BRENDA - Enzyme Database show
show all sequences of 1.14.99.52

Convergent evolution of ergothioneine biosynthesis in cyanobacteria

Liao, C.; Seebeck, F.P.; ChemBioChem 18, 2115-2118 (2017)

Data extracted from this reference:

Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Fe2+
an iron-dependent sulfoxide synthase
Erwinia tasmaniensis
Fe2+
an iron-dependent sulfoxide synthase
Microcystis aeruginosa
Fe2+
an iron-dependent sulfoxide synthase; an iron-dependent sulfoxide synthase
Moorea producens
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
hercynine + gamma-L-glutamyl-L-cysteine + O2
Moorea producens
-
gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
-
-
?
hercynine + gamma-L-glutamyl-L-cysteine + O2
Moorea producens PAL-8-15-08-1
-
gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
-
-
?
L-histidine + L-cysteine + O2
Moorea producens
-
S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O
-
-
?
L-histidine + L-cysteine + O2
Moorea producens PAL-8-15-08-1
-
S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O
-
-
?
additional information
Moorea producens
an OvoA-like protein, full-length OvoA homologue, OvoA_2, is a monofunctional sulfoxide synthase
?
-
-
-
additional information
Microcystis aeruginosa
short cyanobacterial OvoA-type enzymes may contribute to ergothioneine (EC 1.14.99.51) instead of ovothiol production
?
-
-
-
additional information
Erwinia tasmaniensis
the ovothiol biosynthetic sulfoxide synthase OvoA from Erwinia tasmaniensis (OvoAErwin) is a promiscuous enzyme. This enzyme is most efficient in making its native product S-(L-histidin-5-yl)-L-cysteine S-oxide, but, when presented with N-alpha-trimethylhistidine as a sulfur acceptor, the enzyme switches product specificity and produces gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide albeit with significantly lower efficiency
?
-
-
-
additional information
Moorea producens PAL-8-15-08-1
an OvoA-like protein, full-length OvoA homologue, OvoA_2, is a monofunctional sulfoxide synthase
?
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Erwinia tasmaniensis
-
-
-
Microcystis aeruginosa
-
-
-
Moorea producens
A0A1D8U0C7
-
-
Moorea producens
A0A1D8U386
-
-
Moorea producens PAL-8-15-08-1
A0A1D8U0C7
-
-
Moorea producens PAL-8-15-08-1
A0A1D8U386
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
hercynine + gamma-L-glutamyl-L-cysteine + O2
-
744709
Moorea producens
gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
-
-
-
?
hercynine + gamma-L-glutamyl-L-cysteine + O2
-
744709
Moorea producens PAL-8-15-08-1
gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
-
-
-
?
L-histidine + L-cysteine + O2
-
744709
Microcystis aeruginosa
S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O
-
-
-
?
L-histidine + L-cysteine + O2
-
744709
Moorea producens
S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O
-
-
-
?
L-histidine + L-cysteine + O2
-
744709
Erwinia tasmaniensis
S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O
-
-
-
?
L-histidine + L-cysteine + O2
-
744709
Moorea producens PAL-8-15-08-1
S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O
-
-
-
?
additional information
an OvoA-like protein, full-length OvoA homologue, OvoA_2, is a monofunctional sulfoxide synthase
744709
Moorea producens
?
-
-
-
-
additional information
short cyanobacterial OvoA-type enzymes may contribute to ergothioneine (EC 1.14.99.51) instead of ovothiol production
744709
Microcystis aeruginosa
?
-
-
-
-
additional information
the ovothiol biosynthetic sulfoxide synthase OvoA from Erwinia tasmaniensis (OvoAErwin) is a promiscuous enzyme. This enzyme is most efficient in making its native product S-(L-histidin-5-yl)-L-cysteine S-oxide, but, when presented with N-alpha-trimethylhistidine as a sulfur acceptor, the enzyme switches product specificity and produces gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide albeit with significantly lower efficiency
744709
Erwinia tasmaniensis
?
-
-
-
-
additional information
in a competitive reaction containing 1 mM of each histidine, N-alpha-trimethylhistidine, and cysteine, OvoAErwin produces only S-(L-histidin-5-yl)-L-cysteine S-oxide, whereas OvoAErw-NW and EgtB(ovo) produce exclusively gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide
744709
Moorea producens
?
-
-
-
-
additional information
an OvoA-like protein, full-length OvoA homologue, OvoA_2, is a monofunctional sulfoxide synthase
744709
Moorea producens PAL-8-15-08-1
?
-
-
-
-
additional information
in a competitive reaction containing 1 mM of each histidine, N-alpha-trimethylhistidine, and cysteine, OvoAErwin produces only S-(L-histidin-5-yl)-L-cysteine S-oxide, whereas OvoAErw-NW and EgtB(ovo) produce exclusively gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide
744709
Moorea producens PAL-8-15-08-1
?
-
-
-
-
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Fe2+
an iron-dependent sulfoxide synthase
Erwinia tasmaniensis
Fe2+
an iron-dependent sulfoxide synthase
Microcystis aeruginosa
Fe2+
an iron-dependent sulfoxide synthase
Moorea producens
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
hercynine + gamma-L-glutamyl-L-cysteine + O2
Moorea producens
-
gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
-
-
?
hercynine + gamma-L-glutamyl-L-cysteine + O2
Moorea producens PAL-8-15-08-1
-
gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
-
-
?
L-histidine + L-cysteine + O2
Moorea producens
-
S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O
-
-
?
L-histidine + L-cysteine + O2
Moorea producens PAL-8-15-08-1
-
S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O
-
-
?
additional information
Moorea producens
an OvoA-like protein, full-length OvoA homologue, OvoA_2, is a monofunctional sulfoxide synthase
?
-
-
-
additional information
Microcystis aeruginosa
short cyanobacterial OvoA-type enzymes may contribute to ergothioneine (EC 1.14.99.51) instead of ovothiol production
?
-
-
-
additional information
Erwinia tasmaniensis
the ovothiol biosynthetic sulfoxide synthase OvoA from Erwinia tasmaniensis (OvoAErwin) is a promiscuous enzyme. This enzyme is most efficient in making its native product S-(L-histidin-5-yl)-L-cysteine S-oxide, but, when presented with N-alpha-trimethylhistidine as a sulfur acceptor, the enzyme switches product specificity and produces gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide albeit with significantly lower efficiency
?
-
-
-
additional information
Moorea producens PAL-8-15-08-1
an OvoA-like protein, full-length OvoA homologue, OvoA_2, is a monofunctional sulfoxide synthase
?
-
-
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
hercynine + gamma-L-glutamyl-L-cysteine + O2
-
744709
Moorea producens
gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
-
-
-
?
hercynine + gamma-L-glutamyl-L-cysteine + O2
-
744709
Moorea producens PAL-8-15-08-1
gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
-
-
-
?
L-histidine + L-cysteine + O2
-
744709
Microcystis aeruginosa
S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O
-
-
-
?
L-histidine + L-cysteine + O2
-
744709
Moorea producens
S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O
-
-
-
?
L-histidine + L-cysteine + O2
-
744709
Erwinia tasmaniensis
S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O
-
-
-
?
L-histidine + L-cysteine + O2
-
744709
Moorea producens PAL-8-15-08-1
S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O
-
-
-
?
additional information
an OvoA-like protein, full-length OvoA homologue, OvoA_2, is a monofunctional sulfoxide synthase
744709
Moorea producens
?
-
-
-
-
additional information
short cyanobacterial OvoA-type enzymes may contribute to ergothioneine (EC 1.14.99.51) instead of ovothiol production
744709
Microcystis aeruginosa
?
-
-
-
-
additional information
the ovothiol biosynthetic sulfoxide synthase OvoA from Erwinia tasmaniensis (OvoAErwin) is a promiscuous enzyme. This enzyme is most efficient in making its native product S-(L-histidin-5-yl)-L-cysteine S-oxide, but, when presented with N-alpha-trimethylhistidine as a sulfur acceptor, the enzyme switches product specificity and produces gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide albeit with significantly lower efficiency
744709
Erwinia tasmaniensis
?
-
-
-
-
additional information
in a competitive reaction containing 1 mM of each histidine, N-alpha-trimethylhistidine, and cysteine, OvoAErwin produces only S-(L-histidin-5-yl)-L-cysteine S-oxide, whereas OvoAErw-NW and EgtB(ovo) produce exclusively gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide
744709
Moorea producens
?
-
-
-
-
additional information
an OvoA-like protein, full-length OvoA homologue, OvoA_2, is a monofunctional sulfoxide synthase
744709
Moorea producens PAL-8-15-08-1
?
-
-
-
-
additional information
in a competitive reaction containing 1 mM of each histidine, N-alpha-trimethylhistidine, and cysteine, OvoAErwin produces only S-(L-histidin-5-yl)-L-cysteine S-oxide, whereas OvoAErw-NW and EgtB(ovo) produce exclusively gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide
744709
Moorea producens PAL-8-15-08-1
?
-
-
-
-
General Information
General Information
Commentary
Organism
evolution
cyanobacterial OvoA homologues (Egt-B(ovo)) have evolved to catalyze an EgtB-type reaction by convergent evolution, cf. EC 1.14.99.50, in a competitive reaction containing 1 mM of each histidine, N-alpha-trimethylhistidine, and cysteine, OvoAErw-NW and EgtB(ovo) produce exclusively gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide. Because Erwinia tasmaniensis and most other OvoA encoding organisms do not encode an EgtD-type histidine methyltransferase, it seems clear that this N-alpha-trimethylhistidine-consuming side activity of OvoAErwin has no physiological purpose. Such promiscuity may have facilitated the transition of an ancestral sulfoxide synthase from ovothiol to erothioneine biosynthesis
Erwinia tasmaniensis
evolution
cyanobacterial OvoA homologues (Egt-B(ovo)) have evolved to catalyze an EgtB-type reaction by convergent evolution, cf. EC 1.14.99.50, in a competitive reaction containing 1 mM of each histidine, N-alpha-trimethylhistidine, and cysteine, OvoAErw-NW and EgtB(ovo) produce exclusively gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide
Microcystis aeruginosa
evolution
cyanobacterial OvoA homologues (Egt-B(ovo)) have evolved to catalyze an EgtB-type reaction by convergent evolution, cf. EC 1.14.99.50, in a competitive reaction containing 1 mM of each histidine, N-alpha-trimethylhistidine, and cysteine, OvoAErw-NW and EgtB(ovo) produce exclusively gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide; cyanobacterial OvoA homologues (Egt-B(ovo)) have evolved to catalyze an EgtB-type reaction by convergent evolution, cf. EC 1.14.99.50, in a competitive reaction containing 1 mM of each histidine, N-alpha-trimethylhistidine, and cysteine, OvoAErw-NW and EgtB(ovo) produce exclusively gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide
Moorea producens
metabolism
sulfoxide synthase OvoA catalyzes the formation of 5-histidylcysteine sulfoxide in the ovothiol biosynthesis. Short cyanobacterial OvoA-type enzymes may contribute to ergothioneine (EC 1.14.99.51) instead of ovothiol production
Erwinia tasmaniensis
metabolism
sulfoxide synthase OvoA catalyzes the formation of 5-histidylcysteine sulfoxide in the ovothiol biosynthesis. Short cyanobacterial OvoA-type enzymes may contribute to ergothioneine (EC 1.14.99.51) instead of ovothiol production
Microcystis aeruginosa
metabolism
sulfoxide synthase OvoA catalyzes the formation of 5-histidylcysteine sulfoxide in the ovothiol biosynthesis. Short cyanobacterial OvoA-type enzymes may contribute to ergothioneine (EC 1.14.99.51) instead of ovothiol production; sulfoxide synthase OvoA catalyzes the formation of 5-histidylcysteine sulfoxide in the ovothiol biosynthesis. Short cyanobacterial OvoA-type enzymes may contribute to ergothioneine (EC 1.14.99.51) instead of ovothiol production
Moorea producens
additional information
an OvoA-like protein, full-length OvoA homologue, OvoA_1, with a C-terminal methyltransferase, most OvoAs contain a C-terminal methyltransferase; homologue OvoA_2 is a monofunctional sulfoxide synthase without a C-terminal methyltransferase
Moorea producens
General Information (protein specific)
General Information
Commentary
Organism
evolution
cyanobacterial OvoA homologues (Egt-B(ovo)) have evolved to catalyze an EgtB-type reaction by convergent evolution, cf. EC 1.14.99.50, in a competitive reaction containing 1 mM of each histidine, N-alpha-trimethylhistidine, and cysteine, OvoAErw-NW and EgtB(ovo) produce exclusively gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide. Because Erwinia tasmaniensis and most other OvoA encoding organisms do not encode an EgtD-type histidine methyltransferase, it seems clear that this N-alpha-trimethylhistidine-consuming side activity of OvoAErwin has no physiological purpose. Such promiscuity may have facilitated the transition of an ancestral sulfoxide synthase from ovothiol to erothioneine biosynthesis
Erwinia tasmaniensis
evolution
cyanobacterial OvoA homologues (Egt-B(ovo)) have evolved to catalyze an EgtB-type reaction by convergent evolution, cf. EC 1.14.99.50, in a competitive reaction containing 1 mM of each histidine, N-alpha-trimethylhistidine, and cysteine, OvoAErw-NW and EgtB(ovo) produce exclusively gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide
Microcystis aeruginosa
evolution
cyanobacterial OvoA homologues (Egt-B(ovo)) have evolved to catalyze an EgtB-type reaction by convergent evolution, cf. EC 1.14.99.50, in a competitive reaction containing 1 mM of each histidine, N-alpha-trimethylhistidine, and cysteine, OvoAErw-NW and EgtB(ovo) produce exclusively gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide
Moorea producens
metabolism
sulfoxide synthase OvoA catalyzes the formation of 5-histidylcysteine sulfoxide in the ovothiol biosynthesis. Short cyanobacterial OvoA-type enzymes may contribute to ergothioneine (EC 1.14.99.51) instead of ovothiol production
Erwinia tasmaniensis
metabolism
sulfoxide synthase OvoA catalyzes the formation of 5-histidylcysteine sulfoxide in the ovothiol biosynthesis. Short cyanobacterial OvoA-type enzymes may contribute to ergothioneine (EC 1.14.99.51) instead of ovothiol production
Microcystis aeruginosa
metabolism
sulfoxide synthase OvoA catalyzes the formation of 5-histidylcysteine sulfoxide in the ovothiol biosynthesis. Short cyanobacterial OvoA-type enzymes may contribute to ergothioneine (EC 1.14.99.51) instead of ovothiol production
Moorea producens
additional information
an OvoA-like protein, full-length OvoA homologue, OvoA_1, with a C-terminal methyltransferase, most OvoAs contain a C-terminal methyltransferase
Moorea producens
additional information
homologue OvoA_2 is a monofunctional sulfoxide synthase without a C-terminal methyltransferase
Moorea producens
Other publictions for EC 1.14.99.52
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [C]
Temperature Range [C]
Temperature Stability [C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [C] (protein specific)
Temperature Range [C] (protein specific)
Temperature Stability [C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
744709
Liao
Convergent evolution of ergot ...
Erwinia tasmaniensis, Microcystis aeruginosa, Moorea producens, Moorea producens PAL-8-15-08-1
ChemBioChem
18
2115-2118
2017
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3
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8
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12
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12
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7
10
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745390
Peck
Go it alone four-electron oxi ...
Erwinia tasmaniensis
J. Biol. Inorg. Chem.
22
381-394
2017
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1
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1
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1
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1
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2
2
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746445
Castellano
Shedding light on ovothiol bi ...
Paracentrotus lividus
Sci. Rep.
6
21056
2016
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1
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1
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1
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6
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3
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1
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1
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2
4
4
2
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746446
Castellano
Shedding light on ovothiol bi ...
Strongylocentrotus purpuratus
Sci. Rep.
6
21506
2016
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1
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1
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6
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2
1
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734828
Song
Cysteine oxidation reactions c ...
Erwinia tasmaniensis, Erwinia tasmaniensis DSM 17950
Org. Lett.
16
2122-2125
2014
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1
1
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1
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1
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6
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10
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1
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10
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3
3
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743388
Hu
Bioinformatic and biochemical ...
Erwinia tasmaniensis
Org. Lett.
16
5382-5385
2014
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1
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1
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2
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745960
Song
Cysteine oxidation reactions ...
Erwinia tasmaniensis
Org. Lett.
16
2122-2125
2014
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1
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1
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3
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1
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