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Information on EC 3.1.2.6 - hydroxyacylglutathione hydrolase and Organism(s) Leishmania infantum and UniProt Accession Q2PYN0

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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.2 Thioester hydrolases
                3.1.2.6 hydroxyacylglutathione hydrolase
IUBMB Comments
Also hydrolyses S-acetoacetylglutathione, but more slowly.
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This record set is specific for:
Leishmania infantum
UNIPROT: Q2PYN0
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Word Map
The taxonomic range for the selected organisms is: Leishmania infantum
The enzyme appears in selected viruses and cellular organisms
Synonyms
glyoxalase ii, glyoxalase 2, gly ii, glyii, glxii, glx2-2, gloii, hydroxyacylglutathione hydrolase, cgloii, glo ii, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydroxyacylglutathione hydrolase
-
acetoacetylglutathione hydrolase
-
-
-
-
Germ cell specific protein
-
-
-
-
GLO II
-
-
-
-
glyoxalase II
-
-
-
-
hydrolase, acetoacetylglutathione
-
-
-
-
hydrolase, hydroxyacylglutathione
-
-
-
-
Round spermatid protein RSP29
-
-
-
-
S-2-hydroxylacylglutathione hydrolase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of thioester
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -
SYSTEMATIC NAME
IUBMB Comments
S-(2-hydroxyacyl)glutathione hydrolase
Also hydrolyses S-acetoacetylglutathione, but more slowly.
CAS REGISTRY NUMBER
COMMENTARY hide
9025-90-5
-
9025-92-7
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-lactoyltrypanothione + H2O
D-lactate + trypanothione
show the reaction diagram
-
-
-
?
S-D-lactoylglutathione + H2O
D-lactate + glutathione
show the reaction diagram
used by mutant Y291R/C294K
-
-
?
S-D-lactoyltrypanothione + H2O
D-lactate + trypanothione
show the reaction diagram
additionally S-D-lactoylglutathione used by mutant Y291R/C294K
-
-
?
mono-(lactoyl)trypanothione + H2O
D-lactate + trypanothione
show the reaction diagram
-
-
-
-
ir
trypanothione hemithioacetal + H2O
?
show the reaction diagram
-
-
-
-
ir
additional information
?
-
-
no substrate: S-lactoylglutathione
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.439
S-D-lactoylglutathione
Y291R/C294K mutant protein, pH not specified in the publication, temperature not specified in the publication
0.092 - 0.15
S-D-lactoyltrypanothione
0.098
mono-(lactoyl)trypanothione
-
pH 6.8, 30°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
918
S-D-lactoylglutathione
Y291R/C294K mutant protein, pH not specified in the publication, temperature not specified in the publication
16 - 241
S-D-lactoyltrypanothione
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2090
S-D-lactoylglutathione
Y291R/C294K mutant protein, pH not specified in the publication, temperature not specified in the publication
180 - 1600
S-D-lactoyltrypanothione
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q2PYN0_LEIIN
295
0
32573
TrEMBL
Mitochondrion (Reliability: 5)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
32000
x * 32000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 32000, SDS-PAGE
monomer
295 amino acid residues
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystals belong to space group C222(1), and diffract beyond 2.15 A, unit-cell parameters a = 65.6, b = 88.3, c = 85.2 A. Hanging-drop vapour-diffusion method using the crystallization tools
two glyoxalase II structures are solved. One with a bound spermidine molecule (1.8 A) and the other with D-lactate at the active site (1.9 A). The second structure is obtained by crystal soaking with the enzyme substrate (S)-D-lactoyltrypanothione. Hanging drop method
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Y291R/C294K
substrate specificity changed
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
protein stability increased in the presence of 10 mM MnCl2 and 5% PEG (PEG4000, PEG400, PEG8000)
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
immobilized metal ion affinity chromatography (Co2+), gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloned and expressed in Escherichia coli BL21 Codon Plus cells. The protein is expressed with an N-terminal His-tag fusion
His-tagged version of mutant protein expressed in Escherichia coli BL21-Codon plus
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sousa Silva, M.; Ferreira, A.E.N.; Tomas, A.M.; Cordeiro, C.; Freire, A.P.
Quantitative assessment of the glyoxalase pathway in Leishmania infantum as a therapeutic target by modelling and computer simulation
FEBS J.
272
2388-2398
2005
Leishmania infantum
Manually annotated by BRENDA team
Trincao, J.; Sousa Silva, M.; Barata, L.; Bonifacio, C.; Carvalho, S.; Tomas, A.M.; Ferreira, A.E.; Cordeiro, C.; Ponces Freire, A.; Romao, M.J.
Purification, crystallization and preliminary X-ray diffraction analysis of the glyoxalase II from Leishmania infantum
Acta Crystallogr. Sect. F
62
805-807
2006
Leishmania infantum (Q2PYN0), Leishmania infantum
Manually annotated by BRENDA team
Silva, M.S.; Barata, L.; Ferreira, A.E.; Romao, S.; Tomas, A.M.; Freire, A.P.; Cordeiro, C.
Catalysis and structural properties of Leishmania infantum glyoxalase II: trypanothione specificity and phylogeny
Biochemistry
47
195-204
2008
Leishmania infantum (Q2PYN0), Leishmania infantum
Manually annotated by BRENDA team
Barata, L.; Silva, M.S.; Schuldt, L.; Ferreira, A.E.; Gomes, R.A.; Tomas, A.M.; Weiss, M.S.; Freire, A.P.; Cordeiro, C.
Enlightening the molecular basis of trypanothione specificity in trypanosomatids: Mutagenesis of Leishmania infantum glyoxalase II
Exp. Parasitol.
129
402-408
2011
Leishmania infantum (Q2PYN0), Leishmania infantum
Manually annotated by BRENDA team