Information on EC 2.4.2.B13 - NAD+-actin-arginine ADP-ribosyltransferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.4.2.B13
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
NAD+-actin-arginine ADP-ribosyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
NAD+ + [actin]-L-arginine177 = nicotinamide + [actin]-N-(ADP-D-ribosyl)-L-arginine177 + H+
show the reaction diagram
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
Peptoclostridium difficile
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UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
NAD+ + actin
nicotinamide + H+ + (ADP-ribosyl)-actin
show the reaction diagram
NAD+ + beta-actin
nicotinamide + H+ + (ADP-ribosyl)-beta-actin
show the reaction diagram
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modification occurs at residue Arg177
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?
NAD+ + gamma-actin
nicotinamide + H+ + (ADP-ribosyl)-gamma-actin
show the reaction diagram
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modification occurs at residue Arg177
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?
NAD+ + muscle actin
nicotinamide + H+ + (ADP-ribosyl)-muscle actin
show the reaction diagram
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substrate source rabbit skeletal muscle
modification occurs at residue Arg177
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?
additional information
?
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no substrates: alpha-skeletal muscle actin, alpha-smooth muscle actin or alpha-cardiac muscle actin. The N-terminal region of actin isoforms define the substrate specificity for ADP-ribosylation by Clostridium botulinum C2 toxin
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.8
Peptoclostridium difficile
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
high-resolution structures of NAD(+)-iota toxin-actin and iota toxin-ADPR-actin obtained by soaking apo-iota toxin-actin crystal with NAD(+) under different conditions and structures of mutants E378S, E380A, E380S in complex with actin. The structures of NAD(+)-iota toxin-actin and iota toxin-ADPR-actin represent the pre- and postreaction states. A simple strain-alleviation model explains arginine ADP ribosylation occuring via two oxocarbenium ion intermediates
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Peptoclostridium difficile
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E378S
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mutation eliminates ADP-ribosylation activity and reduces the weak NAD+ glycohydrolase activity in absence of actin to 50%
E380A
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mutation eliminates both ADP-ribosylation activity and the weak NAD+ glycohydrolase activity in absence of actin
E380S
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mutation eliminates both ADP-ribosylation activity and the weak NAD+ glycohydrolase activity in absence of actin
additional information
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engineering strategy for the creation of a plant-tolerated, zymogen-like form of an otherwise toxic protein. Engineering of a random propeptide library at the C-terminal end of ADP-ribosyltranferase Vip2 and selecting for malfunctional enzyme variants in yeast leads to a proenzyme proVip2 which possesses reduced enzymatic activity as compared with the wild-type Vip2 protein, but remains a potent toxin toward rootworm larvae. The zymogenized Vip2 can be proteolytically activated by rootworm digestive enzyme machinery
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agriculture
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engineering strategy for the creation of a plant-tolerated, zymogen-like form of an otherwise toxic protein. Engineering of a random propeptide library at the C-terminal end of ADP-ribosyltranferase Vip2 and selecting for malfunctional enzyme variants in yeast leads to a proenzyme proVip2 which possesses reduced enzymatic activity as compared with the wild-type Vip2 protein, but remains a potent toxin toward rootworm larvae. The zymogenized Vip2 can be proteolytically activated by rootworm digestive enzyme machinery