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Merck

H5000

Sigma-Aldrich

Hexokinase from Saccharomyces cerevisiae

Type III, lyophilized powder, ≥25 units/mg protein (biuret)

Synonym(s):

ATP:D-Hexose-6-phosphotransferase, Hexokinase from yeast

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10 NMOL
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Estimated to ship on17 May 2025


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10 NMOL
$960.00

About This Item

CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
UNSPSC Code:
12352204
eCl@ss:
32160410

$960.00


Estimated to ship on17 May 2025


Request a Bulk Order

type

Type III

form

lyophilized powder

specific activity

≥25 units/mg protein (biuret)

mol wt

dimer 110 kDa

UniProt accession no.

foreign activity

glucose-6-phosphate dehydrogenase and phosphoglucose isomerase ≤10%

storage temp.

−20°C

Gene Information

bakers yeast ... HXK1(850614) , HXK2(852639)

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This Item
494097836378362
assay

≥75.0% (HPLC)

assay

≥90% (HPLC)

assay

≥90% (HPLC)

assay

≥90% (HPLC), ≥90% (degree of coupling)

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

Quality Level

100

Quality Level

100

Quality Level

100

Quality Level

100

mol wt

Mw 1466 g/mol

mol wt

-

mol wt

Mw 818 g/mol

mol wt

Mw 793 g/mol

manufacturer/tradename

ATTO-TEC GmbH

manufacturer/tradename

ATTO-TEC GmbH

manufacturer/tradename

ATTO-TEC GmbH

manufacturer/tradename

ATTO-TEC GmbH

Biochem/physiol Actions

Catalyzes the phosphorylation of D-hexose sugars at the C6 position utilizing ATP as a phosphate source.

The rate of phosphorylation varies with different hexoses (pH 7.5, 30 °C).
D-fructose KM: 0.33 mM
D-glucose KM: 0.12 mM
D-mannose KM: 0.05 mM

Yeast hexokinase exists as two similar isoforms, PI and PII (A and B), with isoelectric points of 5.25 and 4, respectively.

Molecular Weight: ~ 54 kDa (monomer)
~110 kDa (dimer)
Optimal pH: 7.5 to 9.0
Extinction Coefficient: E1% = 8.85 (PI) and 9.47 (PII) at 280 nm

Activators: Hexokinase requires Mg2+ ions (KM = 2.6 mM) for activity. Hexokinase is activated by catecholamines and related compounds.

Inhibitors: sorbose-1-phosphate, polyphosphates, 6-deoxy-6-fluoroglucose, 2-C-hydroxy-methylglucose, xylose, lyxose, and thiol reactive compounds (Hg2+ and 4-chloromercuribenzoate)

Unit Definition

One unit will phosphorylate 1.0 μmole of D-glucose per min at pH 7.6 at 25 °C, unless otherwise indicated below.

Physical form

Lyophilized powder containing approx. 15% sodium citrate

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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Charles Betz et al.
The Journal of cell biology, 203(4), 563-574 (2014-01-05)
Target of rapamycin (TOR) forms two conserved, structurally distinct kinase complexes termed TOR complex 1 (TORC1) and TORC2. Each complex phosphorylates a different set of substrates to regulate cell growth. In mammals, mTOR is stimulated by nutrients and growth factors
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Proceedings of the National Academy of Sciences of the United States of America, 111(1), 409-414 (2013-12-25)
A hypoxic microenvironment induces resistance to alkylating agents by activating targets in the mammalian target of rapamycin (mTOR) pathway. The molecular mechanisms involved in this mTOR-mediated hypoxia-induced chemoresistance, however, are unclear. Here we identify the mTOR target N-myc downstream regulated
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Daniel Romaker et al.
Proceedings of the National Academy of Sciences of the United States of America, 111(17), 6335-6340 (2014-04-16)
MicroRNAs (miRNAs) are major posttranscriptional regulators of a wide variety of biological processes. However, redundancy among most miRNAs has made it difficult to identify their in vivo functions. We previously demonstrated that global inhibition of miRNA biogenesis in Xenopus resulted
Seok-Hyung Kim et al.
PLoS genetics, 9(6), e1003563-e1003563 (2013-06-21)
Multiple Acyl-CoA Dehydrogenase Deficiency (MADD) is a severe mitochondrial disorder featuring multi-organ dysfunction. Mutations in either the ETFA, ETFB, and ETFDH genes can cause MADD but very little is known about disease specific mechanisms due to a paucity of animal

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