Disulfide Bridges in the Mesophilic Triosephosphate Isomerase from Giardia lamblia Are Related to Oligomerization and Activity (Record no. 43022)

MARC details
000 -LEADER
fixed length control field 02654nam a2200325Ia 4500
003 - CONTROL NUMBER IDENTIFIER
control field MX-MdCICY
005 - DATE AND TIME OF LATEST TRANSACTION
control field 20250625124725.0
040 ## - CATALOGING SOURCE
Transcribing agency CICY
090 ## - LOCALLY ASSIGNED LC-TYPE CALL NUMBER (OCLC); LOCAL CALL NUMBER (RLIN)
Classification number (OCLC) (R) ; Classification number, CALL (RLIN) (NR) B-8720
008 - FIXED-LENGTH DATA ELEMENTS--GENERAL INFORMATION
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245 10 - TITLE STATEMENT
Title Disulfide Bridges in the Mesophilic Triosephosphate Isomerase from Giardia lamblia Are Related to Oligomerization and Activity
490 0# - SERIES STATEMENT
Volume/sequential designation J. Mol. Biol., 365(3), p.752-763, 2007
520 3# - SUMMARY, ETC.
Summary, etc. Triosephosphate isomerase from the mesophile Giardia lamblia (GlTIM)is the only known TIM with natural disulfide bridges. We previously found that oxidized and reduced thiol states of GlTIM are involved in the interconversion between native dimers and higher oligomeric species, and in the regulation of enzymatic activity. Here, we found that trophozoites and cysts have different oligomeric species of GlTIM and complexes of GlTIM with other proteins. Our data indicate that the internal milieu of G. lamblia is favorable for the formation of disulfide bonds. Enzyme mutants of the three most solvent exposed Cys of GlTIM (C202A, C222A, and C228A)were prepared to ascertain their contribution to oligomerization and activity. The data show that the establishment of a disulfide bridge between two C202 of two dimeric GlTIMs accounts for multimerization. In addition, we found that the establishment of an intramonomeric disulfide bond between C222 and C228 abolishes catalysis. Multimerization and inactivation are both reversed by reducing conditions. The 3D structure of the C202A GlTIMwas solved at 2.1 Å resolution, showing that the environment of the C202 is prone to hydrophobic interactions. Molecular dynamics of an in silico model of GlTIM when the intramonomeric disulfide bond is formed, showed that S216 is displaced 4.6 Å from its original position, causing loss of hydrogen bonds with residues of the active-site loop. This suggests that this change perturb the conformational state that aligns the catalytic center with the substrate, inducing enzyme inactivation.
650 14 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name entry element GIARDIA
650 14 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name entry element TRIOSEPHOSPHATE
650 14 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name entry element DISULFIDE BONDS
650 14 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name entry element GLYCOLYSIS
650 14 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name entry element DINAMIC MOLECULAR
700 12 - ADDED ENTRY--PERSONAL NAME
Personal name Reyes-Vivas, H.
700 12 - ADDED ENTRY--PERSONAL NAME
Personal name Diaz, A.
700 12 - ADDED ENTRY--PERSONAL NAME
Personal name Peon, J.
700 12 - ADDED ENTRY--PERSONAL NAME
Personal name Mendoza-Hernandez, G.
700 12 - ADDED ENTRY--PERSONAL NAME
Personal name Hernandez-Alcantara, G.
700 12 - ADDED ENTRY--PERSONAL NAME
Personal name De La Mora-De La Mora, I.
700 12 - ADDED ENTRY--PERSONAL NAME
Personal name Enriquez-Flores, S.
700 12 - ADDED ENTRY--PERSONAL NAME
Personal name Enriquez-Flores, S.
700 12 - ADDED ENTRY--PERSONAL NAME
Personal name Lopez-Velazquez, G.
856 40 - ELECTRONIC LOCATION AND ACCESS
Uniform Resource Identifier <a href="https://drive.google.com/file/d/1sQnl0ZZsV-JamvNvnXFz_SVxpKzIwEZ7/view?usp=drivesdk">https://drive.google.com/file/d/1sQnl0ZZsV-JamvNvnXFz_SVxpKzIwEZ7/view?usp=drivesdk</a>
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942 ## - ADDED ENTRY ELEMENTS (KOHA)
Source of classification or shelving scheme Clasificación local
Koha item type Documentos solicitados
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  Clasificación local     Ref1 CICY CICY Documento préstamo interbibliotecario 25.06.2025   B-8720 25.06.2025 25.06.2025 Documentos solicitados