Document Detail


GABA production by glutamic acid decarboxylase is regulated by a dynamic catalytic loop.
MedLine Citation:
PMID:  17384644     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Gamma-aminobutyric acid (GABA) is synthesized by two isoforms of the pyridoxal 5'-phosphate-dependent enzyme glutamic acid decarboxylase (GAD65 and GAD67). GAD67 is constitutively active and is responsible for basal GABA production. In contrast, GAD65, an autoantigen in type I diabetes, is transiently activated in response to the demand for extra GABA in neurotransmission, and cycles between an active holo form and an inactive apo form. We have determined the crystal structures of N-terminal truncations of both GAD isoforms. The structure of GAD67 shows a tethered loop covering the active site, providing a catalytic environment that sustains GABA production. In contrast, the same catalytic loop is inherently mobile in GAD65. Kinetic studies suggest that mobility in the catalytic loop promotes a side reaction that results in cofactor release and GAD65 autoinactivation. These data reveal the molecular basis for regulation of GABA homeostasis.
Authors:
Gustavo Fenalti; Ruby H P Law; Ashley M Buckle; Christopher Langendorf; Kellie Tuck; Carlos J Rosado; Noel G Faux; Khalid Mahmood; Christiane S Hampe; J Paul Banga; Matthew Wilce; Jason Schmidberger; Jamie Rossjohn; Ossama El-Kabbani; Robert N Pike; A Ian Smith; Ian R Mackay; Merrill J Rowley; James C Whisstock
Related Documents :
2548104 - Entropy as a factor in the binding of gamma-aminobutyric acid and nipecotic acid to the...
9770274 - Purification and characterization of cystathionine gamma-lyase from lactobacillus ferme...
6728924 - Age dependence of the gamma-carboxyglutamic acid containing proteins.
16193534 - A review of evidence leading to the prediction that 1,4-butanediol is not a carcinogen.
15630164 - Dual mechanisms for telomerase inhibition in dld-1 human colorectal adenocarcinoma cell...
6847664 - Acyltransferase-catalyzed transfer of arachidonic acid to lysophospholipids in rat panc...
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2007-03-25
Journal Detail:
Title:  Nature structural & molecular biology     Volume:  14     ISSN:  1545-9993     ISO Abbreviation:  Nat. Struct. Mol. Biol.     Publication Date:  2007 Apr 
Date Detail:
Created Date:  2007-04-05     Completed Date:  2007-05-30     Revised Date:  2007-10-24    
Medline Journal Info:
Nlm Unique ID:  101186374     Medline TA:  Nat Struct Mol Biol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  280-6     Citation Subset:  IM    
Affiliation:
Department of Biochemistry and Molecular Biology, Monash University, Clayton, Melbourne, VIC 3800, Australia.
Data Bank Information
Bank Name/Acc. No.:
PDB/2OKJ;  2OKK
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Autoantigens / immunology
Binding Sites / drug effects
Catalysis / drug effects
Crystallography, X-Ray
Dimerization
Enzyme Activation / drug effects
Glutamate Decarboxylase / chemistry,  immunology,  metabolism*
Glutamic Acid / pharmacology
Humans
Isoenzymes / chemistry,  immunology,  metabolism*
Models, Molecular
Molecular Sequence Data
Protein Structure, Secondary / drug effects
gamma-Aminobutyric Acid / biosynthesis*
Chemical
Reg. No./Substance:
0/Autoantigens; 0/Isoenzymes; 56-12-2/gamma-Aminobutyric Acid; 56-86-0/Glutamic Acid; EC 4.1.1.15/Glutamate Decarboxylase; EC 4.1.1.15/glutamate decarboxylase 1; EC 4.1.1.15/glutamate decarboxylase 2

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Ultramicroscopy: three-dimensional visualization of neuronal networks in the whole mouse brain.
Next Document:  A riboswitch selective for the queuosine precursor preQ1 contains an unusually small aptamer domain.