BRENDA - Enzyme Database
show all sequences of 1.3.3.16

Architecture of microcin B17 synthetase an octameric protein complex converting a ribosomally synthesized peptide into a DNA gyrase poison

Ghilarov, D.; Stevenson, C.EM.; Travin, D.Y.; Piskunova, J.; Serebryakova, M.; Maxwell, A.; Lawson, D.M.; Severinov, K.; Mol. Cell 73, 749-762 (2019)

Data extracted from this reference:

Crystallization (Commentary)
Crystallization (Commentary)
Organism
structures of synthetase McbBCD reveal an octameric B4C2D2 complex with two bound substrate peptides. Each McbB dimer clamps the N-terminal recognition sequence, while the C-terminal heterocycle of the modified peptide is trapped in the active site of McbC. The McbD and McbC active sites are distant from each other, which necessitates alternate shuttling of the peptide substrate between them, while remaining tethered to the McbB dimer
Escherichia coli
Organism
Organism
UniProt
Commentary
Textmining
Escherichia coli
P23185
dehydrogenase subunit McbC
-
Purification (Commentary)
Purification (Commentary)
Organism
copurification of the modified McbA peptide together with all three components of the microcin B17 synthetase as a stable complex
Escherichia coli
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
a [protein]-(1S,4R)-2-(C-substituted-aminomethyl)-4-acyl-2-thiazoline + O2
-
757653
Escherichia coli
a [protein]-(S)-2-(C-substituted-aminomethyl)-4-acyl-1,3-thiazole + H2O2
-
-
-
?
a [protein]-(S,S)-2-(C-substituted-aminomethyl)-4-acyl-2-oxazoline + O2
-
757653
Escherichia coli
a [protein]-(S)-2-(C-substituted-aminomethyl)-4-acyl-1,3-oxazole + H2O2
-
-
-
?
a [protein]-(S,S)-2-(C-substituted-aminomethyl)-4-acyl-5-methyl-2-oxazoline + O2
-
757653
Escherichia coli
a [protein]-(S)-2-(C-substituted-aminomethyl)-4-acyl-5-methyl-1,3-oxazole + H2O2
-
-
-
?
additional information
proposed general mechanism for McbC: an activated Tyr202 abstracts a proton from the A carbon of an azoline substrate, which results in E2 elimination of the antiproton from the B carbon and hydride transfer to FMN. Instead of a proton being provided to FMN by a general base to yield FMNH2, the negative charge on N1 of FMN may be stabilized by a salt bridge with Arg233
757653
Escherichia coli
?
-
-
-
-
Synonyms
Synonyms
Commentary
Organism
MbcC
-
Escherichia coli
microcin B17-processing protein McbC
-
Escherichia coli
Cofactor
Cofactor
Commentary
Organism
Structure
FMN
each McbC subunit contributes to the binding of the FMN cofactor molecules, with Arg82 of one McbC subunit and Arg117 of the other forming salt bridges with the phosphate group and Arg181 interacting with the O2 of FMN
Escherichia coli
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
FMN
each McbC subunit contributes to the binding of the FMN cofactor molecules, with Arg82 of one McbC subunit and Arg117 of the other forming salt bridges with the phosphate group and Arg181 interacting with the O2 of FMN
Escherichia coli
Crystallization (Commentary) (protein specific)
Crystallization
Organism
structures of synthetase McbBCD reveal an octameric B4C2D2 complex with two bound substrate peptides. Each McbB dimer clamps the N-terminal recognition sequence, while the C-terminal heterocycle of the modified peptide is trapped in the active site of McbC. The McbD and McbC active sites are distant from each other, which necessitates alternate shuttling of the peptide substrate between them, while remaining tethered to the McbB dimer
Escherichia coli
Purification (Commentary) (protein specific)
Commentary
Organism
copurification of the modified McbA peptide together with all three components of the microcin B17 synthetase as a stable complex
Escherichia coli
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
a [protein]-(1S,4R)-2-(C-substituted-aminomethyl)-4-acyl-2-thiazoline + O2
-
757653
Escherichia coli
a [protein]-(S)-2-(C-substituted-aminomethyl)-4-acyl-1,3-thiazole + H2O2
-
-
-
?
a [protein]-(S,S)-2-(C-substituted-aminomethyl)-4-acyl-2-oxazoline + O2
-
757653
Escherichia coli
a [protein]-(S)-2-(C-substituted-aminomethyl)-4-acyl-1,3-oxazole + H2O2
-
-
-
?
a [protein]-(S,S)-2-(C-substituted-aminomethyl)-4-acyl-5-methyl-2-oxazoline + O2
-
757653
Escherichia coli
a [protein]-(S)-2-(C-substituted-aminomethyl)-4-acyl-5-methyl-1,3-oxazole + H2O2
-
-
-
?
additional information
proposed general mechanism for McbC: an activated Tyr202 abstracts a proton from the A carbon of an azoline substrate, which results in E2 elimination of the antiproton from the B carbon and hydride transfer to FMN. Instead of a proton being provided to FMN by a general base to yield FMNH2, the negative charge on N1 of FMN may be stabilized by a salt bridge with Arg233
757653
Escherichia coli
?
-
-
-
-
General Information
General Information
Commentary
Organism
physiological function
during biosynthesis of microcin B17, azole introduction into the microcin B17 precursor requires coordination of the activities of the heterocyclase, which converts Ser and Cys residues into azolines, and the dehydrogenase, which oxidizes the azolines to azoles
Escherichia coli
General Information (protein specific)
General Information
Commentary
Organism
physiological function
during biosynthesis of microcin B17, azole introduction into the microcin B17 precursor requires coordination of the activities of the heterocyclase, which converts Ser and Cys residues into azolines, and the dehydrogenase, which oxidizes the azolines to azoles
Escherichia coli
Other publictions for EC 1.3.3.16
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
Synonyms
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)
757653
Ghilarov
Architecture of microcin B17 ...
Escherichia coli
Mol. Cell
73
749-762
2019
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755718
Bent
Structure of the cyanobactin ...
Cyanothece sp. PCC 7425
Acta Crystallogr. Sect. D
72
1174-1180
2016
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758209
Schmidt
Patellamide A and C biosynthe ...
Prochloron didemni
Proc. Natl. Acad. Sci. USA
102
7315-7320
2005
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758460
Li
From peptide precursors to ox ...
Escherichia coli
Science
274
1188-1193
1996
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