Information on EC 5.5.1.26 - nogalonic acid methyl ester cyclase

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The expected taxonomic range for this enzyme is: Streptomyces nogalater

EC NUMBER
COMMENTARY hide
5.5.1.26
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RECOMMENDED NAME
GeneOntology No.
nogalonic acid methyl ester cyclase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
nogalaviketone = methyl nogalonate
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of antibiotics
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Biosynthesis of type II polyketide products
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SYSTEMATIC NAME
IUBMB Comments
methyl nogalonate lyase (cyclizing)
The enzyme, characterized from the bacterium Streptomyces nogalater, is involved in the biosynthesis of the aromatic polyketide nogalamycin.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
methyl nogalonate
nogalaviketone
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
methyl nogalonate
nogalaviketone
show the reaction diagram
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-
-
-
?
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20471
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4 * 20471, calculated from sequence
20472
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4 * 20472, mass spectrometry
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
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4 * 20471, calculated from sequence; 4 * 20472, mass spectrometry
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structure of the enzyme with a bound product, determined to 1.35 A resolution
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hanging-drop vapour-diffusion method. Crystals of a complex of the enzyme with the substrate nogalonic acid methyl ester, obtained using PEG 4000 as precipitant. The crystals are orthorhombic, space group I222, with unit-cell parameters a = 69.1, b = 72.0, c = 65.4 A. They diffract to 1.35 A resolution using synchrotron radiation
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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produced in Escherichia coli with an N-terminal 6*His tag
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D121A
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inactive mutant enzyme
D121N
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mutant enzyme forms insoluble inclusion bodies
F15Y
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mutant enzyme shows 5% of the activity compared to the wild-type enzyme
Q105A
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mutant enzyme shows 16% of the activity compared to the wild-type enzyme
Q105E
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mutant enzyme forms insoluble inclusion bodies