Pretražite po imenu i prezimenu autora, mentora, urednika, prevoditelja

Napredna pretraga

Pregled bibliografske jedinice broj: 333666

Insights into the catalytic mechanism of tyrosine phenol-lyase from X-ray structures of quinonoid intermediates


Milić, Dalibor; Demidkina, Tatyana V.; Faleev, Nicolai G.; Matković-Čalogović, Dubravka; Antson, Alfred A.
Insights into the catalytic mechanism of tyrosine phenol-lyase from X-ray structures of quinonoid intermediates // Journal of Biological Chemistry, 283 (2008), 43; 29206-29214 (međunarodna recenzija, članak, znanstveni)


CROSBI ID: 333666 Za ispravke kontaktirajte CROSBI podršku putem web obrasca

Naslov
Insights into the catalytic mechanism of tyrosine phenol-lyase from X-ray structures of quinonoid intermediates

Autori
Milić, Dalibor ; Demidkina, Tatyana V. ; Faleev, Nicolai G. ; Matković-Čalogović, Dubravka ; Antson, Alfred A.

Izvornik
Journal of Biological Chemistry (0021-9258) 283 (2008), 43; 29206-29214

Vrsta, podvrsta i kategorija rada
Radovi u časopisima, članak, znanstveni

Ključne riječi
tyrosine phenol-lyase; beta-elimination; quinonoid intermediate; alanine racemization; pyridoxal 5'-phosphate; structural enzymology; X-ray structural analysis

Sažetak
Amino acid transformations catalyzed by a number of PLP-dependent enzymes involve abstraction of the Calpha proton from an external aldimine formed between a substrate and the cofactor leading to the formation of a quinonoid intermediate. In spite of the key role played by the quinonoid intermediates in the catalysis by PLP-dependent enzymes, limited accurate information is available about their structures. We trapped the quinonoid intermediates of Citrobacter freundii tyrosine phenol-lyase with L-alanine and L-methionine in the crystalline state and determined their structures at 1.9 Å and 1.95 Å resolution, respectively, by cryo-crystallography. The data reveal a network of protein-PLP-substrate interactions that stabilize the planar geometry of the quinonoid intermediate. In both structures the protein subunits are found in two conformations – open and closed, uncovering the mechanism by which binding of the substrate and restructuring of the active site during its closure protect the quinonoid intermediate from the solvent and bring catalytically important residues into positions suitable for the abstraction of phenol during the beta -elimination of L-tyrosine. In addition, the structural data indicate a mechanism for alanine racemization involving two bases, Lys257 and a water molecule. These two bases are connected by a hydrogen bonding system allowing internal transfer of the Calpha proton.

Izvorni jezik
Engleski

Znanstvena područja
Kemija



POVEZANOST RADA


Projekti:
119-1193079-1084 - Strukturno istraživanje bioloških makromolekula metodom rentgenske difrakcije (Matković-Čalogović, Dubravka, MZOS ) ( POIROT)

Ustanove:
Prirodoslovno-matematički fakultet, Zagreb

Citiraj ovu publikaciju:

Milić, Dalibor; Demidkina, Tatyana V.; Faleev, Nicolai G.; Matković-Čalogović, Dubravka; Antson, Alfred A.
Insights into the catalytic mechanism of tyrosine phenol-lyase from X-ray structures of quinonoid intermediates // Journal of Biological Chemistry, 283 (2008), 43; 29206-29214 (međunarodna recenzija, članak, znanstveni)
Milić, D., Demidkina, T., Faleev, N., Matković-Čalogović, D. & Antson, A. (2008) Insights into the catalytic mechanism of tyrosine phenol-lyase from X-ray structures of quinonoid intermediates. Journal of Biological Chemistry, 283 (43), 29206-29214.
@article{article, author = {Mili\'{c}, Dalibor and Demidkina, Tatyana V. and Faleev, Nicolai G. and Matkovi\'{c}-\v{C}alogovi\'{c}, Dubravka and Antson, Alfred A.}, year = {2008}, pages = {29206-29214}, keywords = {tyrosine phenol-lyase, beta-elimination, quinonoid intermediate, alanine racemization, pyridoxal 5'-phosphate, structural enzymology, X-ray structural analysis}, journal = {Journal of Biological Chemistry}, volume = {283}, number = {43}, issn = {0021-9258}, title = {Insights into the catalytic mechanism of tyrosine phenol-lyase from X-ray structures of quinonoid intermediates}, keyword = {tyrosine phenol-lyase, beta-elimination, quinonoid intermediate, alanine racemization, pyridoxal 5'-phosphate, structural enzymology, X-ray structural analysis} }
@article{article, author = {Mili\'{c}, Dalibor and Demidkina, Tatyana V. and Faleev, Nicolai G. and Matkovi\'{c}-\v{C}alogovi\'{c}, Dubravka and Antson, Alfred A.}, year = {2008}, pages = {29206-29214}, keywords = {tyrosine phenol-lyase, beta-elimination, quinonoid intermediate, alanine racemization, pyridoxal 5'-phosphate, structural enzymology, X-ray structural analysis}, journal = {Journal of Biological Chemistry}, volume = {283}, number = {43}, issn = {0021-9258}, title = {Insights into the catalytic mechanism of tyrosine phenol-lyase from X-ray structures of quinonoid intermediates}, keyword = {tyrosine phenol-lyase, beta-elimination, quinonoid intermediate, alanine racemization, pyridoxal 5'-phosphate, structural enzymology, X-ray structural analysis} }

Časopis indeksira:


  • Current Contents Connect (CCC)
  • Web of Science Core Collection (WoSCC)
    • Science Citation Index Expanded (SCI-EXP)
    • SCI-EXP, SSCI i/ili A&HCI
  • Scopus
  • MEDLINE





Contrast
Increase Font
Decrease Font
Dyslexic Font