Crystal structure of glutamate-1-semialdehyde-2,1-aminomutase fromArabidopsis thaliana

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Crystal structure of glutamate-1-semialdehyde-2,1-aminomutase from Arabidopsis thaliana

Glutamate-1-semialdehyde-2,1-aminomutase (GSAM) catalyzes the isomerization of glutamate-1-semialdehyde (GSA) to 5-aminolevulinate (ALA) and is distributed in archaea, most bacteria and plants. Although structures of GSAM from archaea and bacteria have been resolved, a GSAM structure from a higher plant is not available, preventing further structure-function analysis. Here, the structure of GSA...

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Intersubunit signaling in glutamate-1-semialdehyde-aminomutase.

Enzymes are highly dynamic and tightly controlled systems. However, allosteric communication linked to catalytic turnover is poorly understood. We have performed an integrated approach to trap several catalytic intermediates in the alpha2-dimeric key enzyme of chlorophyll biosynthesis, glutamate-1-semialdehyde aminomutase. Our data reveal an active-site "gating loop," which undergoes a dramatic...

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Spectral kinetics of glutamate-1-semialdehyde aminomutase of Synechococcus.

Purified Synechococcus glutamate-1-semialdehyde aminotransferase (GSA-AT; EC 5.4.3.8) has absorption maxima characteristic of vitamin B6-containing enzymes and can be converted to the pyridoxamine 5'-phosphate or pyridoxal 5'-phosphate form by reaction with diaminovalerate or dioxovalerate, respectively, suggesting that these two analogues are intermediates in the conversion of glutamate 1-semi...

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Asymmetry of the Active Site Loop Conformation between Subunits of Glutamate-1-semialdehyde Aminomutase in Solution

Glutamate-1-semialdehyde aminomutase (GSAM) is a dimeric, pyridoxal 5'-phosphate (PLP)- dependent enzyme catalysing in plants and some bacteria the isomerization of L-glutamate-1-semialdehyde to 5-aminolevulinate, a common precursor of chlorophyll, haem, coenzyme B12, and other tetrapyrrolic compounds. During the catalytic cycle, the coenzyme undergoes conversion from pyridoxamine 5'-phosphate ...

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Reactions of glutamate semialdehyde aminotransferase (glutamate-1-semialdehyde 2,1 aminomutase) with vinyl and acetylenic substrate analogues analysed by rapid scanning spectrophotometry.

The reactions occurring when glutamate-1-semialdehyde amino-transferase (glutamate-1-semialdehyde 2,1 aminomutase, EC 5.4.3.8) was treated with two potential mechanism-based inactivators, namely 4-aminohex-5-enoate and 4-aminohex-5-ynoate, have been investigated by monitoring rapid transient changes in the absorption spectrum of the enzyme's prosthetic group, pyridoxal 5'-phosphate. In both cas...

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ژورنال

عنوان ژورنال: Acta Crystallographica Section F Structural Biology Communications

سال: 2016

ISSN: 2053-230X

DOI: 10.1107/s2053230x16007263