Information on EC 3.4.19.15 - desampylase

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The expected taxonomic range for this enzyme is: Haloferax volcanii

EC NUMBER
COMMENTARY hide
3.4.19.15
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RECOMMENDED NAME
GeneOntology No.
desampylase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
an N6-[small archaeal modifier protein]-[protein]-L-lysine + H2O = a [protein]-L-lysine + a small archaeal modifier protein
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
N6-[small archaeal modifier protein]-[protein]-L-lysine hydrolase
The enzyme, characterized from the archaeon Haloferax volcanii, specifically cleaves the ubiquitin-like small modifier proteins SAMP1 and SAMP2 from protein conjugates, hydrolysing the isopeptide bond between a lysine residue of the target protein and the C-terminal glycine of the modifier protein. The enzyme contains Zn2+. cf. EC 3.4.19.12, ubiquitinyl hydrolase 1. In peptidase family M67.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
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
N6-SAMP1-[molybdopterin synthase MoaE]-L-lysine + H2O
SAMP1 + [molybdopterin synthase MoaE]-L-lysine
show the reaction diagram
N6-SAMP1-[protein]-L-lysine + H2O
SAMP1 + [protein]-L-lysine
show the reaction diagram
N6-SAMP2-[protein]-L-lysine + H2O
SAMP2 + [protein]-L-lysine
show the reaction diagram
N6-[SAMP1]-[MoaE]-L-lysine + H2O
[MoaE]-L-lysine + SAMP1
show the reaction diagram
N6-[SAMP3]-[MoaE]-L-lysine + H2O
[MoaE]-L-lysine + SAMP3
show the reaction diagram
additional information
?
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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
N6-SAMP1-[molybdopterin synthase MoaE]-L-lysine + H2O
SAMP1 + [molybdopterin synthase MoaE]-L-lysine
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
NaCl
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optimal activity at NaCl concentrations of 0.7–2 M. Little to no activity at low concentrations of salt (150 mM NaCl)
Zn2+
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addition of excess Zn2+ restores the activity of the enzyme activated by N,N,N',N'-tetrakis(2-pyridylmethyl)ethylenediamine, while addition of Fe2+, Cu2+ and Ni2+ do not reactivate the enzyme. Metal content analysis reveals that wild-type enzyme coordinates a Zn2+ atom, while HvJAMM1 H90Q, H88N and S98A variants are significantly reduced in Zn2+ content. Among the variants, H90Q and H88N have the most pronounced effect, reducing the mol/mol of protein content from nearly 1 in wild type to less than 0.05 in the variant proteins. The D101E mutation does not significantly alter the Zn2+ content of the enzyme
additional information
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relatively insensitive to PMSF
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
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inhibits at a molar ratio of inhibitor to enzyme of 50:1
N,N,N',N'-tetrakis(2-pyridylmethyl)ethylenediamine
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inhibits at a molar ratio of inhibitor to enzyme of 5:1. Addition of excess Zn2+ restores its activity, while addition of Fe2+, Cu2+ and Ni2+ does not reactivate the enzyme
N-ethylmaleimide
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inhibits at a molar ratio of inhibitor to enzyme of 20:1
additional information
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relatively insensitive to PMSF
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 10
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no activity at pH 6.5 and below
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 60
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not active at 70°C
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
16771
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1 * 16771, calculated from sequence, MALTI-TOF, the negative surface charge of the enzyme may account for the 1000 Da discrepancy between the molecular mass of the enzyme estimated by SDS-PAGE compared to its theoretical molecular mass
22400
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gel filtration
26000
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1 * 26000, SDS-PAGE, the negative surface charge of the enzyme may account for the 1000 Da discrepancy between the molecular mass of the enzyme estimated by SDS-PAGE compared to its theoretical molecular mass
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D101E
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mutation does not significantly alter the Zn2+ content of the enzyme, inactive in cleavage of SAMP2 conjugates
D31S
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inactive mutant enzyme
H88N
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the mol Zn2+/mol of protein content from nearly 1 in wild type is reduced to less than 0.05 in the variant protein
H90Q
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the mol Zn2+/mol of protein content from nearly 1 in wild type is reduced to less than 0.05 in the variant protein
S98A
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mutant enzyme is significantly reduced in Zn2+ content
D101E
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mutation does not significantly alter the Zn2+ content of the enzyme, inactive in cleavage of SAMP2 conjugates
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D31S
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inactive mutant enzyme
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H88N
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the mol Zn2+/mol of protein content from nearly 1 in wild type is reduced to less than 0.05 in the variant protein
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H90Q
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the mol Zn2+/mol of protein content from nearly 1 in wild type is reduced to less than 0.05 in the variant protein
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S98A
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mutant enzyme is significantly reduced in Zn2+ content
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