Information on EC 5.5.1.B6 - nogalonic acid methyl ester cyclase

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The expected taxonomic range for this enzyme is: Streptomyces galilaeus

EC NUMBER
COMMENTARY hide
5.5.1.B6
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
nogalonic acid methyl ester cyclase
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SYSTEMATIC NAME
IUBMB Comments
methyl nogalonate lyase (cyclizing, auraviketone forming)
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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
aklanonic acid methyl ester
?
show the reaction diagram
-
-
-
?
nogalonic acid methyl ester
auraviketone
show the reaction diagram
-
product has (R)-configuration at C9, ring closure is an intramolecular aldol condensation. The attack of the enol(ate) is on the si face of the C9 carbonyl group, required for the formation of the C9-R stereoisomer, which results in the alcoholate anion pointing away from the carboxyl side-chain of Asp121
-
?
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
aklanonic acid methyl ester
?
show the reaction diagram
O52646
-
-
-
?
nogalonic acid methyl ester
auraviketone
show the reaction diagram
O52646
-
product has (R)-configuration at C9, ring closure is an intramolecular aldol condensation. The attack of the enol(ate) is on the si face of the C9 carbonyl group, required for the formation of the C9-R stereoisomer, which results in the alcoholate anion pointing away from the carboxyl side-chain of Asp121
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.002
nogalonic acid methyl ester
pH 7.4, temperature not specified in the publication
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1
nogalonic acid methyl ester
Streptomyces galilaeus
O52646
pH 7.4, temperature not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
AknH forms a tetramer of 222 symmetry. Two subunits (A-B and C-D, respectively), related by one of the 2-fold symmetry axes, form tight dimer interfaces. The side-chains of Thr128, Gln105 and the main-chain nitrogen of Val92 each interact with oxygen atoms of the polyketide core of the product via a water molecule. Additional enzyme-ligand interactions involve residues Arg120 and Trp122 from the other monomer across the subunit-subunit interface
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D121A
0.2% of wild-type activity, (R)-configuration at C9 of product
H107A
2% of wild-type activity, (R)-configuration at C9 of product
N51L
exchange to corresponding residues of SnoaL, EC 5.5.1.26, producing product with (S)-configuration. 20% of wild-type activity, about 50% (S)-configuration at C9 of product
Q105A
6% of wild-type activity, (R)-configuration at C9 of product
Y15F
exchange to corresponding residues of SnoaL, EC 5.5.1.26, producing product with (S)-configuration. 45% of wild-type activity, about 20% (S)-configuration at C9 of product