Add to ORKGThe X-ray structure of the enzyme 5-aminolaevulinate dehydratase (porphobilinogen synthase) from yeast has been solved to a resolution of 2.3 A using MAD data collected on the ESRF beamline BM14. The enzyme (abbreviated ALAD) catalyses an early key step in the biosynthesis of porphyrins and corrins namely the condensation of two 5-aminolaevulinic acid (ALA) molecules to form the pyrrole porphobilinogen (Jaff
5-Aminolaevulinic acid dehydratase (ALAD) is an early enzyme in the biosynthesis pathway of catalys...
5 Aminolevulinate synthase ALAS is the first and rate limiting enzyme of heme biosynthesis in huma...
SIGLEAvailable from British Library Document Supply Centre-DSC:DXN029537 / BLDSC - British Library D...
5-Aminolaevulinic acid dehydratase (ALAD) catalyzes the formation of porphobilinogen from two molecu...
X-ray diffraction images for yeast 5-aminolevulinic acid dehydratase co-crystallised with the substr...
5-Aminolaevulinate dehydratase (ALAD) is a homo-octameric metallo-enzyme that catalyses the formatio...
The X-ray structure of yeast 5-aminolaevulinic acid dehydratase, in which the catalytic site of the ...
The diffraction images which allowed the original 2.1 Angstrom resolution structure determinati...
The diffraction images which allowed the original 2.1 Angstrom resolution structure determination of...
X-ray diffraction images for yeast 5-aminolaevulinic acid dehydratase complexed with 4-oxosebacic ac...
The structures of 5-aminolaevulinic acid dehydratase (ALAD) complexed with substrate (5-aminolaevuli...
The X-ray structure of yeast 5-aminolaevulinic acid dehydratase, in which the catalytic site of the ...
AbstractThe structures of 5-aminolaevulinic acid dehydratase complexed with two irreversible inhibit...
<p>Diffraction images for a co-crystal of 5-aminolaevulinic acid dehydratase (ALAD) from yeast with ...
<p>X-ray diffraction images collected at the BW7B beamline at DESY (Hamburg) on 2 Jun 1998. More det...
5-Aminolaevulinic acid dehydratase (ALAD) is an early enzyme in the biosynthesis pathway of catalys...
5 Aminolevulinate synthase ALAS is the first and rate limiting enzyme of heme biosynthesis in huma...
SIGLEAvailable from British Library Document Supply Centre-DSC:DXN029537 / BLDSC - British Library D...
5-Aminolaevulinic acid dehydratase (ALAD) catalyzes the formation of porphobilinogen from two molecu...
X-ray diffraction images for yeast 5-aminolevulinic acid dehydratase co-crystallised with the substr...
5-Aminolaevulinate dehydratase (ALAD) is a homo-octameric metallo-enzyme that catalyses the formatio...
The X-ray structure of yeast 5-aminolaevulinic acid dehydratase, in which the catalytic site of the ...
The diffraction images which allowed the original 2.1 Angstrom resolution structure determinati...
The diffraction images which allowed the original 2.1 Angstrom resolution structure determination of...
X-ray diffraction images for yeast 5-aminolaevulinic acid dehydratase complexed with 4-oxosebacic ac...
The structures of 5-aminolaevulinic acid dehydratase (ALAD) complexed with substrate (5-aminolaevuli...
The X-ray structure of yeast 5-aminolaevulinic acid dehydratase, in which the catalytic site of the ...
AbstractThe structures of 5-aminolaevulinic acid dehydratase complexed with two irreversible inhibit...
<p>Diffraction images for a co-crystal of 5-aminolaevulinic acid dehydratase (ALAD) from yeast with ...
<p>X-ray diffraction images collected at the BW7B beamline at DESY (Hamburg) on 2 Jun 1998. More det...
5-Aminolaevulinic acid dehydratase (ALAD) is an early enzyme in the biosynthesis pathway of catalys...
5 Aminolevulinate synthase ALAS is the first and rate limiting enzyme of heme biosynthesis in huma...
SIGLEAvailable from British Library Document Supply Centre-DSC:DXN029537 / BLDSC - British Library D...