Jesús F. Aparicio

Prof. Jesús F. Aparicio

Universidad de León, Spain
orcid

Research Focus & Metrics

Academic Career Length

39Years (1988-Present)

(Calculated once Scilit publication data is synced: current year − year of first publication + 1)

Representative Publications

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15 August 1995 in Proceedings of the National Academy of Sciences
Verified
Journal Article
Closed access
PDF file
TST Schwecke
T Schwecke
Jesús F. AparicioJesús F. Aparicio
Jesús F. Aparicio
IMIstvan Molnar
Istvan Molnar
AKAriane König
Ariane König
LKL E Khaw
L E Khaw
JLJ B Lester
J B Lester
The macrocyclic polyketides rapamycin and FK506 are potent immunosuppressants that prevent T-cell proliferation through specific binding to intracellular protein receptors (immunophilins). The cloning and specific alteration of the biosynthetic genes for these polyketides might allow the biosynthesis of clinically valuable analogues. We report here that three clustered polyketide synthase genes responsible for rapamycin biosynthesis in Streptomyces hygroscopicus together encode 14 homologous sets of enzyme activities (modules), each catalyzing a specific round of chain elongation. An adjacent gene encodes a pipecolate-incorporating enzyme, which completes the macrocycle. The total of 70 constituent active sites makes this the most complex multienzyme system identified so far. The DNA region sequenced (107.3 kbp) contains 24 additional open reading frames, some of which code for proteins governing other key steps in rapamycin biosynthesis.

30 October 1995 in FEBS Letters
Verified
Journal Article
Closed access
SHStephen F. Haydock
Stephen F. Haydock
Jesús F. AparicioJesús F. Aparicio
Jesús F. Aparicio
IMIstván Molnár
István Molnár
TSTorsten Schwecke
Torsten Schwecke
LKLake Ee Khaw
Lake Ee Khaw
PLPeter F. Leadlay
Peter F. Leadlay

1 February 1996 in Gene
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Journal Article
Closed access
Jesús F. AparicioJesús F. Aparicio
Jesús F. Aparicio
IMIstvan Molnar
Istvan Molnar
TSTorsten Schwecke
Torsten Schwecke
AKAriane König
Ariane König
SHStephen F. Haydock
Stephen F. Haydock
PLPeter F. Leadlay
Peter F. Leadlay

21 January 1994 in Science
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Journal Article
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AMAndrew F. A. Marsden
Andrew F. A. Marsden
PCPatrick Caffrey
Patrick Caffrey
Jesús F. AparicioJesús F. Aparicio
Jesús F. Aparicio
MLMark S. Loughran
Mark S. Loughran
JSJames Staunton
James Staunton
MLM S Loughran
M S Loughran
During assembly of complex polyketide antibiotics like erythromycin A, molecular recognition by the multienzyme polyketide synthase controls the stereochemical outcome as each successive methylmalonyl-coenzyme A (CoA) extender unit is added. Acylation of the purified erythromycin-producing polyketide synthase has shown that all six acyltransferase domains have identical stereospecificity for their normal substrate, (2S)-methylmalonyl-CoA. In contrast, the configuration of the methyl-branched centers in the product, that are derived from (2S)-methylmalonyl-CoA, is different. Stereoselection during the chain building process must, therefore, involve additional epimerization steps.

1 November 2000 in Chemistry & Biology
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Journal Article
Closed access
Jesús F. AparicioJesús F. Aparicio
Jesús F. Aparicio
RFRoberto Fouces
Roberto Fouces
MMMarta Mendes
Marta Mendes
NONoemı́ Olivera
Noemı́ Olivera
JMJuan F Martı́n
Juan F Martı́n

18 December 2002 in Applied Microbiology and Biotechnology
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Journal Article
Closed access
PDF file
Jesús F. AparicioJesús F. Aparicio
Jesús F. Aparicio
PCP. Caffrey
P. Caffrey
Jose GilJose Gil
Jose Gil
SZSergey Zotchev
Sergey Zotchev