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  Determinants of enzymatic specificity in the Cys-Met-metabolism PLP-dependent enzyme family: Crystal structure of cystathionine γ-lyase from yeast and intrafamiliar structure comparison

Messerschmidt, A., Worbs, M., Steegborn, C., Wahl, M. C., Huber, R., Laber, B., et al. (2003). Determinants of enzymatic specificity in the Cys-Met-metabolism PLP-dependent enzyme family: Crystal structure of cystathionine γ-lyase from yeast and intrafamiliar structure comparison. Biological Chemistry, 384(3), 373-386.

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Genre: Journal Article
Alternative Title : Biol. Chem.

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 Creators:
Messerschmidt, A.1, Author              
Worbs, M.1, Author              
Steegborn, C.1, Author              
Wahl, M. C.2, Author              
Huber, R.2, Author              
Laber, B., Author
Clausen, T.2, Author              
Affiliations:
1External Organizations, ou_persistent22              
2Huber, Robert / Structure Research, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565155              

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Free keywords: cystathionine gamma-lyase; cysteine methionine metabolism; crystal structure; pyridoxal-5 '-phosphate; substrate specificity
 Abstract: The crystal structure of cystathionine [gamma]lyase (CGL) from yeast has been solved by molecular replacement at a resolution of 2.6 a. The molecule consists of 393 amino acid residues and one PLP moiety and is arranged in the crystal as a tetramer with D2 symmetry as in other related enzymes of the CysMetmetabolism PLPdependent family like cystathionine [beta]lyase (CBL). A structure comparison with other family members revealed surprising insights into the tuning of enzymatic specificity between the different family members. CGLs from yeast or human are virtually identical at their active sites to cystathionine [gamma]synthase (CGS) from E. coli. Both CGLs and bacterial CGSs exhibit [gamma]synthase and [gamma]lyase activities depending on their position in the metabolic pathway and the available substrates. This group of enzymes has a glutamate (E333 in yeast CGL) which binds to the distal group of cystathionine (CTT) or the amino group of cysteine. Plant CGSs use homoserine phosphate instead of Osuccinylhomoserine as one substrate. This is reflected by a partially different active site structure in plant CGSs. In CGL and CBL the pseudosymmetric substrate must dock at the active site in different orientations, with S in [gamma]position (CBL) or in [delta]position (CGL). The conserved glutamate steers the substrate as seen in other CGLs. In CBLs this position is occupied by either tyrosine or hydrophobic residues directing binding of CTT such that S is in the in [gamma]position. In methionine [gamma]lyase a hydrophic patch operates as recognition site for the methyl group of the methionine substrate.

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Language(s): eng - English
 Dates: 2003-03
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 41530
ISI: 000181664600006
 Degree: -

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Title: Biological Chemistry
  Alternative Title : Biol. Chem.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 384 (3) Sequence Number: - Start / End Page: 373 - 386 Identifier: ISSN: 1431-6730