Similar articles for PMID: 12501175

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1

The crystal structure of the H48Q active site mutant of human group IIA secreted phospholipase A2 at 1.5 A resolution provides an insight into the catalytic mechanism.

Edwards SH, Thompson D, Baker SF, Wood SP, Wilton DC. Edwards SH, et al. Biochemistry. 2002 Dec 31;41(52):15468-76. doi: 10.1021/bi020485z. Biochemistry. 2002. PMID: 12501175

2

Catalytic role of the active site histidine of porcine pancreatic phospholipase A2 probed by the variants H48Q, H48N and H48K.

Janssen MJ, van de Wiel WA, Beiboer SH, van Kampen MD, Verheij HM, Slotboom AJ, Egmond MR. Janssen MJ, et al. Protein Eng. 1999 Jun;12(6):497-503. doi: 10.1093/protein/12.6.497. Protein Eng. 1999. PMID: 10388847

3

Structures of the catalytic site mutants D99A and H48Q and the calcium-loop mutant D49E of phospholipase A2.

Sekar K, Biswas R, Li Y, Tsai M, Sundaralingam M. Sekar K, et al. Acta Crystallogr D Biol Crystallogr. 1999 Feb;55(Pt 2):443-7. doi: 10.1107/s0907444998013699. Acta Crystallogr D Biol Crystallogr. 1999. PMID: 10089353

4

Effect of tryptophan insertions on the properties of the human group IIA phospholipase A2: mutagenesis produces an enzyme with characteristics similar to those of the human group V phospholipase A2.

Beers SA, Buckland AG, Giles N, Gelb MH, Wilton DC. Beers SA, et al. Biochemistry. 2003 Jun 24;42(24):7326-38. doi: 10.1021/bi0343222. Biochemistry. 2003. PMID: 12809488

5

Structure, function and interfacial allosterism in phospholipase A2: insight from the anion-assisted dimer.

Bahnson BJ. Bahnson BJ. Arch Biochem Biophys. 2005 Jan 1;433(1):96-106. doi: 10.1016/j.abb.2004.08.013. Arch Biochem Biophys. 2005. PMID: 15581569 Review.

6

Tryptophan-containing mutant of human (group IIa) secreted phospholipase A2 has a dramatically increased ability to hydrolyze phosphatidylcholine vesicles and cell membranes.

Baker SF, Othman R, Wilton DC. Baker SF, et al. Biochemistry. 1998 Sep 22;37(38):13203-11. doi: 10.1021/bi981223t. Biochemistry. 1998. PMID: 9748327

7

Suggestive evidence for the involvement of the second calcium and surface loop in interfacial binding: monoclinic and trigonal crystal structures of a quadruple mutant of phospholipase A2.

Sekar K, Yogavel M, Kanaujia SP, Sharma A, Velmurugan D, Poi MJ, Dauter Z, Tsai MD. Sekar K, et al. Acta Crystallogr D Biol Crystallogr. 2006 Jul;62(Pt 7):717-24. doi: 10.1107/S0907444906014855. Epub 2006 Jun 20. Acta Crystallogr D Biol Crystallogr. 2006. PMID: 16790927

8

Active site of bee venom phospholipase A2: the role of histidine-34, aspartate-64 and tyrosine-87.

Annand RR, Kontoyianni M, Penzotti JE, Dudler T, Lybrand TP, Gelb MH. Annand RR, et al. Biochemistry. 1996 Apr 9;35(14):4591-601. doi: 10.1021/bi9528412. Biochemistry. 1996. PMID: 8605210

9

Crystal structure of the Y52F/Y73F double mutant of phospholipase A2: increased hydrophobic interactions of the phenyl groups compensate for the disrupted hydrogen bonds of the tyrosines.

Sekharudu C, Ramakrishnan B, Huang B, Jiang RT, Dupureur CM, Tsai MD, Sundaralingam M. Sekharudu C, et al. Protein Sci. 1992 Dec;1(12):1585-94. doi: 10.1002/pro.5560011206. Protein Sci. 1992. PMID: 1304890 Free PMC article.

10

Phospholipase A2 engineering. Deletion of the C-terminus segment changes substrate specificity and uncouples calcium and substrate binding at the zwitterionic interface.

Huang B, Yu BZ, Rogers J, Byeon IJ, Sekar K, Chen X, Sundaralingam M, Tsai MD, Jain MK. Huang B, et al. Biochemistry. 1996 Sep 17;35(37):12164-74. doi: 10.1021/bi960234o. Biochemistry. 1996. PMID: 8810924

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