Information on EC 2.5.1.38 - isonocardicin synthase

for references in articles please use BRENDA:EC2.5.1.38
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The expected taxonomic range for this enzyme is: Nocardia uniformis

EC NUMBER
COMMENTARY hide
2.5.1.38
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RECOMMENDED NAME
GeneOntology No.
isonocardicin synthase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + nocardicin G = S-methyl-5'-thioadenosine + isonocardicin C
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3-amino-3-carboxypropyl group transfer
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
nocardicin A biosynthesis
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Monobactam biosynthesis
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Biosynthesis of antibiotics
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:nocardicin-G 3-amino-3-carboxypropyltransferase
The enzyme, characterized from the bacterium Nocardia uniformis, is involved in the biosynthesis of the beta-lactam antibiotic nocardicin A. The enzyme can act on nocardicin E, F, and G, producing isonocardicin A, B, and C, respectively. However, the in vivo substrate is believed to be nocardicin G [3].
CAS REGISTRY NUMBER
COMMENTARY hide
118246-74-5
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
ssp. tsuyamanensis, ATCC 21806
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + nocardicin E
5'-methylthioadenosine + isonocardicin A
show the reaction diagram
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?
S-adenosyl-L-methionine + nocardicin E
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show the reaction diagram
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enzyme is involved in the biosynthesis of the beta-lactam antibiotic nocardicin A
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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
S-adenosyl-L-methionine + nocardicin E
?
show the reaction diagram
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enzyme is involved in the biosynthesis of the beta-lactam antibiotic nocardicin A
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
partially purified enzyme is stable after dialysis against 50 mM phosphate buffer, pH 7.5, containing 20% glycerol and 10 mM 2-mercaptoethanol
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ssp. tsuyamanensis, ATCC 21806, partial
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