Information on EC 4.2.1.145 - capreomycidine synthase

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The expected taxonomic range for this enzyme is: Streptomyces

EC NUMBER
COMMENTARY hide
4.2.1.145
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RECOMMENDED NAME
GeneOntology No.
capreomycidine synthase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(2S,3S)-3-hydroxyarginine = (2S,3R)-capreomycidine + H2O
show the reaction diagram
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
beta-replacement
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intramolecular
SYSTEMATIC NAME
IUBMB Comments
(2S,3S)-3-hydroxyarginine hydrolyase (cyclizing, (2S,3R)-capreomycidine-forming)
A pyridoxal 5'-phosphate protein. The enzyme is involved in the biosynthesis of the cyclic pentapeptide antibiotic viomycin.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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the enzyme is involved in the biosynthesis of the cyclic pentapeptide antibiotic viomycin
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(2S,3S)-3-hydroxyarginine
(2S,3R)-capreomycidine
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
(2S,3S)-3-hydroxyarginine
(2S,3R)-capreomycidine
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloned into the Escherichia coli expression vector pET28a encoding a N-terminal His6-tag
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overproduced in Escherichia coli with an N-terminal hexahistidine affinity tag
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