11075-17-5 Usage
Chemical Properties
Suspension (white)
Uses
The enzyme from Sigma has been used as a comparison to study the specificity of Metarhizium anisopliae carboxypeptidase A (MeCPA). MeCPA had been genetically engineered to facilitate the removal of polyhistidine tags from the C-termini of recombinant proteins. It has also been used to de-tyrosinate α-tubulin, in vitro, in order to induce high affinity to ethyl-N-phenylcarbamate (EPC) sepharose.
Definition
An enzyme that catalyzes the cleavage of amino acids
from a protein at the C-terminus of a polypeptide
chain.
General Description
Carboxypeptidase A-agarose product is prepared by the immobilization of carboxypeptidase A, originally isolated from the bovine pancreas, to activated 4% crosslinked beaded agarose.
Industrial uses
Carboxypeptidase A(CPA) is an enzyme of the digestive system that is known to cleave amino acids favouring the C-terminal end as well as certain esters. This enzymatic activity depends on the metal at the catalytic site. Zn2+ and some Co2+-containing CPAs exhibit peptidase function, whilst esterase function has been seen by CPAs containing a variety of divalent d-block metals. CPA has a size similar to CA, consisting of about 300 amino acids and a molecular mass of 34 kDa.
Biochem/physiol Actions
Carboxypeptidase as isolated from bovine pancreas glands is a metalloenzyme that contains 1 g atom of zinc per mole of protein. It catalyzes the hydrolysis of the carboxyl-terminal peptide bond in peptides and proteins. It is primarily specific to aromatic and hydrophobic side chains such as phenylalanine, tryptophan or leucine. The enzyme also exhibits esterase activity. It is inhibited by beta-phenylpropionate and indole acetate.
Purification Methods
Carboxypeptidase A is purified by DEAE-cellulose chromatography, activation with trypsin and dialysed against 0.1M NaCl, yielding crystals. It is recrystallised by dissolving in 20 mL of M NaCl and dialysed for 24hours each against the following salts present in 500mL of 0.02M sodium veronal pH 8.0, 0.5M NaCl, 0.2M NaCl and 0.15M NaCl. The last dialysate usually induces crystallisation. If it does not crystallise, then dialyse the last solution against 0.02M sodium veronal containing 0.10M NaCl. Only 2 or 3 recrystallisations are required to attain maximum activity. [Cox et al. Biochemistry 3 44 1964.] Enzyme activity is measured by hydrolysing hippuryl-L-phenylalanine (or phenylacetic acid) and observing the rate of change of optical density at 254nm (reaction extinction coefficient is ~0.592 cm2/Wmole at pH 7.5) [Bergmyer Methods in Enzymatic Analysis (Academic Press) 1 436 1974].
Check Digit Verification of cas no
The CAS Registry Mumber 11075-17-5 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 1,1,0,7 and 5 respectively; the second part has 2 digits, 1 and 7 respectively.
Calculate Digit Verification of CAS Registry Number 11075-17:
(7*1)+(6*1)+(5*0)+(4*7)+(3*5)+(2*1)+(1*7)=65
65 % 10 = 5
So 11075-17-5 is a valid CAS Registry Number.
11075-17-5Relevant articles and documents
Method for synthesizing N-ethylethanolamine by micro-channel reactor
-
Paragraph 0029; 0035-0037; 0043-0045; 0051-0053; 0059-0061, (2020/12/09)
The invention discloses a method for synthesizing N-ethylethanolamine by a micro-channel reactor. The method comprises the steps: adopting a Corning high-flux continuous flow micro-channel reactor, setting the flow velocity of the ethylene oxide aqueous solution to be 36.0-46.0mL/min and the flow velocity of the ethylamine aqueous solution to be 20.0mL/min, and respectively pumping the ethylene oxide aqueous solution and the ethylamine aqueous solution into the reactor to be preheated in a first module, that is, a straight-flow type preheating module, which has the temperature of 25-40 DEG C and is independent from each other; and then respectively making the solution enter a second module, that is, an enhanced mass transfer type mixing module, through an inlet A or an inlet B of the reactor, carrying out mixing reaction for 60-200 seconds at the temperature of 25-40 DEG C, and enabling the mixed liquid after the reaction to flow out from an outlet of the reactor; and collecting the output liquid of the micro-channel reaction device, and carrying out dehydrating to obtain the N-ethylethanolamine. The method has the advantages of short time, high efficiency, few byproducts, safety,stability and controllability, and the synthesized N-ethylethanolamine is suitable for pharmaceutical and chemical intermediates.
Hydrogenolysis of Amide Acetals and Iminium Esters
Kadyrov, Renat
, p. 170 - 172 (2017/12/26)
Amide acetals and iminium esters were hydrogenated into amines under very mild reaction conditions over common hydrogenation catalysts. This finding provides a new strategy for the selective reduction of amides. The synthetic utility of this approach was demonstrated by the selective reduction of amides bearing ester and nitrile groups.
Catalytic Hydrogenation for the Preparation of Amines from Amide Acetals, Ketene N,O-Acetals or Ester Imides
-
Paragraph 0153; 0154, (2016/10/04)
The present invention relates to a process for the preparation of amines, comprising the following steps: Reaction of a (i) amide acetal of the general formula (I), or (ii) ketene N,O-acetal of the general formula (II), or (iii) ester imide of the general formula (III) with H2 in the presence of a hydrogenation catalyst, where catalyst and amide acetal or ketene N,O-acetal or ester imide are used in a molar ratio of from 1:10 to 1:100 000 and where a hydrogen pressure of from 0.1 bar to 200 bar is established and where a temperature in the range of from 0° C. to 250° C. is established.
