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Literature summary for 3.4.19.15 extracted from

  • Hepowit, N.L.; Uthandi, S.; Miranda, H.V.; Toniutti, M.; Prunetti, L.; Olivarez, O.; De Vera, I.M.; Fanucci, G.E.; Chen, S.; Maupin-Furlow, J.A.
    Archaeal JAB1/MPN/MOV34 metalloenzyme (HvJAMM1) cleaves ubiquitin-like small archaeal modifier proteins (SAMPs) from protein-conjugates (2012), Mol. Microbiol., 86, 971-987.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.19.15

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Haloferax volcanii

Protein Variants

Protein Variants Comment Organism
D101E mutation does not significantly alter the Zn2+ content of the enzyme, inactive in cleavage of SAMP2 conjugates Haloferax volcanii
D31S inactive mutant enzyme Haloferax volcanii
H88N the mol Zn2+/mol of protein content from nearly 1 in wild type is reduced to less than 0.05 in the variant protein Haloferax volcanii
H90Q the mol Zn2+/mol of protein content from nearly 1 in wild type is reduced to less than 0.05 in the variant protein Haloferax volcanii
S98A mutant enzyme is significantly reduced in Zn2+ content Haloferax volcanii

Inhibitors

Inhibitors Comment Organism Structure
1,10-phenanthroline inhibits at a molar ratio of inhibitor to enzyme of 50:1 Haloferax volcanii
EDTA
-
 Haloferax volcanii
additional information relatively insensitive to PMSF Haloferax volcanii
N,N,N',N'-tetrakis(2-pyridylmethyl)ethylenediamine 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 Haloferax volcanii
N-ethylmaleimide inhibits at a molar ratio of inhibitor to enzyme of 20:1 Haloferax volcanii

Metals/Ions

Metals/Ions Comment Organism Structure
additional information relatively insensitive to PMSF Haloferax volcanii
NaCl optimal activity at NaCl concentrations of 0.7–2 M. Little to no activity at low concentrations of salt (150 mM NaCl) Haloferax volcanii
Zn2+ 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 Haloferax volcanii

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
16771
-
 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 Haloferax volcanii
22400
-
 gel filtration Haloferax volcanii
26000
-
 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 Haloferax volcanii

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
N6-SAMP1-[molybdopterin synthase MoaE]-L-lysine + H2O Haloferax volcanii
-
 SAMP1 + [molybdopterin synthase MoaE]-L-lysine
-
 ?
N6-SAMP1-[molybdopterin synthase MoaE]-L-lysine + H2O Haloferax volcanii DSM 3757
-
 SAMP1 + [molybdopterin synthase MoaE]-L-lysine
-
 ?

Organism

Organism UniProt Comment Textmining
Haloferax volcanii D4GTS4
-
-
Haloferax volcanii DSM 3757 D4GTS4
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Haloferax volcanii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme can cleave proteins attached to SAMP1 by linear and isopeptide bonds. The enzyme is inactive in hydrolyzing the amide bond that links aminomethylcoumarin to the C-terminus of monomeric ubiquinone or diglycine Haloferax volcanii ?
-
 ?
additional information the enzyme can cleave proteins attached to SAMP1 by linear and isopeptide bonds. The enzyme is inactive in hydrolyzing the amide bond that links aminomethylcoumarin to the C-terminus of monomeric ubiquinone or diglycine Haloferax volcanii DSM 3757 ?
-
 ?
N6-SAMP1-[molybdopterin synthase MoaE]-L-lysine + H2O
-
 Haloferax volcanii SAMP1 + [molybdopterin synthase MoaE]-L-lysine
-
 ?
N6-SAMP1-[molybdopterin synthase MoaE]-L-lysine + H2O the enzyme cleaves isopeptide-liked SAMP1 from molybdopterin synthase MoaE. It also cleaves linear fusions of SAMP to molybdopterin synthase MoaE Haloferax volcanii SAMP1 + [molybdopterin synthase MoaE]-L-lysine
-
 ?
N6-SAMP1-[molybdopterin synthase MoaE]-L-lysine + H2O
-
 Haloferax volcanii DSM 3757 SAMP1 + [molybdopterin synthase MoaE]-L-lysine
-
 ?
N6-SAMP1-[molybdopterin synthase MoaE]-L-lysine + H2O the enzyme cleaves isopeptide-liked SAMP1 from molybdopterin synthase MoaE. It also cleaves linear fusions of SAMP to molybdopterin synthase MoaE Haloferax volcanii DSM 3757 SAMP1 + [molybdopterin synthase MoaE]-L-lysine
-
 ?
N6-SAMP1-[protein]-L-lysine + H2O broad spectrum of activity in removing SAMP1/2 from diverse proteins. HvJAMM1 is unable to hydrolyze bovine serum albumin, hemoglobin, creatine phosphokinase, carbonic anhydrase, beta-amylase or cytochrome c. Long-term incubation with the enzyme has little if any impact on the level or length of these proteins Haloferax volcanii SAMP1 + [protein]-L-lysine
-
 ?
N6-SAMP1-[protein]-L-lysine + H2O broad spectrum of activity in removing SAMP1/2 from diverse proteins. HvJAMM1 is unable to hydrolyze bovine serum albumin, hemoglobin, creatine phosphokinase, carbonic anhydrase, beta-amylase or cytochrome c. Long-term incubation with the enzyme has little if any impact on the level or length of these proteins Haloferax volcanii DSM 3757 SAMP1 + [protein]-L-lysine
-
 ?
N6-SAMP2-[protein]-L-lysine + H2O broad spectrum of activity in removing SAMP1/2 from diverse proteins. HvJAMM1 is unable to hydrolyze bovine serum albumin, hemoglobin, creatine phosphokinase, carbonic anhydrase, beta-amylase or cytochrome c. Long-term incubation with the enzyme has little if any impact on the level or length of these proteins Haloferax volcanii SAMP2 + [protein]-L-lysine
-
 ?
N6-SAMP2-[protein]-L-lysine + H2O broad spectrum of activity in removing SAMP1/2 from diverse proteins. HvJAMM1 is unable to hydrolyze bovine serum albumin, hemoglobin, creatine phosphokinase, carbonic anhydrase, beta-amylase or cytochrome c. Long-term incubation with the enzyme has little if any impact on the level or length of these proteins Haloferax volcanii DSM 3757 SAMP2 + [protein]-L-lysine
-
 ?

Subunits

Subunits Comment Organism
monomer 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 Haloferax volcanii
monomer 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 Haloferax volcanii

Synonyms

Synonyms Comment Organism
HvJAMM1
-
 Haloferax volcanii
HVO_2505 locus name Haloferax volcanii

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
45 50
-
 Haloferax volcanii

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
20 60 not active at 70°C Haloferax volcanii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7 10 no activity at pH 6.5 and below Haloferax volcanii

General Information

General Information Comment Organism
metabolism the enzyme mediates a decrease in the level of SAMP1/2 modified proteins in the cell, and this activity appears to be stimulated by heat shock Haloferax volcanii
physiological function the enzyme may reactivate molybdopterin synthase by cleaving SAMP1 from the catalytic lysine residues of MoaE Haloferax volcanii