Assay for rapid analysis of the tri-peptidase activity of LTA4 hydrolase

Proteins: Structure, Function and Genetics

Volumn 67, Issue 4, 2007, Pages 1113-1118

  Tholander, Fredrik ^a   Haeggström, Jesper Z ^a  

^a KAROLINSKA INSTITUTE   (Sweden)

Author keywords

Aminopeptidase; Competing substrates; Enzyme kinetics; Inflammation; Leukotriene; Natural substrate; Progress curve; Screening

Indexed keywords

CHROMOGENIC SUBSTRATE; LEUKOTRIENE A4 HYDROLASE; PEPTIDASE;

ARTICLE; COMPUTER ANALYSIS; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME ASSAY; KINETICS; PRIORITY JOURNAL; SCREENING; SPECTROPHOTOMETRY;

ANILINE COMPOUNDS; ARGININE; EPOXIDE HYDROLASES; KINETICS; PEPTIDES; SOFTWARE DESIGN; SUBSTRATE SPECIFICITY; TIME FACTORS;

EID: 34248594514     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.21329     Document Type: Article

References (16)

1. Haeggstrom JZ. Leukotriene A4 hydrolase/aminopeptidase, the gatekeeper of chemotactic leukotriene B4 biosynthesis. J Biol Chem 2004;279:50639-50642.
2. 4 hydrolase/ aminopeptidase. Prostaglandins 1992;44:251-257.
3. 4 hydrolase is an arginine aminopeptidase of high efficiency and specificity. J Biol Chem 1994;269:11269-11273.
4. 4 hydrolase: an anion activated peptidase. Biochim Biophys Acta 1992;1123:275-281.
5. Waley SG. Kinetic parameters from progress curves of competing substrates. Application to beta-lactamases. Biochem J 1983;211: 511-513.
6. Dixon M, Thorn CJ, Tipton KF, Webb EC. Enzymes In: Enzyme kinetics. London: Longman; 1979. pp 72-75.
7. 4 hydrolase/aminopeptidase: glutamate 271 is a catalytic residue with specific roles in two distinct enzyme mechanisms. J Biol Chem 2002;277:1398-1404.
8. Rudberg PC, Tholander F, Thunnissen MGM, Samuelsson B, Haeggström JZ. Leukotriene A4 hydrolase: selective abrogation of leukotriene B4 formation by mutation of aspartic acid 375. Proc Natl Acad Sci USA 2002;99:4215-4220.
9. Hollaway MR, Ticho T. A competition time-course method for following enzymic reactions applied to the hydrolysis of acetamide catalysed by an aliphatic amidase. FEBS Lett 1979;106: 185-188.
10. Ivanov IP, Miteva HJ, Yomtova VM. A simplified equation allowing the determination of kinetic constants of "invisible" substrates. Anal Biochem 2003;323:247-248.
11. Hwang SY, Brown KS, Gilvarg C. Rapid determination of kinetic constants by competitive spectrophotometry. Anal Biochem 1988; 170:161-167.
12. Xie D, Suvorov L, Erickson JW, Gulnik AS. Real-time measurements of dark substrate catalysis. Protein Sci 1999;8:2460-2464.
13. Mendes P. GEPASI: a software package for modelling the dynamics, steady states and control of biochemical and other systems. Comput Appl Biosci 1993;9:563-571.
14. Kuzmic P. Program DYNAFIT for the analysis of enzyme kinetic data: application to HIV proteinase. Anal Biochem 1996;237: 260-273.
15. Alkema WB, Floris R, Janssen DB. The use of chromogenic reference substrates for the kinetic analysis of penicillin acylases. Anal Biochem 1999;275:47-53.
16. Barret AJ, Rawlings ND, Woessner JF. Family M1 of membrane alanyl aminopeptidase. In: Barret AJ, Rawlings ND, Woessner JF, editors. Handbook of proteolytic enzymes. San Diego: Academic Press; 1998. pp 994-996.