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OEM Supply Daf - L-Cystine CAS:56-89-3 99% White crystals or crystalline powder – XD BIOCHEM

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OEM Supply Daf - L-Cystine CAS:56-89-3 99% White crystals or crystalline powder – XD BIOCHEM Detail:

Catalog Number XD90322
Product Name L-Cystine
CAS 56-89-3
Molecular Formula C6H12N2O4S2
Molecular Weight 240.30
Storage Details Ambient
Harmonized Tariff Code 29309013

 

Product Specification

Appearance White crystals or crystalline powder
Assay 99%
Grade USP32
Specific rotation -215° to -225°
Heavy metals <0.0015%
AS 1.5ppm max
SO4 0.040%max
Fe <0.003%
Loss on Drying 0.20%max
Residual on Ignition 0.10%max
Cl 0.10%max

 

The crystal structures of carboxypeptidase T (CpT) complexes with phenylalanine and arginine substrate analogs – benzylsuccinic acid and (2-guanidinoethylmercapto)succinic acid – were determined by the molecular replacement method at resolutions of 1.57 Å and 1.62 Å to clarify the broad substrate specificity profile of the enzyme. The conservative Leu211 and Leu254 residues (also present in both carboxypeptidase A and carboxypeptidase B) were shown to be structural determinants for recognition of hydrophobic substrates, whereas Asp263 was for recognition of positively charged substrates. Mutations of these determinants modify the substrate profile: the CpT variant Leu211Gln acquires carboxypeptidase B-like properties, and the CpT variant Asp263Asn the carboxypeptidase A-like selectivity. The Pro248-Asp258 loop interacting with Leu254 and Tyr255 was shown to be responsible for recognition of the substrate’s C-terminal residue. Substrate binding at the S1′ subsite leads to the ligand-dep endent shift of this loop, and Leu254 side chain movement induces the conformation rearrangement of the Glu277 residue crucial for catalysis. This is a novel insight into the substrate selectivity of metallocarboxypeptidases that demonstrates the importance of interactions between the S1′ subsite and the catalytic center.


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    OEM Supply Daf - L-Cystine CAS:56-89-3 99% White crystals or crystalline powder – XD BIOCHEM