From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:1oza.jpg|left|200px]] | + | {{Seed}} |
| | + | [[Image:1oza.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_1oza| PDB=1oza | SCENE= }} | | {{STRUCTURE_1oza| PDB=1oza | SCENE= }} |
| | | | |
| - | '''Crystal Structure of the R103L Mutant of Aspartate Semialdehyde Dehydrogenase from Haemophilus influenzae'''
| + | ===Crystal Structure of the R103L Mutant of Aspartate Semialdehyde Dehydrogenase from Haemophilus influenzae=== |
| | | | |
| | | | |
| - | ==Overview==
| + | <!-- |
| - | The reversible dephosphorylation of beta-aspartyl phosphate to L-aspartate-beta-semialdehyde (ASA) in the aspartate biosynthetic pathway is catalyzed by aspartate-beta-semialdehyde dehydrogenase (ASADH). The product of this reaction is a key intermediate in the biosynthesis of diaminopimelic acid, an integral component of bacterial cell walls and a metabolic precursor of lysine and also a precursor in the biosynthesis of threonine, isoleucine and methionine. The structures of selected Haemophilus influenzae ASADH mutants were determined in order to evaluate the residues that are proposed to interact with the substrates ASA or phosphate. The substrate Km values are not altered by replacement of either an active-site arginine (Arg270) with a lysine or a putative phosphate-binding group (Lys246) with an arginine. However, the interaction of phosphate with the enzyme is adversely affected by replacement of Arg103 with lysine and is significantly altered when a neutral leucine is substituted at this position. A conservative Glu243 to aspartate mutant does not alter either ASA or phosphate binding, but instead results in an eightfold increase in the Km for the coenzyme NADP. Each of the mutations is shown to cause specific subtle active-site structural alterations and each of these changes results in decreases in catalytic efficiency ranging from significant (approximately 3% native activity) to substantial (<0.1% native activity).
| + | The line below this paragraph, {{ABSTRACT_PUBMED_15272161}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 15272161 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_15272161}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 29: |
Line 33: |
| | [[Category: Enzyme]] | | [[Category: Enzyme]] |
| | [[Category: Haemophilus influenzae]] | | [[Category: Haemophilus influenzae]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:28:04 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 21:49:15 2008'' |
Revision as of 18:49, 28 July 2008
Template:STRUCTURE 1oza
Crystal Structure of the R103L Mutant of Aspartate Semialdehyde Dehydrogenase from Haemophilus influenzae
Template:ABSTRACT PUBMED 15272161
About this Structure
1OZA is a Single protein structure of sequence from Haemophilus influenzae. Full crystallographic information is available from OCA.
Reference
The role of substrate-binding groups in the mechanism of aspartate-beta-semialdehyde dehydrogenase., Blanco J, Moore RA, Faehnle CR, Coe DM, Viola RE, Acta Crystallogr D Biol Crystallogr. 2004 Aug;60(Pt 8):1388-95. Epub 2004, Jul 21. PMID:15272161
Page seeded by OCA on Mon Jul 28 21:49:15 2008
