5191-80-0 Usage
Description
H-CYS(DPM)-OH, also known as S-benzylated cysteine, is a derivative of the amino acid cysteine where the thiol group is protected by a diphenylmethyl (DPM) group. This modification results in a white powder with unique chemical properties that make it suitable for various applications in different industries.
Uses
Used in Pharmaceutical Industry:
H-CYS(DPM)-OH is used as a protecting group for cysteine in the synthesis of peptides and proteins. The S-diphenylmethyl group effectively protects the thiol group of cysteine, preventing unwanted side reactions and ensuring the correct formation of disulfide bonds, which are crucial for the structure and function of many bioactive molecules.
Used in Chemical Synthesis:
H-CYS(DPM)-OH is used as an intermediate in the synthesis of various organic compounds, particularly those involving thiol-containing molecules. The DPM group can be selectively removed under mild conditions, allowing for the controlled deprotection of the thiol group and facilitating further chemical reactions.
Used in Research and Development:
H-CYS(DPM)-OH serves as a valuable tool in research and development, particularly in the fields of biochemistry, molecular biology, and medicinal chemistry. It can be used to study the effects of thiol protection on the properties and reactivity of cysteine-containing molecules, as well as to develop new methods for the synthesis and modification of peptides and proteins.
Check Digit Verification of cas no
The CAS Registry Mumber 5191-80-0 includes 7 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 4 digits, 5,1,9 and 1 respectively; the second part has 2 digits, 8 and 0 respectively.
Calculate Digit Verification of CAS Registry Number 5191-80:
(6*5)+(5*1)+(4*9)+(3*1)+(2*8)+(1*0)=90
90 % 10 = 0
So 5191-80-0 is a valid CAS Registry Number.
InChI:InChI=1/C16H17NO2S/c17-14(16(18)19)11-20-15(12-7-3-1-4-8-12)13-9-5-2-6-10-13/h1-10,14-15H,11,17H2,(H,18,19)
5191-80-0Relevant articles and documents
Crystallographic studies on the reaction of isopenicillin N synthase with an unsaturated substrate analogue
Elkins, Jonathan M.,Rutledge, Peter J.,Burzlaff, Nicolai I.,Clifton, Ian J.,Adlington, Robert M.,Roach, Peter L.,Baldwin, Jack E.
, p. 1455 - 1460 (2007/10/03)
Isopenicillin N synthase (IPNS) catalyses conversion of the linear tripeptie δ-(L-α-aminoadipoyl)-L-cysteinyl-D-valine (ACV) to isopenicillin N (IPN), the central step in biosynthesis of the β-lactam antibiotics. The unsaturated substrate analogue δ-(L-α-aminoadipoyl)-L-cysteinyl-D-vinylglycine (ACvG) has previously been incubated with IPNS and a single product was isolated, a 2-α-hydroxymethyl isopenicillin N (HMPen), formed via a monooxygenase mode of reactivity. ACvG has now been crystallised with IPNS and the structure of the anaerobic IPNS:Fe(II):ACvG complex determined to 1.15 A resolution. Furthermore, by exposing the anaerobically grown crystals to high-pressure oxygen gas, a structure corresponding to the bicyclic product HMPen has been obtained at 1.60 A resolution. In light of these and other IPNS structures, and recent developments with related dioxygenases, the [2 + 2] cycloaddition mechanism for HMPen formation from ACvG has been revised, and a stepwise radical mechanism is proposed. This revised mechanism remains consistent with the observed stereospecificity of the transformation, but fits better with apparent constraints on the coordination geometry around the active site iron atom.
Sulfide derivatives of cysteine.
VERDERAME
, p. 312 - 315 (2007/10/04)
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