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Page 1
Showing results for suc ala
Your search for sucralan retrieved no results
Inhibitors on an elastase-like enzyme activity catalyzing Suc-Ala-Ala-Pro-Leu-pNA amidolysis in human seminal plasma.
Matsuda Y, Katayama M, Hara I, Sato H, Tomomasa H, Iizumi T, Umeda T, Ishikawa H. Matsuda Y, et al. Arch Androl. 2000 Jan-Feb;44(1):1-9. doi: 10.1080/014850100262353. Arch Androl. 2000. PMID: 10690759
No relation was observed between human pancreatic elastase antigen and the Suc-Ala-Ala-Pro-Leu-pNA amidolytic enzyme enzyme activity in HSP. ...Suc-Ala-Ala-Pro-Leu-pNA amidolytic enzyme activity in HSP is not an elastase-like metalloprote …
No relation was observed between human pancreatic elastase antigen and the Suc-Ala-Ala-Pro-Leu-pNA amidolytic enzyme en …
PepN, the major Suc-LLVY-AMC-hydrolyzing enzyme in Escherichia coli, displays functional similarity with downstream processing enzymes in Archaea and eukarya. Implications in cytosolic protein degradation.
Chandu D, Kumar A, Nandi D. Chandu D, et al. J Biol Chem. 2003 Feb 21;278(8):5548-56. doi: 10.1074/jbc.M207926200. Epub 2002 Dec 12. J Biol Chem. 2003. PMID: 12482750 Free article.
We identified PepN, previously characterized as the sole alanine aminopeptidase in E. coli, to be responsible for the hydrolysis of Suc-LLVY-AMC. PepN is an aminoendopeptidase. First, extracts from an ethyl methanesulfonate-derived PepN mutant, 9218, did not cleave Suc …
We identified PepN, previously characterized as the sole alanine aminopeptidase in E. coli, to be responsible for the hydrolysis of Suc …
Solid-phase synthesis of peptide-4-nitroanilides.
Kaspari A, Schierhorn A, Schutkowski M. Kaspari A, et al. Int J Pept Protein Res. 1996 Nov;48(5):486-94. doi: 10.1111/j.1399-3011.1996.tb00867.x. Int J Pept Protein Res. 1996. PMID: 8956082
The method was extended to amino acids possessing a side chain missing an anchor for binding to the matrix. We synthesized Suc-Ala-Phe-Pro-Gln-Phe-NH-Np anchoring the dipeptide derivative Fmoc-Glu-Phe-NH-Np with the carboxyl group to Rink amide resin using standard …
The method was extended to amino acids possessing a side chain missing an anchor for binding to the matrix. We synthesized Suc-Ala …
Site-Selective Incorporation of a Functional Group into Lys175 in the Vicinity of the Active Site of Chymotrypsin by Using Peptidyl α-Aminoalkylphosphonate Diphenyl Ester-Derivatives.
Ono S, Koga M, Arimura Y, Hatakeyama T, Kobayashi M, Sagara JI, Nakai T, Horino Y, Kuroda H, Oyama H, Arima K. Ono S, et al. Molecules. 2023 Mar 31;28(7):3150. doi: 10.3390/molecules28073150. Molecules. 2023. PMID: 37049913 Free PMC article.
We previously reported that Lys175 in the region of the active site of chymotrypsin (Csin) could be site-selectively modified by using an N-hydroxy succinimide (NHS) ester of the peptidyl derivative containing 1-amino-2-ethylphenylphosphonate diphenyl ester [NHS-Suc-Ala …
We previously reported that Lys175 in the region of the active site of chymotrypsin (Csin) could be site-selectively modified by using an N- …
Synthesis and application of MeOSuc-Ala-Ala-Pro-Phe-CH2Cl as potent proteinase K inhibitor.
Kore AR, Shanmugasundaram M, Hoang Q, Kuo M, Chapman LM, Chen HH. Kore AR, et al. Bioorg Med Chem Lett. 2009 Mar 1;19(5):1296-300. doi: 10.1016/j.bmcl.2009.01.077. Epub 2009 Feb 9. Bioorg Med Chem Lett. 2009. PMID: 19211247
The synthesis and proteolytic inhibitor function of two new tetrapeptides, methoxysuccinyl-Ala-Ala-Pro-Phe-chloromethyl ketone (MeOSuc-AAPF-CH(2)Cl) and methoxysuccinyl-Ala-Pro-Ala-Phe-chloromethyl ketone (MeOSuc-APAF-CH(2)Cl) are described. ...Interes …
The synthesis and proteolytic inhibitor function of two new tetrapeptides, methoxysuccinyl-Ala-Ala-Pro-Phe-chloromethyl ketone …
A new serine protease family with elastase activity is produced by Streptomyces bacteria.
Fujii T, Fukano K, Hirano K, Mimura A, Terauchi M, Etoh SI, Iida A. Fujii T, et al. Microbiology (Reading). 2020 Mar;166(3):253-261. doi: 10.1099/mic.0.000880. Microbiology (Reading). 2020. PMID: 31896394 Free article.
Although the deduced primary structure of SEL has sequence similarity to proteins in the S1 protease family, the amino acid sequence shares low identity (< 31.5 %) with any known elastase. SEL efficiently hydrolyses synthetic peptides having Ala or Val in the P1 positio …
Although the deduced primary structure of SEL has sequence similarity to proteins in the S1 protease family, the amino acid sequence shares …
Production of 5-aminolevulinic acid by cell free multi-enzyme catalysis.
Meng Q, Zhang Y, Ju X, Ma C, Ma H, Chen J, Zheng P, Sun J, Zhu J, Ma Y, Zhao X, Chen T. Meng Q, et al. J Biotechnol. 2016 May 20;226:8-13. doi: 10.1016/j.jbiotec.2016.03.024. Epub 2016 Mar 21. J Biotechnol. 2016. PMID: 27012885
Here we reported our work on developing a cell free process for ALA production using thermostable enzymes. Cheap substrates (succinate and glycine) were used for ALA synthesis by two enzymes: 5-aminolevulinic acid synthase (ALAS) from Laceyella sacchari (LS-ALAS) an …
Here we reported our work on developing a cell free process for ALA production using thermostable enzymes. Cheap substrates (succinat …
Conformational preferences of X-Pro sequences: Ala-Pro and Aib-Pro motifs.
Byun BJ, Song IK, Chung YJ, Ryu KH, Kang YK. Byun BJ, et al. J Phys Chem B. 2010 Nov 11;114(44):14077-86. doi: 10.1021/jp107200f. J Phys Chem B. 2010. PMID: 20949964
Ac-Ala-Pro-NHMe favors the type VI beta-turns in the gas phase and the open conformations in water. ...The calculated rotational barrier for Ac-Ala-Pro-NHMe is consistent with the observed value of 19.3 kcal/mol for Suc-Ala-Ala-Pro-Phe-pNA from …
Ac-Ala-Pro-NHMe favors the type VI beta-turns in the gas phase and the open conformations in water. ...The calculated rotational barr …
Elastase secretion in Acanthamoeba polyphaga.
Ferreira GA, Magliano AC, Pral EM, Alfieri SC. Ferreira GA, et al. Acta Trop. 2009 Nov;112(2):156-63. doi: 10.1016/j.actatropica.2009.07.015. Epub 2009 Jul 24. Acta Trop. 2009. PMID: 19632188
Screening with synthetic substrates mainly showed the activity of serine peptidases. ACM efficiently hydrolysed Suc-Ala(2)-Pro-Leu-pNA and Suc-Ala(2)-Pro-Phe-pNA over a broad pH range (7.0-9.5) and was weakly active against Suc-Ala(3)-pNA …
Screening with synthetic substrates mainly showed the activity of serine peptidases. ACM efficiently hydrolysed Suc-Ala(2)-Pro …
296 results