Information on EC 2.4.2.B12 - NAD+-actin-arginine ADP-ribosyltransferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.4.2.B12
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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SYSTEMATIC NAME
IUBMB Comments
NAD+:[actin]-L-arginine177 ADP-D-ribosyltransferase
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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-
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Manually annotated by BRENDA team
Peptoclostridium difficile
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
actin + NAD+
?
show the reaction diagram
Peptoclostridium difficile
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-
-
-
?
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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?
NAD+ + non-muscle actin from human platelets
nicotinamide + (ADP-D-ribosyl)-non-muscle actin from human platelets
show the reaction diagram
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-
-
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?
NAD+ + rabbit muscle actin
nicotinamide + (ADP-D-ribosyl)-rabbit muscle actin
show the reaction diagram
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-
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?
NAD+ + [actin]-L-arginine177
nicotinamide + [actin]-N-(ADP-D-ribosyl)-L-arginine177 + H+
show the reaction diagram
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?
additional information
?
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.22 - 8.67
NAD+
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000067 - 0.014
NAD+
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
Peptoclostridium difficile
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assay at
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
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
Peptoclostridium difficile
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Manually annotated by BRENDA team
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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structure of the Ia complex with NADH at 1.8 A. Vapor diffusion method
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catalytic subunit CdtA in its native form at pH 4.0, 8.5, and 9.0 and in complex with ADP-ribose donors, NAD+ and NADPH at pH 9.0. The crystal structures of the native protein show pronounced conformational flexibility confined to the active site region of the protein and enhanced disorder at low pH. The suggested catalytically important residues Glu385 and Glu387 seem to play no role or a less important role in ligand binding
Peptoclostridium difficile
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Peptoclostridium difficile
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
Peptoclostridium difficile can be divided into at least five diffent toxin-producing groups: large clostridial cytotoxins producers, large clostridial cytotoxins and binary toxin producers, toxin B-only producers, toxin B and binary toxin producers and binary toxin-only producers. These groupings add further support to the theory Peptoclostridium difficile is divided into stable subpopulations that have evolved from common ancestors
Peptoclostridium difficile
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E301A
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no NADase activity detected
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
F349A
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the ratio of turnover-number to Km-value in the NADase reaction is 1% of the wild-type ratio. The ratio of turnover-number to Km-value in the ADP-ribosyltransferase activity is 1.9% of the wild-type ratio with rabbit muscle actin as substrate and 4% of the wild-type ratio with non-muscle actin from human platelets as substrate
F349Y
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the ratio of turnover-number to Km-value in the NADase reaction is 110% of the wild-type ratio
N255A
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the ratio of turnover-number to Km-value in the NADase reaction is 90% of the wild-type ratio. The ratio of turnover-number to Km-value in the ADP-ribosyltransferase activity is 20% of the wild-type ratio with rabbit muscle actin as substrate and 77% of the wild-type ratio with non-muscle actin from human platelets as substrate
R352A
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no ADP-ribosyltransferase activity with rabbit muscle actin and non-muscle actin from human platelets; the ratio of turnover-number to Km-value in the NADase reaction is 2% of the wild-type ratio, no activity
Y246A
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the ratio of turnover-number to Km-value in the NADase reaction is 90% of the wild-type ratio. The ratio of turnover-number to Km-value in the ADP-ribosyltransferase activity is 1.9% of the wild-type ratio with rabbit muscle actin as substrate and 19% of the wild-type ratio with non-muscle actin from human platelets as substrate
Y251A
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the ratio of turnover-number to Km-value in the NADase reaction is 10% of the wild-type ratio
Y251F
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the ratio of turnover-number to Km-value in the NADase reaction is 40% of the wild-type ratio
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
medicine