Hydrolysis and transfer reactions catalyzed by gamma-glutamyl transpeptidase; evidence for separate substrate sites and for high affinity of L-cystine
about
Human GGT2 does not autocleave into a functional enzyme: A cautionary tale for interpretation of microarray data on redox signalingNovel insights into eukaryotic γ-glutamyltranspeptidase 1 from the crystal structure of the glutamate-bound human enzymeTranslocation of intracellular glutathione to membrane-bound gamma-glutamyl transpeptidase as a discrete step in the gamma-glutamyl cycle: glutathionuria after inhibition of transpeptidaseGamma-glutamyl compounds: substrate specificity of gamma-glutamyl transpeptidase enzymesStructural, functional, and clinical aspects of gamma-glutamyltransferase.The importance and regulation of hepatic glutathione.Involvement of Ser-451 and Ser-452 in the catalysis of human gamma-glutamyl transpeptidase.Human gamma-glutamyl transpeptidase mutants involving conserved aspartate residues and the unique cysteine residue of the light subunit.Affinity labeling of gamma-glutamyl transpeptidase and location of the gamma-glutamyl binding site on the light subunit.Mechanism of translational control by hemin in reticulocyte lysatesSelective inhibition of gamma-glutamyl-cycle enzymes by substrate analogs.Autocatalytic cleavage of human gamma-glutamyl transpeptidase is highly dependent on N-glycosylation at asparagine 95.Formation of gamma-glutamycyst(e)ine in vivo is catalyzed by gamma-glutamyl transpeptidase.Intrahepatic transport and utilization of biliary glutathione and its metabolites.Inhibition of gamma-glutamyl transpeptidase and induction of glutathionuria by gamma-glutamyl amino acidsSerine-borate complex as a transition-state inhibitor of gamma-glutamyl transpeptidase.Divergent effects of compounds on the hydrolysis and transpeptidation reactions of γ-glutamyl transpeptidase.Inhibition of human γ-glutamyl transpeptidase: development of more potent, physiologically relevant, uncompetitive inhibitors.Transport and direct utilization of gamma-glutamylcyst(e)ine for glutathione synthesis.gamma-Glutamyltranspeptidase-catalysed acyl-transfer to the added acceptor does not proceed via the ping-pong mechanism.Gamma-glutamyl transpeptidase activity in brain microvessels exhibits regional heterogeneity.GGT dimers hydrolyse GSHSubunit separation in reversed micelle system reveals the existence of active centers both on light and heavy gamma-glutamyltransferase subunits.
P2860
Q24293100-8A5D8757-0621-46F7-8415-3094433FAB77Q24336791-E4BCA5E2-07BE-4FA3-8156-02EC35921B0BQ28646487-B4941545-D17C-414F-A489-C11C671879A4Q34174116-93DB1234-AF7F-4EA2-A792-9BAD732D8025Q34246012-396AF63A-A0F2-44FF-AAD8-BF03E1636D65Q34284969-9260FC28-5B80-4345-B789-01A62AA3FFA1Q34305191-55775788-9BA5-4D37-B299-AED2465D46C2Q34311377-88206802-4993-41BB-B518-A42DCB8AB647Q35009214-B5811D33-B90B-49C2-84B4-A019771DADD9Q35043577-E64132F3-6F18-41A9-9CF0-8E147E3A00F0Q35043606-3C0A40E1-3C19-41A1-802C-EA7F6A7E4AD1Q35309561-AE8B672A-3166-4FC6-8AC4-8E84CBAF0420Q35359325-6F6A0819-41F8-4CD9-ADD0-3E05306D5CBFQ35592101-94BE5497-0261-457B-B38A-E5F68C044B10Q35616248-5628D94F-C8BF-47C4-9691-07EFB5CD5C14Q35994048-4BC0E610-B6EC-4D8F-A773-3F55BC2DEF5DQ36123399-5EEBC04B-57C5-4F29-AE22-6E1DEDEF8F23Q37332744-A643221C-2F18-4F9A-B6A6-73CD241ECEB7Q37602746-8C8FD979-095F-4BF6-AA8C-16BBB4EA0051Q42829985-6F8E0DAE-3581-470D-8F4C-083630A6DF81Q48523319-452E584E-0076-4F7B-AA89-627122D036F3Q50295406-2A0DF5FB-1401-4D1A-BDCD-14AF9A5AD4E8Q54071492-FFBE5B4E-D5E4-4577-BFC0-C6AE3729B037
P2860
Hydrolysis and transfer reactions catalyzed by gamma-glutamyl transpeptidase; evidence for separate substrate sites and for high affinity of L-cystine
description
1976 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
1976 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 1976
@ast
im Juli 1976 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 1976/07/12)
@sk
vědecký článek publikovaný v roce 1976
@cs
wetenschappelijk artikel (gepubliceerd op 1976/07/12)
@nl
наукова стаття, опублікована в липні 1976
@uk
مقالة علمية (نشرت في 12-7-1976)
@ar
name
Hydrolysis and transfer reacti ...... for high affinity of L-cystine
@ast
Hydrolysis and transfer reacti ...... for high affinity of L-cystine
@en
Hydrolysis and transfer reacti ...... for high affinity of L-cystine
@nl
type
label
Hydrolysis and transfer reacti ...... for high affinity of L-cystine
@ast
Hydrolysis and transfer reacti ...... for high affinity of L-cystine
@en
Hydrolysis and transfer reacti ...... for high affinity of L-cystine
@nl
prefLabel
Hydrolysis and transfer reacti ...... for high affinity of L-cystine
@ast
Hydrolysis and transfer reacti ...... for high affinity of L-cystine
@en
Hydrolysis and transfer reacti ...... for high affinity of L-cystine
@nl
P1476
Hydrolysis and transfer reacti ...... for high affinity of L-cystine
@en
P2093
A. Meister
G. A. Thompson
P356
10.1016/0006-291X(76)90245-X
P407
P577
1976-07-12T00:00:00Z