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Published in 2021 at "FEBS letters"
DOI: 10.1002/1873-3468.14214
Abstract: The caseinolytic mitochondrial matrix peptidase chaperone subunit (ClpX) plays an important role in the heme-dependent regulation of 5-aminolevulinate synthase (ALAS1), a key enzyme in heme biosynthesis. However, the mechanisms underlying the role of ClpX in…
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Keywords:
dependent recognition;
clpx;
alas1;
aminolevulinate synthase ... See more keywords
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Published in 2023 at "Biochemistry"
DOI: 10.1021/acs.biochem.3c00087
Abstract: A recently discovered heme-dependent enzyme tyrosine hydroxylase (TyrH) offers a green approach for functionalizing the high-strength C-H and C-F bonds in aromatic compounds. However, there is ambiguity regarding the nature of the oxidant (compound 0…
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Keywords:
heme dependent;
tyrosine hydroxylase;
conformation;
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Published in 2023 at "ACS nano"
DOI: 10.1021/acsnano.2c11894
Abstract: Enzymes fold into three-dimensional structures to distribute amino acid residues for catalysis, which inspired the supramolecular approach to construct enzyme-mimicking catalysts. A key concern in the development of supramolecular strategies is the ability to confine…
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Keywords:
nanocatalysts review;
heme dependent;
supramolecular nanocatalysts;
dependent supramolecular ... See more keywords
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Published in 2021 at "Journal of the American Chemical Society"
DOI: 10.1021/jacs.1c00175
Abstract: The heme-dependent l-tyrosine hydroxylases (TyrHs) in natural product biosynthesis constitute a new enzyme family in contrast to the nonheme iron enzymes for DOPA production. A representative TyrH exhibits dual reactivity of C-H and C-F bond…
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Keywords:
bond;
dependent tyrosine;
tyrosine;
bond activation ... See more keywords