Literature summary for 2.7.1.60 extracted from

Martinez, J.; Nguyen, L.; Hinderlich, S.; Zimmer, R.; Tauberger, E.; Reutter, W.; Saenger, W.; Fan, H.; Moniot, S.
Crystal structures of N-acetylmannosamine kinase provide insights into enzyme activity and inhibition (2012), J. Biol. Chem., 287, 13656-13665.

Crystallization (Commentary)

Crystallization (Comment)	Organism
ManNAc kinase in complex with its substrate ManNAc, its product ManNAc 6-phosphate, with or without ADP, vapor diffusion at 18°C, mixing 0.002 ml of 15 mg/ml protein in 10 mM Tris-HCl, pH 8.0, 150 mM NaCl, and 2 mM ManNAc, with 0.002 ml of reservoir solution containing 0.2 M calcium acetate, 0.1 M sodiumcacodylate, pH 6.5, and 40% PEG 300, 5 days, X-ray diffraction structure determination and analysis at 1.64-2.10 A resolution. No crystals by co-crystallization of hMNK with ManNAc and ADP, ATP, AMPPCP, or AMPPNP, but ternary complexes are obtained by soaking crystals of the binary hMNK-ManNAc complex replacing stepwise their mother liquor with solutions containing 0.1 M sodium cacodylate, pH 6.5, 50% PEG 300, and 20 mM ADPor ATP or nonhydrolyzable ATP derivatives	Homo sapiens

Crystallization (Comment)

Organism

ManNAc kinase in complex with its substrate ManNAc, its product ManNAc 6-phosphate, with or without ADP, vapor diffusion at 18°C, mixing 0.002 ml of 15 mg/ml protein in 10 mM Tris-HCl, pH 8.0, 150 mM NaCl, and 2 mM ManNAc, with 0.002 ml of reservoir solution containing 0.2 M calcium acetate, 0.1 M sodiumcacodylate, pH 6.5, and 40% PEG 300, 5 days, X-ray diffraction structure determination and analysis at 1.64-2.10 A resolution. No crystals by co-crystallization of hMNK with ManNAc and ADP, ATP, AMPPCP, or AMPPNP, but ternary complexes are obtained by soaking crystals of the binary hMNK-ManNAc complex replacing stepwise their mother liquor with solutions containing 0.1 M sodium cacodylate, pH 6.5, 50% PEG 300, and 20 mM ADPor ATP or nonhydrolyzable ATP derivatives

Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
D517A	site-directed mutagenesis, inactive mutant	Homo sapiens
D517N	site-directed mutagenesis, inactive mutant	Homo sapiens

Inhibitors

Inhibitors	Comment	Organism
3-O-methyl-N-acetylglucosamine	-	Homo sapiens
6-O-acetyl-N-acetylmannosamine	-	Homo sapiens
N-propanoylglucosamine	-	Homo sapiens

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.127	-	N-acyl-D-mannosamine	pH 8.1, 37°C, recombinant enzyme	Homo sapiens
4.4	-	ATP	pH 8.1, 37°C, recombinant enzyme	Homo sapiens

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
cytoplasm	-	Homo sapiens	5737	-

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	required, Mg2+ is octahedrically coordinated with the beta-phosphate-O3 atom and Asp-413-Odelta2 in the axial positions, whereas four water molecules occupy the equatorial sites	Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ATP + N-acyl-D-mannosamine	Homo sapiens	-	ADP + N-acyl-D-mannosamine 6-phosphate	-	?

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q9Y223	-	-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
2.6	-	pH 8.1, 37°C, recombinant enzyme	Homo sapiens

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + N-acyl-D-mannosamine	-	Homo sapiens	ADP + N-acyl-D-mannosamine 6-phosphate	-	?

Synonyms

Synonyms	Comment	Organism
MNK	-	Homo sapiens
UDP-GlcNAc-2 epimerase/ManNAc kinase	-	Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
37	-	assay at	Homo sapiens

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
8.1	-	assay at	Homo sapiens

Cofactor

Cofactor	Comment	Organism	Structure
ATP	binding structure, overview	Homo sapiens

General Information

General Information	Comment	Organism
additional information	active site structure of the N-acetylmannosamine kinase domain, ligand binding and reaction mechanism, catalytic role of Asp517, overview. The side chain of Asp-413 does not directly bind one of the oxygens of the beta-phosphate but is necessary for Mg2+ coordination and consequently crucial for ATP binding	Clostridium acetobutylicum
physiological function	the bifunctional UDP-N-acetylglucosamine-2-epimerase/N-acetylmannosamine kinase transforms UDP-N-acetylglucosamine to N-acetylmannosamine followed by its phosphorylation to ManNAc 6-phosphate and has a direct impact on the sialylation of cell surface components	Clostridium acetobutylicum