16060-65-4

Usage

Definition

ChEBI: Benzoic acid substituted at the para position by a guanidino group.

Upstream product

• 285556-33-4 4-((imino(methylthio)methyl)amino)benzoic acid 
• 420-04-2 CYANAMID 
• 150-13-0 4-amino-benzoic acid 
• 1184-90-3 aminoiminomethanesulfonic acid 
• 59721-29-8 camostat mesylate 
• 42823-46-1 4-guanidinobenzoic acid hydrochloride 
• 21658-26-4 4'-Nitrophenyl 4-guanidinobenzoate 
• 123-91-1 1,4-dioxane 
• 541-41-3 chloroformic acid ethyl ester 
• 162046-58-4 4-(N-tert-butyloxycarbonylaminomethyl)-cyclohexane-1-carboxylic acid 
• 619-45-4 4-methoxycarbonyl aniline 

Downstream Products

• 15639-51-7 4-guanidino-benzoic acid ethyl ester 
• 77020-02-1 4-Guanidino-benzoic acid carbamoylmethyl ester 
• 125789-07-3 4-Guanidino-benzoic acid 2,5-dioxo-pyrrolidin-1-yl ester 
• 59721-27-6 N,N-Di-n-Propylcarbamoylmethyl-p-(p-Guanidinobenzoyloxy)Benzoate Tosylate 
• 1616960-57-6 4-guanidino-N-(2-(2-methyl-1H-indol-1-yl)ethyl)benzamide 

Relevant academic research and scientific papers

The PREPL A protein, a new member of the prolyl oligopeptidase family, lacking catalytic activity

The PREPL (previously called KIAA0436) gene encodes a putative serine peptidase from the prolyl oligopeptidase family. A chromosomal deletion involving the PREPL gene leads to a severe syndrome with multiple symptoms. Homology with oligopeptidase B suggested that the enzyme cleaves after an arginine or lysine residue. Several PREPL splice variants have been identified, and a 638-residue variant (PREPL A) was expressed in Escherichia coli and purified. Its secondary structure was similar to that of oligopeptidase B, but differential-scanning calorimetry indicated a higher conformational stability. Dimerization may account for the enhanced stability. Unexpectedly, the PREPL A protein did not cleave peptide substrates containing a P1 basic residue, but did slowly hydrolyse an activated ester substrate, and reacted with diisopropyl fluorophosphate. These results indicated that the catalytic serine is a reactive residue. However, the negligible hydrolytic activity suggests that the function of PREPL A is different from that of the other members of the prolyl oligopeptidase family. Birkhaeuser Verlag, 2005.

Direct guanylation of amino groups by cyanamide in water: Catalytic generation and activation of unsubstituted carbodiimide by scandium(iii) triflate

Guanylation proceeded efficiently upon treatment of the various amines with cyanamide in the presence of catalytic amounts of scandium(III) triflate under mild conditions. The method did not require the guanylation reagents to be preactivated, and the reaction proceeded efficiently in water. The method, therefore, has practical utility for substrates that dissolve only in aqueous solutions, for example, peptides or pharmacologically important compounds. Georg Thieme Verlag Stuttgart New York.

Hydrolytic profile for ester- or amide-linkage by carboxylesterases pI 5.3 and 4.5 from human liver

Carboxylesterases (EC 3.1.1.1) from human liver were purified using Q- Sepharose, Sephadex G-150, isoelectrofocusing and Con A-Sepharose. The calculated molecular mass of the pI 5.3 enzyme was 120 kDa and 61 kDa from the results of Sephadex G-150 gel filtration and SDS-polyacrylamide gel electrophoresis (PAGE), respectively, suggesting that this enzyme is a dimer. On the other hand, carboxylesterase pI 4.5, with a molecular-mass of 64 kDa, was a monomer. The activities of both enzymes were inhibited by typical serine enzyme inhibitors. Amino acid sequence analysis of the purified enzymes pI 5.3 and 4.5 showed high homology with rabbit carboxylesterase form 1 and 2, respectively. The results also suggested that carboxylesterase pI 5.3 is identical to the deduced amino acid sequence from cDNA for HUI, and that carboxylesterase pI 4.5 is identical to the deduced amino acid sequence from the cDNA registered as human carboxylesterase (hCE-2) in GenBank. We first purified carboxylesterase pI 4.5 and investigated its hydrolytic activity upon various drugs. The two enzymes differed in substrate specificity. Prodrugs of angiotensin-converting enzyme inhibitors, such as delapril and imidapril, were converted to active metabolites by carboxylesterase pI 5.3, but not by carboxylesterase pI 4.5. The hydrolysis velocity of temocapril by carboxylesterase pI 5.3 was 12-fold faster than by carboxylesterase pI 4.5. In contrast, aspirin oxybutynin and procaine were hydrolyzed by only carboxylesterase pI 4.5. We also found that an amide- linkage in drugs, except for that in aniracetam was not a good substrate for the two enzymes. Consequently, carboxylesterases pI 5.3 and 4.5 maybe involved in the metabolism of various drugs containing an ester-linkage.

Synthesis of 4-(4-guanidinobenzoyloxy)benzamides and 1-(4-guanidinobenzoyloxy)benzoyloxy acetamides as trypsin inhibitors

Seventeen new compounds of 4-(4-guanidinobenzoyloxy)benzamides and 4-(4-guanidinobenzoyloxy)benzoyloxyacetamides were prepared and their inhibitory activities on trypsin, thrombin and porcine pancreatic elastase were measured. These compounds were found to be selective trypsin inhibitors with inhibiting activities from 0.44 to 43 μM.

Synthesis and structure-activity study of protease inhibitors. V. Chemical modification of 6-amidino-2-naphthyl 4-guanidinobenzoate

By developing 6-amidino-2-naphthyl 4-guanidinobenzoate (I, FUT-175) as a basic structure, its various derivatives were synthesized and their inhibitory activities on trypsin, plasmin, kallikrein, thrombin, C1r and C1s as well as on complement-mediated hemolysis were examined. The protective effect of these compounds on complement-mediated Forssman shock was also examined in guinea pigs. 6-Amidino-2-naphthyl 4-[(4,5-dihydro-1H-imidazol-2-yl)amino]benzoate (41, FUT-187) was found to be a suitable compound for oral administration with anti-complement activity superior to that of compound I.

Esterase-like activity of human serum albumin. VII. Reaction with p-nitrophenyl 4-guanidinobenzoate

The reaction of p-nitrophenyl 4-guanidinobenzoate (NPGB) with human serum albumin (HSA) was examined kinetically at various pH's and 25°C. The Michaelis constant (K(s) in M) and the catalytic rate constant (k2 in s-1) were determined. The ratio of k2 to k0 (hydrolysis rate constant of NPGB in s-1) at pH 7.4 was 75.6, indicating the esterase-like activity of HSA The effects of the reversible binding of site-specific drugs and the chemical modification by site-specific reagents on the HSA activity indicated that HSA has multiple reactive sites towards NPGB. Results of the reaction in the presence of excess NPGB over HSA also suggested the existence of multiple active sites. The pH-profile for k2 showed inflection points at about pH 6.0 and pH 10.0, suggesting the involvement of groups with pK(a)'s of 6.0 and 10.0 in HSA.

Phenylalanine derivative and proteinase inhibitor

A phenylalanine derivative having the formula (I): wherein mis 0, l, or 2 and nis 3, 4, or 5;, X represents (a) hydroxy, (b) nitro, (c) amino, (d) phenoxy which may be substituted with (i) halogen or (ii) nitro, (e) C1-C4 alkyloxy which may be substituted with (i) phenyl or (ii) benzoyl, (f) benzoyl, (g) pyridyloxy which may be substituted with (i) halogen or (ii) nitro, or (h) C1-C4 alkyl which may be substituted with halogen;, Y represents or -OR3 wherein, R1 and R2 are independently (a) hydrogen, (b) phenyl which may be substituted with (i) benzoyl, (ii) C1-C4 alkylcarbonyl, (iii) C1-C4 alkyl which may be further substituted with C1-C4 alkoxycarbonyl or hydroxycarbonyl, (iv) C2-C5 alkenyl which may be further substituted with hydroxycarbonyl or C1-C4 alkoxycarbonyl, (v) C1-C4 alkoxycarbonyl, or (vi) amidino, (c) pyridyl which may be substituted with halogen or carboxyl (d) imidazolyl, (e) pyrimidyl, (f) tetrazolyl, (g) thiazolyl which may be substituted with C1-C4 alkyl which may be further substituted with C1-C4 alkoxycarbonyl, (h) C1-C6 alkyl which may be substituted with C1-C4 alkoxy, C1-C4 alkoxycarbonyl, phenyl, or benzoyl, (i) C5-C7 cycloalkyl which may be substituted with C1-C4 alkoxycarbonyl or (j) R1 and R2 may form, with the nitrogen atom attached thereto, (i) pyperazyl which may be substituted on the nitrogen atom with C1-C4 alkyl which may be further substituted with phenyl, (ii) piperidino which may be substituted with carboxyl or C1-C4 alkoxycarbonyl, (iii) pyrrolidyl which may be substituted with C1-C4 alkoxycarbonyl, or (iv) morpholyl; and, R3 represents (a) hydrogen, (b) C1-C6 alkyl which may be substituted with (i) C1-C4 alkoxy, (ii) phenyl, or (iii) pyridyl, or (c) pyridyl; or a pharmaceutically acceptable acid salt thereof. This phenylalanine derivative is effective as a proteinase.

A Facile Conversion of Amino Acids to Guanidino Acids

The conversion of amino acids to guanidino acids by the action of aminoiminomethanesulfonic acids (2a-c) is reported.Compounds 2a-c were synthesized by peracetic acid oxidation of the corresponding thioureas.