Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 3.1.2.6 - hydroxyacylglutathione hydrolase and Organism(s) Plasmodium falciparum

for references in articles please use BRENDA:EC3.1.2.6
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Plasmodium falciparum
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Plasmodium falciparum
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
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
S-D-lactoylglutathione + H2O
D-lactate + glutathione
show the reaction diagram
-
substrate is predominantly bound via ionic interactions with the conserved residues Arg257 and Lys260. Correct substrate binding is a pH- and salt-dependent rate-limiting step for catalysis. Bi Bi mechanism with the direct involvement of a hydroxide ion as a second substrate
-
-
?
S-lactoylglutathione + H2O
D-lactate + glutathione
show the reaction diagram
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
0.26 mol per mol of enzyme
Zinc
-
recombinant GloII is zinc-dependent
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
D-lactate
-
competitive inhibition
glutathione
-
non-competitive inhibition. Is a stronger inhibitor than the ethyl ester of glutathione. Theorell-Chance Bi Bi mechanism with glutathione as the second product
glutathione ethyl ester
-
carboxylate group of the glycine-moiety is modified, non-competitive inhibition
S-(N-hydroxy-N-bromophenylcarbamoyl)glutathione
50% inhibition at 0.0016 mM; 50% inhibition at 0.02 mM
S-(N-hydroxy-N-chlorophenylcarbamoyl)glutathione
50% inhibition at 0.002 mM; 50% inhibition at 0.03 mM
S-(N-hydroxy-N-phenylcarbamoyl)glutathione
50% inhibition at 0.006 mM; 50% inhibition at 0.185 mM
S-(p-azidophenacyl)glutathione
-
S-hexylglutathione
-
S-propylglutathione
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Zn2+
2fold activation
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.114 - 5.782
S-D-lactoylglutathione
0.1 - 0.463
S-Lactoylglutathione
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
60 - 375
S-D-lactoylglutathione
64.3 - 119.6
S-Lactoylglutathione
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
11 - 3300
S-D-lactoylglutathione
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000031
D-lactate
-
inhibitor binding to the free enzyme, at 25°C, pH 6.8
3.5 - 13
glutathione
14 - 49
glutathione ethyl ester
0.0005 - 0.03
S-(N-hydroxy-N-bromophenylcarbamoyl)glutathione
0.0007 - 0.05
S-(N-hydroxy-N-chlorophenylcarbamoyl)glutathione
0.006
S-(N-hydroxy-N-phenylcarbamoyl)glutathione
25°C
1.3
S-(p-azidophenacyl)glutathione
25°C
1.5
S-hexylglutathione
25°C
1.9
S-propylglutathione
25°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.25
calculated, N-terminally truncated active form
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q5J7B5_PLAFA
263
0
30528
TrEMBL
other Location (Reliability: 3)
Q71KM2_PLAFA
322
0
38414
TrEMBL
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30500
x * 30500, calculated
31800
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structural models based on crystallization data
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K260D
-
unaltered metal binding sites and is correctly folded, but reduced activity. Has a much lower catalytic efficiency, but the spectrum is very similar to the wild-type enzyme. Has a highly simplified bell-shaped pH-activity profile with a maximum at pH 6.7 in contrast to the broad asymmetric profiles of the other enzymes
K260Q
-
unaltered metal binding sites and is correctly folded, but reduced activity
R154K
-
unaltered metal binding sites and is correctly folded, but reduced activity
R154M
-
unaltered metal binding sites and is correctly folded, but reduced activity
R257D
-
unaltered metal binding sites and is correctly folded, but reduced activity
R257Q
-
unaltered metal binding sites and is correctly folded, but reduced activity
Y185F
2.5fold increase in Km-value
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
wild-type and glutathione-binding site mutants, by sonication, centrifugation and on Ni-NTA column
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
into pQE30 vector. N-terminally MRGS(H)6GS-tagged GloII wild-type and mutant enzymes transformed into Escherichia coli competent XL1-Blue cells or EZ cells
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Akoachere, M.; Iozef, R.; Rahlfs, S.; Deponte, M.; Mannervik, B.; Creighton, D.J.; Schirmer, H.; Becker, K.
Characterization of the glyoxalases of the malarial parasite Plasmodium falciparum and comparison with their human counterparts
Biol. Chem.
386
41-52
2005
Plasmodium falciparum (Q5J7B5), Plasmodium falciparum (Q71KM2), Plasmodium falciparum
Manually annotated by BRENDA team
Urscher, M.; Deponte, M.
Plasmodium falciparum glyoxalase II: Theorell-Chance product inhibition patterns, rate-limiting substrate binding via Arg(257)/Lys(260), and unmasking of acid-base catalysis
Biol. Chem.
390
1171-1183
2009
Plasmodium falciparum
Manually annotated by BRENDA team