1t5f

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[[Image:1t5f.gif|left|200px]]
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{{Seed}}
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[[Image:1t5f.png|left|200px]]
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{{STRUCTURE_1t5f| PDB=1t5f | SCENE= }}
{{STRUCTURE_1t5f| PDB=1t5f | SCENE= }}
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'''arginase I-AOH complex'''
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===arginase I-AOH complex===
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==Overview==
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Arginase is a binuclear manganese metalloenzyme that catalyzes the hydrolysis of l-arginine to form l-ornithine and urea. Chiral L-amino acids bearing aldehyde side chains have been synthesized in which the electrophilic aldehyde C=O bond is isosteric with the C=N bond of L-arginine. This substitution is intended to facilitate nucleophilic attack by the metal-bridging hydroxide ion upon binding to the arginase active site. Syntheses of the amino acid aldehydes have been accomplished by reduction, oxidation, and Wittig-type reaction with a commercially available derivative of L-glutamic acid. Amino acid aldehydes exhibit inhibition in the micromolar range, and the X-ray crystal structure of arginase I complexed with one of these inhibitors, (S)-2-amino-7-oxoheptanoic acid, has been determined at 2.2 A resolution. In the enzyme-inhibitor complex, the inhibitor aldehyde moiety is hydrated to form the gem-diol: one hydroxyl group bridges the Mn(2+)(2) cluster and donates a hydrogen bond to D128, and the second hydroxyl group donates a hydrogen bond to E277. The binding mode of the neutral gem-diol may mimic the binding of the neutral tetrahedral intermediate and its flanking transition states in arginase catalysis.
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(as it appears on PubMed at http://www.pubmed.gov), where 15315440 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15315440}}
==About this Structure==
==About this Structure==
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[[Category: Aoh]]
[[Category: Aoh]]
[[Category: Arginase]]
[[Category: Arginase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:32:54 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 13:54:50 2008''

Revision as of 10:54, 28 July 2008

Template:STRUCTURE 1t5f

arginase I-AOH complex

Template:ABSTRACT PUBMED 15315440

About this Structure

1T5F is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

Design of amino acid aldehydes as transition-state analogue inhibitors of arginase., Shin H, Cama E, Christianson DW, J Am Chem Soc. 2004 Aug 25;126(33):10278-84. PMID:15315440

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