochromogenes | hydroxymethylphosphonate + formate | - |
ir | |
1.13.11.72 | 2-hydroxyethylphosphonate + O2 | an irreversible step involving O2 | Streptomyces viridochromogenes | hydroxymethylphosphonate + formate | - |
ir | |
1.13.11.72 | 2-hydroxyethylphosphonate + O2 | - |
Streptomyces viridochromogenes DSM 40736 | hydroxymethylphosphonate + formate | - |
ir | |
1.13.11.72 | 2-hydroxyethylphosphonate + O2 | an irreversible step involving O2 | Streptomyces viridochromogenes DSM 40736 | hydroxymethylphosphonate + formate | - |
ir | |
1.13.11.72 | additional information | HEPD oxidizes a relatively unactivated substrate that cannot easily facilitate O2 activation. 2-Hydroxyethylphosphonate does not contain a thiol group that upon binding to the iron can activate it for catalysis, nor does it contain an 2-oxo acid functionality | Streptomyces viridochromogenes | ? | - |
? | |
1.13.11.72 | additional information | HEPD oxidizes a relatively unactivated substrate that cannot easily facilitate O2 activation. 2-Hydroxyethylphosphonate does not contain a thiol group that upon binding to the iron can activate it for catalysis, nor does it contain an 2-oxo acid functionality | Streptomyces viridochromogenes DSM 40736 | ? | - |
? | |
1.13.11.73 | 2-hydroxyethylphosphonate + O2 | - |
Nitrosopumilus maritimus | methylphosphonate + HCO3- | - |
ir | |
1.13.11.73 | 2-hydroxyethylphosphonate + O2 | the pro-(R) hydrogen at C2 of 2-hydroxyethylphosphonate is quantitatively incorporated by enzyme MPnS into methylphosphonate. AN irreversible step involving O2 | Nitrosopumilus maritimus | methylphosphonate + HCO3- | - |
ir | |
1.14.99.50 | hercynine + gamma-L-glutamyl-L-cysteine + O2 | - |
Mycobacterium avium | gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide + H2O | - |
? | |
1.14.99.50 | hercynine + gamma-L-glutamyl-L-cysteine + O2 | sulfoxide incorporation at C2 by EgtB | Mycobacterium avium | gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide + H2O | - |
? | |
1.14.99.50 | additional information | no activity with L-cysteine and L-histdine | Mycobacterium avium | ? | - |
? | |
1.14.99.52 | L-histidine + L-cysteine + O2 | - |
Erwinia tasmaniensis | S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O | - |
? | |
1.14.99.52 | L-histidine + L-cysteine + O2 | OvoA modifies the C5 position of the imidazole ring of L-His, site selectivity of the transformation | Erwinia tasmaniensis | S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O | - |
? | |
1.14.99.52 | additional information | OvoA incubated with hercynine (the normal substrate for EgtB, EC 1.14.99.50) and cysteine produces primarily cysteine sulfinic acid, the product of cysteine dioxygenase-type chemistry, cf. EC 1.13.11.20 | Erwinia tasmaniensis | ? | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.13.11.72 | HEPD | - |
Streptomyces viridochromogenes |
1.13.11.72 | phpD | - |
Streptomyces viridochromogenes |
1.13.11.73 | methylphosphonate synthase | - |
Nitrosopumilus maritimus |
1.13.11.73 | mpnS | - |
Nitrosopumilus maritimus |
1.14.99.50 | 5-histidylcysteine sulfoxide synthase | - |
Mycobacterium avium |
1.14.99.50 | EgtB | - |
Mycobacterium avium |
1.14.99.52 | OvoA | - |
Erwinia tasmaniensis |
1.14.99.52 | sulfoxide synthase | - |
Erwinia tasmaniensis |
EC Number | General Information | Comment | Organism |
---|---|---|---|
1.13.11.72 | evolution | one group of mononuclear non-heme iron-dependent enzymes includes 2-hydroxyethylphosphonate dioxygenase (HEPD) and methylphosphonate synthase (MPnS, EC 1.13.11.73) that both carry out the oxidative cleavage of the carbon-carbon bond of 2-hydroxyethylphosphonate but generate different products. Common properties include the initial substrate oxidation by a ferric-superoxo-intermediate and a second oxidation by a ferryl species. Sequence homology between HEPD and MPnS combined with identical requirements for catalysis suggests a consensus mechanism in which product identity is determined by branching at an intermediate in the catalytic cycle | Streptomyces viridochromogenes |
1.13.11.72 | additional information | the active site metal is coordinated by 2-His-1-Glu on one face of a pseudooctrahedron | Streptomyces viridochromogenes |
1.13.11.73 | evolution | one group of mononuclear non-heme iron-dependent enzymes includes 2-hydroxyethylphosphonate dioxygenase (HEPD, EC 1.13.11.72) and methylphosphonate synthase (MPnS) that both carry out the oxidative cleavage of the carbon-carbon bond of 2-hydroxyethylphosphonate but generate different products. Common properties include the initial substrate oxidation by a ferric-superoxo-intermediate and a second oxidation by a ferryl species. Sequence homology between HEPD and MPnS combined with identical requirements for catalysis suggests a consensus mechanism in which product identity is determined by branching at an intermediate in the catalytic cycle | Nitrosopumilus maritimus |
1.13.11.73 | additional information | apo MPnS homology modeling using the crystal structure of Cd2+-substituted HEPD, EC 1.13.11.72, in complex with substrate 2-hydroxyethylphosphonate, PDB ID 3GBF | Nitrosopumilus maritimus |
1.14.99.50 | evolution | EgtB contains a strongly conserved HX3HXE motif, implying that it is a member of the facial triad enzyme family with the Fe(II) site ligated by 2-His-1-Glu | Mycobacterium avium |
1.14.99.52 | malfunction | mutation of any of the residues in the HX3HXE motif in OvoA results in an over 100fold attenuation of activity | Erwinia tasmaniensis |
1.14.99.52 | additional information | residues in the HX3HXE motif are catalytically important (i.e., likely bind iron). Structure homology modeling, overview | Erwinia tasmaniensis |