4.4.1.5: lactoylglutathione lyase

This is an abbreviated version!
For detailed information about lactoylglutathione lyase, go to the full flat file.

Reaction

Synonyms

aldoketomutase, CLO GlxI, Glb33, GLI, GLO I, GLO-1, GLO-I, Glo1, GloA, GloA1, GloA2, GloA3, GloI, Glx I, Glx-I, Glx1, GLXI, Gly I, gly-I, GLY1, glyoxalase 1, glyoxalase I, glyoxalase-1, glyoxalase-I, glyoxylase I, GmGlyox I, ketone-aldehyde mutase, lactoylglutathione lyase, lactoylglutathione methylglyoxal lyase, LGL, lyase, lactoylglutathione, methylglyoxalase, methylglyoxylase, OsGLYI-11.2, PfGlx I, rhGLO I, S-D-lactoylglutathione methylglyoxal lyase, S-D-lactoylglutathione methylglyoxal lyase (isomerizing), S-D-lactoylglutathione:methylglyoxal lyase, SpGlo1, STM3117, YaiA

ECTree

     4 Lyases

         4.4 Carbon-sulfur lyases

             4.4.1 Carbon-sulfur lyases (only sub-subclass identified to date)

                4.4.1.5 lactoylglutathione lyase

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Results	in table
43	Activating Compound
16665	AA Sequence
23	Application
1	CAS Registry Number
55	Cloned(Commentary)
35	Cofactor
15	Crystallization (Commentary)
1045	Disease/ Diagnostics
25	Expression
41	General Information
1	General Stability
42	IC50 Value
326	Inhibitors
2	kcat/KM [mM/s]
63	Ki Value [mM]
143	KM Value [mM]
60	Localization
250	Metals/Ions
105	Molecular Weight [Da]
121	Natural Substrates/ Products (Substrates)
295	Organism
6	Pathway
75	PDB ID
27	pH Optimum
4	pH Range
2	pH Stability
17	pI Value
6	Posttranslational Modification
34	Protein Variants
62	Purification (Commentary)
17	Reaction
20	Reaction Type
269	Reference
186	Source Tissue
92	Specific Activity [micromol/min/mg]
5	Storage Stability
354	Substrates and Products (Substrate)
76	Subunits
337	Synonyms
1	Systematic Name
14	Temperature Optimum [°C]
2	Temperature Stability [°C]
56	Turnover Number [1/s]

Posttranslational Modification

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Posttranslational Modification on EC 4.4.1.5 - lactoylglutathione lyase

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POSTTRANSLATIONAL MODIFICATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

glutathionylation

Homo sapiens

Q04760

glutathionylation strongly inhibits Glo1 activity in vitro

710387

glycoprotein

Starmerella magnoliae

D6QLX5

sequence contains two potential N-glycosylation sites

715887

phosphoprotein

2 entries

side-chain modification

Homo sapiens

-

posttranslational modification of Glo1 by oxidized glutathione (GSSG) and nitrosylation strongly inhibits Glo1 activity

729175

additional information

Homo sapiens

-

NO-mediated modification can suppress NF-kappaB-dependent reporter gene expression, less powerful in suppression than phosphorylation of GLO1

694142

phosphoprotein

Homo sapiens

-

phosphorylated by calcium, calmodulin-dependent protein kinase II at Thr106 revealed by site-directed mutagenesis of several serine and threonine residues. Mutagenesis of Thr106 to Ala completely abolishes the phosphorylation. GLO1 is only phosphorylated when it is co-expressed with the catalytic subunit of calcium, calmodulin-dependent protein kinase II but no phosphorylation is observed when GLO1 is co-expressed with protein kinase A. Phosphorylation can suppress NF-kappaB-dependent reporter gene expression, more powerful in suppression than NO-mediated modification of GLO1. Tumor necrosis factor induces phosphorylation of GLO1 on Thr106

694142

phosphoprotein

Homo sapiens

-

the enzyme is susceptible to post-translational modifications, in particular phosphorylation in response to TNFalpha, a key mediator of inflammation

729175