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Information on EC 3.1.1.17 - gluconolactonase and Organism(s) Mus musculus and UniProt Accession Q64374

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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.1 Carboxylic-ester hydrolases
                3.1.1.17 gluconolactonase
IUBMB Comments
Acts on a wide range of hexose-1,5-lactones. The hydrolysis of L-gulono-1,5-lactone was previously listed separately.
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This record set is specific for:
Mus musculus
UNIPROT: Q64374
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Word Map
The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
regucalcin, lactonase, smp30, senescence marker protein-30, smp30/gnl, human paraoxonase 1, senescence marker protein 30, gluconolactonase, smp-30, aldonolactonase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
regucalcin
-
senescence marker protein-30
-
aldonolactonase
-
-
-
-
D-glucono-delta-lacton-hydrolase
-
-
-
-
D-glucono-delta-lactone lactonohydrolase
-
-
-
-
GL
-
-
-
-
glucono-delta-lactonase
-
-
-
-
gulonolactonase
-
-
-
-
lactonase
-
-
-
-
senescence marker protein-30
-
-
senescence marker protein-30/gluconolactonase
-
-
SMP30/GNL
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of carboxylic ester
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
D-glucono-1,5-lactone lactonohydrolase
Acts on a wide range of hexose-1,5-lactones. The hydrolysis of L-gulono-1,5-lactone was previously listed separately.
CAS REGISTRY NUMBER
COMMENTARY hide
9012-44-6
EC 3.1.1.18
9012-73-1
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-glucono-1,5-lactone + H2O
D-gluconate
show the reaction diagram
-
-
-
?
xylitol + H2O
?
show the reaction diagram
-
-
-
?
D-glucono-1,5-lactone + H2O
D-gluconate
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
GNL is a key enzyme involved in vitamin C biosynthesis
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-glucono-1,5-lactone + H2O
D-gluconate
show the reaction diagram
-
-
-
?
D-glucono-1,5-lactone + H2O
D-gluconate
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
GNL is a key enzyme involved in vitamin C biosynthesis
-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
highest expression
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
additional information
-
not detected in spleen
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
-
the enzyme is involved in ascorbic acid biosynthesis
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
RGN_MOUSE
299
0
33407
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
34000
x * 34000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 34000, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 1.6 M ammonium sulfate and 100 mM Tris-HCl, pH 8.5
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
SMP30/GNL knockout mice lack the ability to synthesize vitamin C in vivo
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Toyopearl DEAE-650M column chromatography, Toyopearl SuperQ-650M column chromatography, phenyl Sepharose column chromatography, and Superdex 200 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
SMP30/GNL mRNA expression is evident at the start of gestation, increases for the next 8 days then decreases rapidly until day 11 of gestation
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kondo, Y.; Sasaki, T.; Sato, Y.; Amano, A.; Aizawa, S.; Iwama, M.; Handa, S.; Shimada, N.; Fukuda, M.; Akita, M.; Lee, J.; Jeong, K.S.; Maruyama, N.; Ishigami, A.
Vitamin C depletion increases superoxide generation in brains of SMP30/GNL knockout mice
Biochem. Biophys. Res. Commun.
377
291-296
2008
Mus musculus
Manually annotated by BRENDA team
Furusawa, H.; Sato, Y.; Tanaka, Y.; Inai, Y.; Amano, A.; Iwama, M.; Kondo, Y.; Handa, S.; Murata, A.; Nishikimi, M.; Goto, S.; Maruyama, N.; Takahashi, R.; Ishigami, A.
Vitamin C is not essential for carnitine biosynthesis in vivo: verification in vitamin C-depleted senescence marker protein-30/gluconolactonase knockout mice
Biol. Pharm. Bull.
31
1673-1679
2008
Mus musculus
Manually annotated by BRENDA team
Kagami, Y.; Kondo, Y.; Handa, S.; Maruyama, N.; Ishigami, A.
Senescence marker protein-30/gluconolactonase expression in the mouse ovary during gestation
Biol. Pharm. Bull.
36
2005-2008
2013
Mus musculus
Manually annotated by BRENDA team
Aizawa, S.; Senda, M.; Harada, A.; Maruyama, N.; Ishida, T.; Aigaki, T.; Ishigami, A.; Senda, T.
Structural basis of the gamma-lactone-ring formation in ascorbic acid biosynthesis by the senescence marker protein-30/gluconolactonase
PLoS ONE
8
e53706
2013
Homo sapiens (Q15493), Mus musculus (Q64374), Mus musculus
Manually annotated by BRENDA team