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Millipore

Moxalactam Supplement

suitable for microbiology

Synonym(s):

Listeria MOX Supplement

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About This Item

Empirical Formula (Hill Notation):
C20H20N6O9S
CAS Number:
Molecular Weight:
520.47
EC Number:
MDL number:
UNSPSC Code:
41171614
PubChem Substance ID:
NACRES:
NA.85

sterility

sterile

Quality Level

form

powder

shelf life

limited shelf life, expiry date on the label

application(s)

environmental
food and beverages

microbiology

storage temp.

2-8°C

suitability

Listeria spp.

SMILES string

CO[C@]2(NC(=O)C(C(O)=O)c1ccc(O)cc1)[C@H]3OCC(CSc4nnnn4C)=C(N3C2=O)C(O)=O

InChI

1S/C20H20N6O9S/c1-25-19(22-23-24-25)36-8-10-7-35-18-20(34-2,17(33)26(18)13(10)16(31)32)21-14(28)12(15(29)30)9-3-5-11(27)6-4-9/h3-6,12,18,27H,7-8H2,1-2H3,(H,21,28)(H,29,30)(H,31,32)/t12?,18-,20+/m1/s1

InChI key

JWCSIUVGFCSJCK-CAVRMKNVSA-N

General description

An antibiotic supplement recommended for selective isolation and cultivation of Listeria monocytogenes.

Application

for selective isolation and cultivation of Listeria monocytogenes

Components

(per vial, sufficient for 1000 ml medium)
Moxalactam 20.0 mg

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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A Zervosen et al.
European journal of biochemistry, 268(13), 3840-3850 (2001-07-04)
Incubation of moxalactam and cefoxitin with the Aeromonas hydrophila metallo-beta-lactamase CphA leads to enzyme-catalyzed hydrolysis of both compounds and to irreversible inactivation of the enzyme by the reaction products. As shown by electrospray mass spectrometry, the inactivation of CphA by
Xiaojun Wang et al.
Proteins, 47(1), 86-96 (2002-03-01)
The class A beta-lactamase TEM-1 is a key bacterial resistance enzyme against beta-lactam antibiotics, but little is known about the energetic bases for complementarity between TEM-1 and its inhibitors. Most inhibitors form a covalent adduct with the catalytic Ser70, making
Lionel Vercheval et al.
The Biochemical journal, 432(3), 495-504 (2010-11-27)
The activity of class D β-lactamases is dependent on Lys70 carboxylation in the active site. Structural, kinetic and affinity studies show that this post-translational modification can be affected by the presence of a poor substrate such as moxalactam but also
L Nauton et al.
Journal of molecular biology, 375(1), 257-269 (2007-11-15)
One mechanism by which bacteria can escape the action of beta-lactam antibiotics is the production of metallo-beta-lactamases. Inhibition of these enzymes should restore the action of these widely used antibiotics. The tetrameric enzyme L1 from Stenotrophomonas maltophilia was used as
James Spencer et al.
Journal of the American Chemical Society, 127(41), 14439-14444 (2005-10-13)
Metallo-beta-lactamases are zinc-dependent enzymes responsible for resistance to beta-lactam antibiotics in a variety of host bacteria, usually Gram-negative species that act as opportunist pathogens. They hydrolyze all classes of beta-lactam antibiotics, including carbapenems, and escape the action of available beta-lactamase

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