Literature summary for 2.7.1.36 extracted from

Miller, B.R.; Kung, Y.
Structural insight into substrate and product binding in an archaeal mevalonate kinase (2018), PLoS ONE, 13, e0208419 .

Cloned(Commentary)

Cloned (Comment)	Organism
recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain DH10B	Methanosarcina mazei

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified enzyme in mevalonate-bound and 5-phosphomevalonate-bound form, hanging drop vapor diffusion method, mixing of 11 mg/ml protein in 20 mM Tris pH 7.7, 10 mM MgCl2, and 10% glycerol, with 100 mM Bis-Tris pH 5.5, 200 mM sodium potassium tartrate, and 15-25% PEG 8000 or 10000, microseeding. Seeded drops contain 0.001 ml of protein with 1 mM (R)-mevalonate, 5 mM AMPPNP, and 5 mM MgCl2, and 800 nl crystallization solution, and 200 nl of the seed stock. Diffraction-quality plate crystals grow in crystallization solutions that contain 100 mM Bis-Tris, pH 5.5, 200-300 mM sodium potassium tartrate, and 15-25% PEG 8000 or 10000, X-ray diffraction structure determination and analysis at 2.1-2.46 A resolution, molecular replacement using the structure of the apo-MmMK from Methanosarcina mazei (PDB ID 4HAC) as the search model	Methanosarcina mazei

Crystallization (Comment)

Organism

purified enzyme in mevalonate-bound and 5-phosphomevalonate-bound form, hanging drop vapor diffusion method, mixing of 11 mg/ml protein in 20 mM Tris pH 7.7, 10 mM MgCl2, and 10% glycerol, with 100 mM Bis-Tris pH 5.5, 200 mM sodium potassium tartrate, and 15-25% PEG 8000 or 10000, microseeding. Seeded drops contain 0.001 ml of protein with 1 mM (R)-mevalonate, 5 mM AMPPNP, and 5 mM MgCl2, and 800 nl crystallization solution, and 200 nl of the seed stock. Diffraction-quality plate crystals grow in crystallization solutions that contain 100 mM Bis-Tris, pH 5.5, 200-300 mM sodium potassium tartrate, and 15-25% PEG 8000 or 10000, X-ray diffraction structure determination and analysis at 2.1-2.46 A resolution, molecular replacement using the structure of the apo-MmMK from Methanosarcina mazei (PDB ID 4HAC) as the search model

Methanosarcina mazei

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	Michaelis-Menten kinetics	Methanosarcina mazei

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	required	Methanosarcina mazei

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ATP + (R)-mevalonate	Methanosarcina mazei	-	ADP + (R)-5-phosphomevalonate	-	?

Organism

Organism	UniProt	Comment	Textmining
Methanosarcina mazei	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography	Methanosarcina mazei

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + (R)-mevalonate	-	Methanosarcina mazei	ADP + (R)-5-phosphomevalonate	-	?
additional information	analysis of substrate and product binding by archaeal mevalonate kinase compared to eukaryotic enzymes, a striking lack of direct interactions between this archaeal MK and its substrate is detected, substrate-binding site structure, overview	Methanosarcina mazei	?	-	-

Synonyms

Synonyms	Comment	Organism
MmMK	-	Methanosarcina mazei

General Information

General Information	Comment	Organism
metabolism	mevalonate kinase (MK) is a key enzyme of the mevalonate pathway, which produces the biosynthetic precursors for steroids, including cholesterol, and isoprenoids, the largest class of natural products	Methanosarcina mazei
additional information	structure comparisons of MVKs from different species, active site structure and structure-function analysis, detailed overview	Methanosarcina mazei