Skip to Content
Merck
CN

C0897

Citrate Lyase from Klebsiella pneumoniae

lyophilized powder, ≥0.20 unit/mg solid

Synonym(s):

Citrate oxaloacetate lyase

Sign In to View Organizational & Contract Pricing.

Select a Size


About This Item

CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-740-7
MDL number:
EC Number:
Technical Service
Need help? Our team of experienced scientists is here for you.
Let Us Assist
Technical Service
Need help? Our team of experienced scientists is here for you.
Let Us Assist

Product Name

Citrate Lyase from Klebsiella pneumoniae, lyophilized powder, ≥0.20 unit/mg solid

form

lyophilized powder

specific activity

≥0.20 unit/mg solid

mol wt

>5 kDa

storage temp.

2-8°C

Quality Level

Looking for similar products? Visit Product Comparison Guide

Application

Citrate Lyase from Klebsiella pneumoniae has been used in the digestion of low molecular weight human milk fraction (>5 kDa referred to as 5kF).

Biochem/physiol Actions

Citrate lyase is found in several microorganisms and catalyzes the first step of citrate degradation, forming acetate and oxaloacetate. The enzyme contains 3 polypeptide subunits, α-subunit (a transferase), β-subunit (acyl lyase) and γ-subunit (acyl-carrier protein).

Other Notes

One unit will convert 1.0 μmole of citrate to oxalacetate per min at pH 7.6 at 25 °C.

Physical form

Lyophilized powder containing bovine serum albumin, sucrose, and MgSO4

Storage Class

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

Regulatory Information

含少量动物源组分生物产品
常规特殊物品
This item has

Choose from one of the most recent versions:

Certificates of Analysis (COA)

Lot/Batch Number

Don't see the Right Version?

If you require a particular version, you can look up a specific certificate by the Lot or Batch number.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

R Singh et al.
Journal of biochemical and biophysical methods, 64(3), 189-199 (2005-09-13)
We demonstrate a facile blue native polyacrylamide gel electrophoresis (BN-PAGE) technique to detect two malate-generating enzymes, namely fumarase (FUM), malate synthase (MS) and four oxaloacetate-forming enzymes, namely pyruvate carboxylase (PC), phosphoenolpyruvate carboxykinase (PEPCK), citrate lyase (CL) and aspartate aminotransferase (AST).
M Martín et al.
Journal of bacteriology, 182(14), 3904-3912 (2000-06-27)
In this study we describe the expression pattern of the Leuconostoc paramesenteroides citMCDEFGRP operon in response to the addition of citrate to the growth medium. An 8.8-kb polycistronic transcript, which includes the citMCDEFGRP genes, was identified; its synthesis was dramatically
M Isabel Burguete et al.
Dalton transactions (Cambridge, England : 2003), (36)(36), 4027-4033 (2007-09-11)
A turn-on fluorescent indicator for citric acid (citrate) has been developed, displaying high emission enhancement (+1500%) and low interference by other carboxylates. The sensor is based on the non-emissive copper(II) complex of a fluorescent amino amide, which, upon addition of
S Bekal-Si Ali et al.
Journal of bacteriology, 181(14), 4411-4416 (1999-07-10)
In this paper, we describe two open reading frames coding for a NAD-dependent malic enzyme (mae) and a putative regulatory protein (clyR) found in the upstream region of citCDEFG of Leuconostoc mesenteroides subsp. cremoris 195. The transcriptional analysis of the
Celia W Goulding et al.
Journal of molecular biology, 365(2), 275-283 (2006-10-27)
Fatty acid biosynthesis is essential for the survival of Mycobacterium tuberculosis and acetyl-coenzyme A (acetyl-CoA) is an essential precursor in this pathway. We have determined the 3-D crystal structure of M. tuberculosis citrate lyase beta-subunit (CitE), which as annotated should

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service