1arc

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[[Image:1arc.gif|left|200px]]
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{{STRUCTURE_1arc| PDB=1arc | SCENE= }}
{{STRUCTURE_1arc| PDB=1arc | SCENE= }}
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'''THE PRIMARY STRUCTURE AND STRUCTURAL CHARACTERISTICS OF ACHROMOBACTER LYTICUS PROTEASE I, A LYSINE-SPECIFIC SERINE PROTEASE'''
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===THE PRIMARY STRUCTURE AND STRUCTURAL CHARACTERISTICS OF ACHROMOBACTER LYTICUS PROTEASE I, A LYSINE-SPECIFIC SERINE PROTEASE===
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==Overview==
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The complete amino acid sequence of Achromobacter lyticus protease I (EC 3.4.21.50), which specifically hydrolyzes lysyl peptide bonds, has been established. This has been achieved by sequence analysis of the reduced and S-carboxymethylated protease and of peptides obtained by enzymatic digestion with Achromobacter protease I itself and Staphylococcus aureus V8 protease and by chemical cleavage with cyanogen bromide. The protease consists of 268 residues with three disulfide bonds, which have been assigned to Cys6-Cys216, Cys12-Cys80, and Cys36-Cys58. Comparison of the amino acid sequence of Achromobacter protease and other serine proteases of bacterial and mammalian origins has revealed that Achromobacter protease I is a mammalian-type serine protease of which the catalytic triad comprises His57, Asp113, and Ser194. It has also been shown that the protease has 9- and 26-residue extensions of the peptide chain at the N and C termini, respectively, and overall sequence homology is as low as 20% with bovine trypsin. The presence of a disulfide bridge between the N-terminal extension Cys6 and Cys216 close to the putative active site in the C-terminal region is thought to be responsible for the generation of maximal proteolytic function in the pH range 8.5-10.7 and enhanced stability to denaturation.
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(as it appears on PubMed at http://www.pubmed.gov), where 2492988 is the PubMed ID number.
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{{ABSTRACT_PUBMED_2492988}}
==About this Structure==
==About this Structure==
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[[Category: Katsube, Y.]]
[[Category: Katsube, Y.]]
[[Category: Kitagawa, Y.]]
[[Category: Kitagawa, Y.]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:37:01 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 17:27:48 2008''

Revision as of 14:27, 30 June 2008

Image:1arc.png

Template:STRUCTURE 1arc

THE PRIMARY STRUCTURE AND STRUCTURAL CHARACTERISTICS OF ACHROMOBACTER LYTICUS PROTEASE I, A LYSINE-SPECIFIC SERINE PROTEASE

Template:ABSTRACT PUBMED 2492988

About this Structure

1ARC is a Single protein structure of sequence from Achromobacter lyticus. Full crystallographic information is available from OCA.

Reference

The primary structure and structural characteristics of Achromobacter lyticus protease I, a lysine-specific serine protease., Tsunasawa S, Masaki T, Hirose M, Soejima M, Sakiyama F, J Biol Chem. 1989 Mar 5;264(7):3832-9. PMID:2492988

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