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Literature summary for 2.7.4.3 extracted from

  • Gavel, O.Y.; Bursakov, S.A.; Di Rocco, G.; Trincao, J.; Pickering, I.J.; George, G.N.; Calvete, J.J.; Shnyrov, V.L.; Brondino, C.D.; Pereira, A.S.; Lampreia, J.; Tavares, P.; Moura, J.J.; Moura, I.
    A new type of metal-binding site in cobalt- and zinc-containing adenylate kinases isolated from sulfate-reducers Desulfovibrio gigas and Desulfovibrio desulfuricans ATCC 27774 (2008), J. Inorg. Biochem., 102, 1380-1395.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
KCl no inhibitory up to 150 mM, 65% residual activity at 700 mM Desulfovibrio desulfuricans
KCl not inhibitory up to 150 mM, 65% residual activity at 700 mM Megalodesulfovibrio gigas

Metals/Ions

Metals/Ions Comment Organism Structure
Cobalt 0.3 mol of cobalt and 0.1 mol of zinc per mol of protein Desulfovibrio desulfuricans
Cobalt 0.4 mol of cobalt and 0.3 mol of zinc per mol of protein. Presence of three sulfydryl groups of cysteines potentially bound to Co2+ or Zn2+. Bound Zn2+ or Co2+ is clearly present in the LID domain and tetrahedrally coordinated to 129Cys, 135His, 151Cys, and 154Cys. Site 129Cys-X5-His-X15-Cys-X2-Cys is responsible for chelating zinc or cobalt Megalodesulfovibrio gigas
Zinc 0.3 mol of cobalt and 0.1 mol of zinc per mol of protein Desulfovibrio desulfuricans
Zinc 0.4 mol of cobalt and 0.3 mol of zinc per mol of protein. Presence of three sulfydryl groups of cysteines potentially bound to Co2+ or Zn2+. Bound Zn2+ or Co2+ is clearly present in the LID domain and tetrahedrally coordinated to 129Cys, 135His, 151Cys, and 154Cys. Site 129Cys-X5-His-X15-Cys-X2-Cys is responsible for chelating zinc or cobalt Megalodesulfovibrio gigas

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
24500
-
1 * 24500, SDS-PAGE, 1 * 24700, electrospray mass spectrometry, 1 * 24500, calculated Megalodesulfovibrio gigas
24700
-
1 * 24500, SDS-PAGE, 1 * 24700, electrospray mass spectrometry, 1 * 24500, calculated Megalodesulfovibrio gigas
24800
-
1 * 25500, SDS-PAGE, 1 * 24800, electrospray mass spectrometry Desulfovibrio desulfuricans
25500
-
1 * 25500, SDS-PAGE, 1 * 24800, electrospray mass spectrometry Desulfovibrio desulfuricans
26000
-
gel filtration Desulfovibrio desulfuricans
26000
-
gel filtration Megalodesulfovibrio gigas

Organism

Organism UniProt Comment Textmining
Desulfovibrio desulfuricans
-
-
-
Megalodesulfovibrio gigas
-
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1560
-
apoenzyme, pH 7.4, 30°C Megalodesulfovibrio gigas
1640
-
ATP formation, pH 7.4, 30°C Desulfovibrio desulfuricans
1980
-
fully zinc-substitued form, pH 7.4, 30°C Megalodesulfovibrio gigas
2020
-
native form, pH 7.4, 30°C Megalodesulfovibrio gigas
2170
-
fully cobalt-substitued form, pH 7.4, 30°C Megalodesulfovibrio gigas

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ADP
-
Desulfovibrio desulfuricans AMP + ATP
-
r
ADP
-
Megalodesulfovibrio gigas AMP + ATP
-
r

Subunits

Subunits Comment Organism
monomer 1 * 24500, SDS-PAGE, 1 * 24700, electrospray mass spectrometry, 1 * 24500, calculated Megalodesulfovibrio gigas
monomer 1 * 25500, SDS-PAGE, 1 * 24800, electrospray mass spectrometry Desulfovibrio desulfuricans

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
ADP formation Desulfovibrio desulfuricans

pH Range

pH Minimum pH Maximum Comment Organism
5.8 6.5 direction of ADP formation Megalodesulfovibrio gigas
7.5 9 direction of ATP formation Megalodesulfovibrio gigas

pH Stability

pH Stability pH Stability Maximum Comment Organism
4.8 11 stable within Desulfovibrio desulfuricans
4.8 11 stable within Megalodesulfovibrio gigas