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50661

Sigma-Aldrich

D-Tagatose 6-phosphate lithium salt

≥95% (TLC)

Synonym(s):

D-Tagatofuranose 6-phosphate lithium salt

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About This Item

Empirical Formula (Hill Notation):
C6H13O9P · xLi+
CAS Number:
Molecular Weight:
260.14 (free acid basis)
UNSPSC Code:
12352201
NACRES:
NA.25

Assay

≥95% (TLC)

optical activity

[α]/D 14.5±2.5°, c = 0.1 in H2O

storage temp.

−20°C

Related Categories

Application

D-Tagatose 6-phophate is a metabolite in the biosynthetic pathway converting galactose 6-phosphate to pyruvate. D-Tagatose 6-phosphate is a substrate for tagatose-6-phosphate kinase which converts it into D-tagatose 1,6-bisphosphate with the transfer of a phosphate from ATP.

Biochem/physiol Actions

An enzyme substrate for D-tagatose-6-phosphate kinase, and key metabolite of the tagatose-6-phosphate pathway linking D-galactose-6-phosphate with D-glyceraldehyde-3-phosphate.

Packaging

Bottomless glass bottle. Contents are inside inserted fused cone.

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

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Linda Miallau et al.
The Journal of biological chemistry, 282(27), 19948-19957 (2007-04-27)
High resolution structures of Staphylococcus aureus d-tagatose-6-phosphate kinase (LacC) in two crystal forms are herein reported. The structures define LacC in apoform, in binary complexes with ADP or the co-factor analogue AMP-PNP, and in a ternary complex with AMP-PNP and
B Nobelmann et al.
Biochimica et biophysica acta, 1262(1), 69-72 (1995-05-17)
The sequence of the gat operon for galactitol (Gat) utilization from a wild-type isolate of Escherichia coli, strain EC3132, is presented. The operon comprises 7 open reading frames (ORFs) called gatYZABCDR. The genes are transcribed from a promoter located upstream
V L Crow et al.
Journal of bacteriology, 153(1), 76-83 (1983-01-01)
The three enzymes of the D-tagatose 6-phosphate pathway (galactose 6-phosphate isomerase, D-tagatose 6-phosphate kinase, and tagatose 1,6-diphosphate aldolase) were absent in lactose-negative (Lac-) derivatives of Streptococcus lactis C10, H1, and 133 grown on galactose. The lactose phosphoenolpyruvate-dependent phosphotransferase system and

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