Literature summary for 2.4.3.8 extracted from

Gu, Y.; Yu, R.K.
Identification and analysis of novel functional sites in human GD3-synthase (2008), Biochem. Biophys. Res. Commun., 370, 67-71.

Cloned(Commentary)

Cloned (Comment)	Organism
expression in CHO-K1 cells. Secretion of mouse interleukin-2 signal sequence and transmembrane domain truncated human GD3-synthase cDNA amino-acid residues 49-356	Homo sapiens

Crystallization (Commentary)

Crystallization (Comment)	Organism
secondary structure alignments between Campylobacter jejunii sialyltransferase CstII and human GD3-synthase. In the human enzyme, the side chain on residue N188 has a strong hydrogen bond with the carboxyl group on the sialic acid group of the donor substrate. Residue P189 has no interaction with the donor. The distance between S190 and the donor substrate is 4.4 A, this residue might weakly interact with the donor. R272 is 8.8 A away from the donor, suggesting that this residue has no function on donor substrate binding	Homo sapiens

Crystallization (Comment)

Organism

secondary structure alignments between Campylobacter jejunii sialyltransferase CstII and human GD3-synthase. In the human enzyme, the side chain on residue N188 has a strong hydrogen bond with the carboxyl group on the sialic acid group of the donor substrate. Residue P189 has no interaction with the donor. The distance between S190 and the donor substrate is 4.4 A, this residue might weakly interact with the donor. R272 is 8.8 A away from the donor, suggesting that this residue has no function on donor substrate binding

Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
N188D	mutation in a conserved residue identified by structure alignments between Campylobacter jejunii sialyltransferase CstII and human GD3-synthase, 6fold decrease in ratio Km to Vmax	Homo sapiens
R272A	mutation in a conserved residue identified by structure alignments between Campylobacter jejunii sialyltransferase CstII and human GD3-synthase, 4fold decrease in ratio Km to Vmax	Homo sapiens
S190A	mutation in a conserved residue identified by structure alignments between Campylobacter jejunii sialyltransferase CstII and human GD3-synthase, 4fold decrease in ratio Km to Vmax	Homo sapiens

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism
0.081	-	CMP-N-acetylneuraminate	mutant R272A, pH 6.5, 37°C	Homo sapiens
0.083	-	ganglioside GM3	wild-type, pH 6.5, 37°C	Homo sapiens
0.087	-	ganglioside GM3	mutant N188D, pH 6.5, 37°C	Homo sapiens
0.088	-	CMP-N-acetylneuraminate	wild-type, pH 6.5, 37°C	Homo sapiens
0.11	-	CMP-N-acetylneuraminate	mutant S190A, pH 6.5, 37°C	Homo sapiens
0.184	-	ganglioside GM3	mutant S190A, pH 6.5, 37°C	Homo sapiens
0.22	-	CMP-N-acetylneuraminate	mutant N188D, pH 6.5, 37°C	Homo sapiens
0.979	-	ganglioside GM3	mutant R272A, pH 6.5, 37°C	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q92185	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
CMP-N-acetylneuraminate + ganglioside GM3	-	Homo sapiens	CMP + ?	-	?