BRENDA - Enzyme Database
show all sequences of 1.14.15.35

Identification and characterization of a new erythromycin biosynthetic gene cluster in Actinopolyspora erythraea YIM90600, a novel erythronolide-producing halophilic actinomycete isolated from salt field

Chen, D.; Feng, J.; Huang, L.; Zhang, Q.; Wu, J.; Zhu, X.; Duan, Y.; Xu, Z.; PLoS ONE 9, e108129 (2014)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
gene eryF, genetic structure, sequence comparison, recombinant expression of His6-tagged enzyme in Saccharopolyspora erythraea strain ZL2001
Saccharopolyspora erythraea
gene eryF, whole-genome sequencing, DNA and amino acid sequence determination and analysis, genetic structure,sequence comparison, genomic DNA of Saccharopolyspora erythraea strain ZL2001 serves as template for PCR amplification, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3), recombinant expression in and complementation fo Saccharopolyspora erythraea eryF-deletion mutant strain EX105(ZL2001)
Actinopolyspora erythraea
Engineering
Amino acid exchange
Commentary
Organism
additional information
construction of an erythronolide H-producing Saccharopolyspora erythraea mutant via gene complementation is not successful. Construction of en eryF deletion mutant strainEX105 from strain ZL2001 and complementation by Actinopolyspora erythraea eryF expression
Saccharopolyspora erythraea
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
6-deoxyerythronolide B + reduced ferredoxin [iron-sulfur] cluster + H+ + O2
Saccharopolyspora erythraea
C-6 hydroxylation
erythronolide B + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
?
6-deoxyerythronolide B + reduced ferredoxin [iron-sulfur] cluster + H+ + O2
Actinopolyspora erythraea
C-6 hydroxylation
erythronolide B + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
?
6-deoxyerythronolide B + reduced ferredoxin [iron-sulfur] cluster + H+ + O2
Actinopolyspora erythraea
a two-step oxidation (14-hydroxylation and 6,18-epoxyidation) via the intermediate erythronolide B
erythronolide H + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
?
6-deoxyerythronolide B + reduced ferredoxin [iron-sulfur] cluster + H+ + O2
Saccharopolyspora erythraea NRRL2338
C-6 hydroxylation
erythronolide B + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
?
6-deoxyerythronolide B + reduced ferredoxin [iron-sulfur] cluster + H+ + O2
Actinopolyspora erythraea YIM90600
C-6 hydroxylation
erythronolide B + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
?
6-deoxyerythronolide B + reduced ferredoxin [iron-sulfur] cluster + H+ + O2
Actinopolyspora erythraea YIM90600
a two-step oxidation (14-hydroxylation and 6,18-epoxyidation) via the intermediate erythronolide B
erythronolide H + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
?
additional information
Actinopolyspora erythraea
the enzyme plays a role as a C-12 hydroxylase, rather than a C-14 hydroxylase of the erythronolide in vitro
?
-
-
-
additional information
Actinopolyspora erythraea YIM90600
the enzyme plays a role as a C-12 hydroxylase, rather than a C-14 hydroxylase of the erythronolide in vitro
?
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Actinopolyspora erythraea
A0A099D4T8
halophilic actinomycete isolated from Baicheng salt field
-
Actinopolyspora erythraea YIM90600
A0A099D4T8
halophilic actinomycete isolated from Baicheng salt field
-
Saccharopolyspora erythraea
Q00441
-
-
Saccharopolyspora erythraea NRRL2338
Q00441
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
6-deoxyerythronolide B + reduced ferredoxin [iron-sulfur] cluster + H+ + O2
C-6 hydroxylation
746251
Saccharopolyspora erythraea
erythronolide B + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
6-deoxyerythronolide B + reduced ferredoxin [iron-sulfur] cluster + H+ + O2
C-6 hydroxylation
746251
Actinopolyspora erythraea
erythronolide B + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
6-deoxyerythronolide B + reduced ferredoxin [iron-sulfur] cluster + H+ + O2
C-6 hydroxylation
746251
Saccharopolyspora erythraea NRRL2338
erythronolide B + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
6-deoxyerythronolide B + reduced ferredoxin [iron-sulfur] cluster + H+ + O2
C-6 hydroxylation
746251
Actinopolyspora erythraea YIM90600
erythronolide B + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
6-deoxyerythronolide B + reduced ferredoxin [iron-sulfur] cluster + H+ + O2
a two-step oxidation (14-hydroxylation and 6,18-epoxyidation) via the intermediate erythronolide B
746251
Actinopolyspora erythraea
erythronolide H + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
6-deoxyerythronolide B + reduced ferredoxin [iron-sulfur] cluster + H+ + O2
a two-step oxidation (14-hydroxylation and 6,18-epoxyidation) via the intermediate erythronolide B
746251
Actinopolyspora erythraea YIM90600
erythronolide H + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
additional information
the enzyme plays a role as a C-12 hydroxylase, rather than a C-14 hydroxylase of the erythronolide in vitro
746251
Actinopolyspora erythraea
?
-
-
-
-
additional information
the enzyme plays a role as a C-12 hydroxylase, rather than a C-14 hydroxylase of the erythronolide in vitro
746251
Actinopolyspora erythraea YIM90600
?
-
-
-
-
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
30
-
assay at
Actinopolyspora erythraea
30
-
assay at
Saccharopolyspora erythraea
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Actinopolyspora erythraea
7.5
-
assay at
Saccharopolyspora erythraea
Cofactor
Cofactor
Commentary
Organism
Structure
cytochrome P450
-
Actinopolyspora erythraea
cytochrome P450
-
Saccharopolyspora erythraea
Ferredoxin
-
Actinopolyspora erythraea
Ferredoxin
-
Saccharopolyspora erythraea
ferredoxin [iron-sulfur] cluster
-
Actinopolyspora erythraea
ferredoxin [iron-sulfur] cluster
-
Saccharopolyspora erythraea
Cloned(Commentary) (protein specific)
Commentary
Organism
gene eryF, genetic structure, sequence comparison, recombinant expression of His6-tagged enzyme in Saccharopolyspora erythraea strain ZL2001
Saccharopolyspora erythraea
gene eryF, whole-genome sequencing, DNA and amino acid sequence determination and analysis, genetic structure,sequence comparison, genomic DNA of Saccharopolyspora erythraea strain ZL2001 serves as template for PCR amplification, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3), recombinant expression in and complementation fo Saccharopolyspora erythraea eryF-deletion mutant strain EX105(ZL2001)
Actinopolyspora erythraea
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
cytochrome P450
-
Actinopolyspora erythraea
cytochrome P450
-
Saccharopolyspora erythraea
Ferredoxin
-
Actinopolyspora erythraea
Ferredoxin
-
Saccharopolyspora erythraea
ferredoxin [iron-sulfur] cluster
-
Actinopolyspora erythraea
ferredoxin [iron-sulfur] cluster
-
Saccharopolyspora erythraea
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
additional information
construction of an erythronolide H-producing Saccharopolyspora erythraea mutant via gene complementation is not successful. Construction of en eryF deletion mutant strainEX105 from strain ZL2001 and complementation by Actinopolyspora erythraea eryF expression
Saccharopolyspora erythraea
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
6-deoxyerythronolide B + reduced ferredoxin [iron-sulfur] cluster + H+ + O2
Saccharopolyspora erythraea
C-6 hydroxylation
erythronolide B + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
?
6-deoxyerythronolide B + reduced ferredoxin [iron-sulfur] cluster + H+ + O2
Actinopolyspora erythraea
C-6 hydroxylation
erythronolide B + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
?
6-deoxyerythronolide B + reduced ferredoxin [iron-sulfur] cluster + H+ + O2
Actinopolyspora erythraea
a two-step oxidation (14-hydroxylation and 6,18-epoxyidation) via the intermediate erythronolide B
erythronolide H + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
?
6-deoxyerythronolide B + reduced ferredoxin [iron-sulfur] cluster + H+ + O2
Saccharopolyspora erythraea NRRL2338
C-6 hydroxylation
erythronolide B + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
?
6-deoxyerythronolide B + reduced ferredoxin [iron-sulfur] cluster + H+ + O2
Actinopolyspora erythraea YIM90600
C-6 hydroxylation
erythronolide B + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
?
6-deoxyerythronolide B + reduced ferredoxin [iron-sulfur] cluster + H+ + O2
Actinopolyspora erythraea YIM90600
a two-step oxidation (14-hydroxylation and 6,18-epoxyidation) via the intermediate erythronolide B
erythronolide H + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
?
additional information
Actinopolyspora erythraea
the enzyme plays a role as a C-12 hydroxylase, rather than a C-14 hydroxylase of the erythronolide in vitro
?
-
-
-
additional information
Actinopolyspora erythraea YIM90600
the enzyme plays a role as a C-12 hydroxylase, rather than a C-14 hydroxylase of the erythronolide in vitro
?
-
-
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
6-deoxyerythronolide B + reduced ferredoxin [iron-sulfur] cluster + H+ + O2
C-6 hydroxylation
746251
Saccharopolyspora erythraea
erythronolide B + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
6-deoxyerythronolide B + reduced ferredoxin [iron-sulfur] cluster + H+ + O2
C-6 hydroxylation
746251
Actinopolyspora erythraea
erythronolide B + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
6-deoxyerythronolide B + reduced ferredoxin [iron-sulfur] cluster + H+ + O2
C-6 hydroxylation
746251
Saccharopolyspora erythraea NRRL2338
erythronolide B + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
6-deoxyerythronolide B + reduced ferredoxin [iron-sulfur] cluster + H+ + O2
C-6 hydroxylation
746251
Actinopolyspora erythraea YIM90600
erythronolide B + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
6-deoxyerythronolide B + reduced ferredoxin [iron-sulfur] cluster + H+ + O2
a two-step oxidation (14-hydroxylation and 6,18-epoxyidation) via the intermediate erythronolide B
746251
Actinopolyspora erythraea
erythronolide H + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
6-deoxyerythronolide B + reduced ferredoxin [iron-sulfur] cluster + H+ + O2
a two-step oxidation (14-hydroxylation and 6,18-epoxyidation) via the intermediate erythronolide B
746251
Actinopolyspora erythraea YIM90600
erythronolide H + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
additional information
the enzyme plays a role as a C-12 hydroxylase, rather than a C-14 hydroxylase of the erythronolide in vitro
746251
Actinopolyspora erythraea
?
-
-
-
-
additional information
the enzyme plays a role as a C-12 hydroxylase, rather than a C-14 hydroxylase of the erythronolide in vitro
746251
Actinopolyspora erythraea YIM90600
?
-
-
-
-
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
30
-
assay at
Actinopolyspora erythraea
30
-
assay at
Saccharopolyspora erythraea
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Actinopolyspora erythraea
7.5
-
assay at
Saccharopolyspora erythraea
General Information
General Information
Commentary
Organism
evolution
the Er gene cluster from Actinopolyspora erythraea strain YIM90600 shares high identity and similarity with the one of Saccharopolyspora erythraea strain NRRL2338, except for two absent genes, eryBI and eryG. By correlating genotype and chemotype, the biosynthetic pathways of 3'-demethyl-erythromycin C, erythronolide H (EH) and erythronolide I are proposed. Formation of erythronolide H is supposed to be sequentially biosynthesized via C-6/C-18 epoxidation and C-14 hydroxylation from 6-deoxyerythronolide B
Actinopolyspora erythraea
evolution
the Er gene cluster from Actinopolyspora erythraea strain YIM90600 shares high identity and similarity with the one of Saccharopolyspora erythraea strain NRRL2338, except for two absent genes, eryBI and eryG, correlation of genotype and chemotype
Saccharopolyspora erythraea
metabolism
the ezyme is involved in the biosynthetic pathway of the final erythronolide product, erythronolid A, pathway overview
Actinopolyspora erythraea
metabolism
the ezyme is involved in the biosynthetic pathway of the final erythronolide product, erythronolid A, pathway overview
Saccharopolyspora erythraea
General Information (protein specific)
General Information
Commentary
Organism
evolution
the Er gene cluster from Actinopolyspora erythraea strain YIM90600 shares high identity and similarity with the one of Saccharopolyspora erythraea strain NRRL2338, except for two absent genes, eryBI and eryG. By correlating genotype and chemotype, the biosynthetic pathways of 3'-demethyl-erythromycin C, erythronolide H (EH) and erythronolide I are proposed. Formation of erythronolide H is supposed to be sequentially biosynthesized via C-6/C-18 epoxidation and C-14 hydroxylation from 6-deoxyerythronolide B
Actinopolyspora erythraea
evolution
the Er gene cluster from Actinopolyspora erythraea strain YIM90600 shares high identity and similarity with the one of Saccharopolyspora erythraea strain NRRL2338, except for two absent genes, eryBI and eryG, correlation of genotype and chemotype
Saccharopolyspora erythraea
metabolism
the ezyme is involved in the biosynthetic pathway of the final erythronolide product, erythronolid A, pathway overview
Actinopolyspora erythraea
metabolism
the ezyme is involved in the biosynthetic pathway of the final erythronolide product, erythronolid A, pathway overview
Saccharopolyspora erythraea
Other publictions for EC 1.14.15.35
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)
728197
Sen
Role of two alternate water ne ...
Saccharopolyspora erythraea, Saccharopolyspora erythraea NRRL 2338
J. Phys. Chem. B
118
2810-2820
2014
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746251
Chen
Identification and characteri ...
Actinopolyspora erythraea, Actinopolyspora erythraea YIM90600, Saccharopolyspora erythraea, Saccharopolyspora erythraea NRRL2338
PLoS ONE
9
e108129
2014
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8
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4
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726944
Roberts
NMR studies of ligand binding ...
Saccharopolyspora erythraea, Saccharopolyspora erythraea NRRL 2338
Biochemistry
45
1673-1684
2006
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7
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725366
Nagano
Crystal structures of the ferr ...
Saccharopolyspora erythraea, Saccharopolyspora erythraea NRRL 2338
J. Biol. Chem.
280
22102-22107
2005
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727300
Khan
7-Benzyloxyquinoline oxidation ...
Saccharopolyspora erythraea, Saccharopolyspora erythraea NRRL 2338
Chem. Res. Toxicol.
15
806-814
2002
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728082
Harris
Oxidation and electronic state ...
Saccharopolyspora erythraea, Saccharopolyspora erythraea NRRL 2338
J. Inorg. Biochem.
91
568-585
2002
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728805
Cupp-Vickery
Structure of cytochrome P450er ...
Saccharopolyspora erythraea
Steroids
62
112-116
1997
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728360
Cupp-Vickery
Structure of cytochrome P450er ...
Saccharopolyspora erythraea, Saccharopolyspora erythraea NRRL 2338
Nat. Struct. Biol.
2
144-153
1995
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726926
Andersen
Substrate specificity of 6-deo ...
Saccharopolyspora erythraea
Biochemistry
32
1905-1913
1993
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6
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728800
Weber
An erythromycin derivative pro ...
Saccharopolyspora erythraea
Science
252
114-117
1991
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726925
Shafiee
Macrolide antibiotic biosynthe ...
Saccharopolyspora erythraea
Biochemistry
26
6204-6210
1987
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