HOME
login
history
all enzymes
BRENDA home
History
Enzyme Nomenclature
Information on EC 3.1.3.1 - alkaline phosphatase
for references in articles please use BRENDA:EC3.1.3.1
Word Map on EC 3.1.3.1
- 3.1.3.1
- osteoblast
-
osteocalcin
- collagen
-
osteogenic
- bilirubin
- renal
- women
- marrow
- urinary
- phosphorus
- lactate
- mesenchymal
- parathyroid
- osteoporosis
- resorption
- cholesterol
- interval
- count
- injury
- pancreatitis
- creatinine
- arterial
- children
- fracture
- pain
- bile
-
transaminase
- spine
- necrosis
- anterior
- femoral
-
lumbar
-
histochemical
-
morphogenetic
- biliary
-
stromal
- duct
-
osteopontin
-
postoperative
- calcification
-
gamma-glutamyl
- periodontal
-
postmenopausal
-
preoperative
- cartilage
- ligament
-
hepatotoxicity
- transpeptidase
-
radiological
-
biocompatibility
- synthesis
- agriculture
- biotechnology
- molecular biology
- diagnostics
- medicine
- food industry
- environmental protection
- analysis
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
The expected taxonomic range for this enzyme is: Archaea, Eukaryota, Bacteria
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
EC NUMBER 
COMMENTARY 
3.1.3.1
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
RECOMMENDED NAME
GeneOntology No.
alkaline phosphatase
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a phosphate monoester + H2O = an alcohol + phosphate
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate
-
a phosphate monoester + H2O = an alcohol + phosphate
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate
a phosphate monoester + H2O = an alcohol + phosphate
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate
-
a phosphate monoester + H2O = an alcohol + phosphate
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate
-
a phosphate monoester + H2O = an alcohol + phosphate
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate
-
a phosphate monoester + H2O = an alcohol + phosphate
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate
-
a phosphate monoester + H2O = an alcohol + phosphate
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate
-
a phosphate monoester + H2O = an alcohol + phosphate
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate
-
a phosphate monoester + H2O = an alcohol + phosphate
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate, active site structure, highly conserved in evolution of alkaline phosphatases
a phosphate monoester + H2O = an alcohol + phosphate
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate
-
a phosphate monoester + H2O = an alcohol + phosphate
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate
-
a phosphate monoester + H2O = an alcohol + phosphate
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate
-
a phosphate monoester + H2O = an alcohol + phosphate
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate
-
a phosphate monoester + H2O = an alcohol + phosphate
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate, active site structure, mechanism
shrimp
-
a phosphate monoester + H2O = an alcohol + phosphate
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate
-
a phosphate monoester + H2O = an alcohol + phosphate
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate
-
a phosphate monoester + H2O = an alcohol + phosphate
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate, catalytically active His153 and His328
-
a phosphate monoester + H2O = an alcohol + phosphate
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate
-
a phosphate monoester + H2O = an alcohol + phosphate
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate
-
a phosphate monoester + H2O = an alcohol + phosphate
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate
-
a phosphate monoester + H2O = an alcohol + phosphate
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate
-
a phosphate monoester + H2O = an alcohol + phosphate
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate, substrate binding and active site structure
-
a phosphate monoester + H2O = an alcohol + phosphate
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate
-
a phosphate monoester + H2O = an alcohol + phosphate
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate
-
a phosphate monoester + H2O = an alcohol + phosphate
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate
-
a phosphate monoester + H2O = an alcohol + phosphate
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate
-
a phosphate monoester + H2O = an alcohol + phosphate
Arg166 contributes to catalysis through binding interactions and through additional transition state stabilization that may arise from complementarity of the guanidinum group to the geometry of the trigonal bipyramidal transition state
-
a phosphate monoester + H2O = an alcohol + phosphate
double in-line displacement mechanism involving two-metal ion catalysis
-
a phosphate monoester + H2O = an alcohol + phosphate
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate
-
-
a phosphate monoester + H2O = an alcohol + phosphate
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate
-
-
a phosphate monoester + H2O = an alcohol + phosphate
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate
-
-
a phosphate monoester + H2O = an alcohol + phosphate
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate
-
-
a phosphate monoester + H2O = an alcohol + phosphate
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate
-
-
a phosphate monoester + H2O = an alcohol + phosphate
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate
-
-
a phosphate monoester + H2O = an alcohol + phosphate
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
-
-
phosphomonoester
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
phosphate-monoester phosphohydrolase (alkaline optimum)
Wide specificity. Also catalyses transphosphorylations. The human placental enzyme is a zinc protein. Some enzymes hydrolyse diphosphate (cf. EC 3.6.1.1 inorganic diphosphatase)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
9001-78-9
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
thermostable conidial and mycelial alkaline phosphatases, thermophilic fungus
-
-
levamisole-insensitive alkaline phosphatase activity; levamisole-sensitive alkaline phosphatase activity
-
-
Saccharomyces pombe
substrate specific enzyme form from structural gene PHO2, non specific enzyme form from structural gene PHO3 and particulate enzyme form from structural gene PHO3
-
-
2 distinct enzyme forms, an inducible enzyme form IAPase in 4 isozymes, and a constitutive enzyme form CAPase
-
-
2 distinct enzyme forms, an inducible enzyme form IAPase in 4 isozymes, and a constitutive enzyme form CAPase
-
-
-
664333, 664434, 664559, 665025, 680322, 681098, 681515, 693244, 693398, 695120, 707733, 713744, 714329, 714864, 94567, 94586, 94600, 94610, 94633, 94640
-
-
beagle and mixed breed, 2 genes encoding 2 isozyme types: a tissue non-specific isozyme and an intestinal isozyme
-
-
-
653130, 665308, 666720, 680200, 680377, 682632, 692734, 695120, 729061, 94562, 94563, 94565, 94566, 94567, 94580, 94581, 94586, 94594, 94628, 94632, 94638
-
-
gene phoA, 3 isozymes 1, 2, and 3 differing in the N-terminal sequence; gene phoA, 3 isozymes 1,2, and 3 differing in the N-terminal sequence
-
-
-
650752, 651458, 666373, 666377, 677519, 678570, 679113, 680067, 681634, 681752, 690959, 691694, 692297, 694196, 694888, 707746, 709457, 709773, 714341, 714682, 730020, 94563, 94564, 94567, 94568, 94573, 94575, 94579, 94581, 94582, 94584, 94585, 94597, 94603, 94609, 94610, 94611, 94616, 94623, 94627, 94629, 94630, 94637, 94639
-
-
4 isozyme types: 1. nonspecific liver/bone/kidney, which is also present in osteoblast and neutrophilic granulocytes, 2. intestinal, 3. placental, 4. germ-cell
-
-
secreted alkaline phosphatase SEAP containing a single N-glycan chain, a model protein for investigation of glycosylation pattern
-
-
a major intestinal-like isoenzyme and a minor tissue-unspecific type
-
-
-
652666, 664288, 664887, 677474, 678570, 680168, 681561, 690297, 690298, 691134, 691566, 693930, 714001, 94567, 94570, 94574, 94578, 94593, 94608, 94610, 94621, 94636
-
-
substrate specific enzyme form, non specific enzyme form from structural gene PHO8, and particulate enzyme form from structural gene PHO8
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
malfunction
deletion of OE5192R produces a mutant strain with virtually no phosphatase activity
malfunction
the ability of living parasites to cleave exogenous adenosine monophosphate and generate adenosine is very largely abolished when SmAP gene expression is suppressed following RNAi treatment targeting the gene
physiological function
-
Daphnia magna eating phosphorus-poor food have significantly higher alkaline phosphatase activity in their bodies compared with individuals eating phosphorus-rich food. By contrast, poor phosphorus-nutrition of Daphnia lowers alkaline phosphatase activity in released materials compared with that measured from their phosphorus-sufficient conspecifics
physiological function
-
in neonatal blood plasma, soluble 5'-nucleotidase and alkaline phosphatase mediate conversion of AMP to adenosine, whereas soluble adenosine deaminase catabolizes adenosine to inosine. Newborn blood plasma demonstrates substantially higher adenosine-generating 5'-nucleotidase and alkaline phosphatase activity and lower metabolizing adenosine deaminase activity than adult plasma. Abundant alkaline phosphatase expressed on the surface of circulating neonatal neutrophils is the dominant AMPase on these cells
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2'-[2-benzthiazole]-6'-hydroxybenzthiazole phosphate + H2O
2'-[2-benzthiazole]-6'-hydroxybenzthiazole + phosphate
-
weakly fluorescent substrate
highly fluorescent product
?
2-chloro-5-(4-methoxyspiro (1,2-dioxetane-3,2'-(5'-chloro)tricyclo[3.3.1.13,7]decan)-4-yl)phenyl phosphate + H2O
2-chloro-5-(4-methoxyspiro (1,2-dioxetane-3,2'-(5'-chloro)tricyclo[3.3.1.13,7]decan)-4-yl)phenol + phosphate
-
CDP-star
-
-
?
3'-ITP + H2O
?
-
51.5% of the activity with 4-nitrophenyl phosphate
-
-
?
5'-dCMP + H2O
deoxycytidine + phosphate
-
80% of activity with p-nitrophenyl phosphate
-
-
?
adenosine 5'-(beta-glucosyl)diphosphate + H2O
?
-
29.8% of the activity with 4-nitrophenyl phosphate
-
-
?
adenosine 5'-diphosphate + H2O
AMP + phosphate
-
77% of the activity with 4-nitrophenyl phosphate
-
-
?
adenosine 5'-monophosphate + H2O
?
306.1% of the activity with 4-nitrophenyl phosphate
-
-
?
adenosine 5'-triphosphate + H2O
?
257.4% of the activity with 4-nitrophenyl phosphate
-
-
?
adenosine 5'-triphosphate + H2O
AMP + phosphate
-
61% of the activity with 4-nitrophenyl phosphate
-
-
?
alpha-glycerophosphate + H2O
glycerol + phosphate
-
60% of activity with p-nitrophenyl phosphate
-
-
?
alpha-naphthyl acid phosphate + H2O
?
88.6% of the activity with 4-nitrophenyl phosphate
-
-
?
alpha/beta-glycerophosphate + H2O
glycerol + phosphate
-
low activity with alpha-isomer
-
?
bromochloroindolyl phosphate + nitroblue tetrazolium
?
-
i.e. BCIP/NBT system
-
?
cytidine 5'-monophosphate + H2O
?
343.8% of the activity with 4-nitrophenyl phosphate
-
-
?
D-fructose 1,6-diphosphate + H2O
?
-
52% of the activity with 4-nitrophenyl phosphate
-
-
?
disodium 3-(4-meth- oxyspiro [1,2-dioxetane-3,2'-(5'-chloro)-tricyclo [3.3.1.13,7]- decan]-4-yl)phenyl phosphate + H2O
?
-
-
-
-
?
guanosine 5'-monophosphate + H2O
?
358.8% of the activity with 4-nitrophenyl phosphate
-
-
?
histone II-A + H2O
?
-
enzyme shows protein phosphatase activity
-
?
indoxyl phosphate + nitroblue tetrazolium chloride
nitrioblue diformazan + phosphate
-
-
-
?
methyl 4-nitrophenyl phosphate + H2O
methyl phosphate + 4-nitrophenol
-
-
-
-
?
methyl 4-nitrophenyl phosphorothioate + H2O
4-nitrophenol + methyl phosphorothioate
-
only the R-enantiomer is detectably hydrolyzed by the enzyme
-
-
?
methyl p-nitrophenyl phosphate + H2O
methanol + p-nitrophenol + phosphate
-
-
-
-
?
methyl p-nitrophenyl phosphorothioate + H2O
methanol + p-nitrophenol + phosphorothioate
-
-
-
-
?
N-acetylcysteamine S-phosphate + H2O
N-acetylcysteamine + phosphate
-
-
-
-
?
phosphothreonine + H2O
phosphate + Thr
-
22.1% of the activity with 4-nitrophenyl phosphate
-
-
?
phosphotyrosine + H2O
phosphate + Tyr
-
23.7% of the activity with 4-nitrophenyl phosphate
-
-
?
uridine 5'-monophosphate + H2O
?
388.6% of the activity with 4-nitrophenyl phosphate
-
-
?
2'-deoxyadenosine 5'-monophosphate + H2O
?
113.3% of the activity with 4-nitrophenyl phosphate
-
-
?
2'-deoxyadenosine 5'-monophosphate + H2O
?
113.3% of the activity with 4-nitrophenyl phosphate
-
-
?
2-phosphoglycerate + H2O
glycerol + phosphate
-
53.7% of the activity with 4-nitrophenyl phosphate
-
-
?
2-phosphoglycerate + H2O
glycerol + phosphate
-
hydrolyzed by isoenzyme III, weak activity with isoenzyme I and II
-
-
?
2-phosphoglycerate + H2O
glycerol + phosphate
-
wild-type activity is 16.9% of wild-type activity with 4-nitrophenyl phosphate. Activity with mutant os-1 enzyme is 16.3fold higher than activity from wild-type enzyme
-
-
?
3-phosphoglycerate + H2O
glycerol + phosphate
-
hydrolyzed by isoenzyme III, weak activity with isoenzyme II, no activity with isoenzyme I
-
-
?
4-methylumbelliferyl phosphate + H2O
4-methylumbelliferone + phosphate
-
-
-
-
?
4-methylumbelliferyl phosphate + H2O
4-methylumbelliferone + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
reaction is at least partially diffusion-controlled
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
non-specific, phosphoseryl intermediate
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
strong support for a model in which electrostatic interactions between the bimetallo Zn2+ site and a nonbridging phosphate ester oxygen atom make a significant contribution to the large rate enhancement observed for alkaline phosphatase-catalyzed phosphate monoester hydrolysis
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
hydrolysis of 4-nitrophenylphosphate is nonlinear with time when the enzyme is microinjected into reversed micelles (of hexadecyltrimethylammoniumbromide in cyclohexane, with 1-butanol as cosurfactant) that contain substrate
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
hydrolysis of 4-nitrophenylphosphate is nonlinear with time when the enzyme is microinjected into reversed micelles (of hexadecyltrimethylammoniumbromide in cyclohexane, with 1-butanol as cosurfactant) that contain substrate
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
allosteric mechanism
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
activity with mutant os-1 enzyme is 12.2fold higher than activity from wild-type enzyme
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
best substrate
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
non-specific, via phosphoseryl intermediate
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
5'-AMP + H2O
adenosine + phosphate
-
90% of activity with p-nitrophenyl phosphate
-
-
?
5'-AMP + H2O
adenosine + phosphate
-
90% of activity with p-nitrophenyl phosphate
-
-
?
5'-CMP + H2O
cytidine + phosphate
-
80% of activity with p-nitrophenyl phosphate
-
-
?
5'-GMP + H2O
guanosine + phosphate
-
40% of activity with p-nitrophenyl phosphate
-
-
?
5'-UMP + H2O
uridine + phosphate
-
30% of activity with p-nitrophenyl phosphate
-
-
?
5'-UMP + H2O
uridine + phosphate
-
30% of activity with p-nitrophenyl phosphate
-
-
?
5-bromo-4-chloro-3-indolyl phosphate + H2O
?
50.3% of the activity with 4-nitrophenyl phosphate
-
-
?
5-bromo-4-chloro-3-indolyl phosphate + H2O
?
50.3% of the activity with 4-nitrophenyl phosphate
-
-
?
ADP + H2O
AMP + phosphate
-
wild-type activity is 16.9% of wild-type activity with 4-nitrophenyl phosphate. Activity with mutant os-1 enzyme is 1.2fold lower than activity from wild-type enzyme
-
-
?
alpha-naphthyl phosphate + H2O
alpha-naphthol + phosphate
-
-
-
?
alpha-naphthyl phosphate + H2O
alpha-naphthol + phosphate
-
-
-
?
alpha-naphthyl phosphate + H2O
naphthol + phosphate
-
hydrolyzed by isoenzyme II and III, no activity with isoenzyme I
-
-
?
AMP + H2O
adenosine + phosphate
-
wild-type activity is 9.6% of wild-type activity with 4-nitrophenyl phosphate. Activity with mutant os-1 enzyme is 18.2fold higher than activity from wild-type enzyme
-
-
?
ATP + H2O
?
-
57.8% of the activity with 4-nitrophenyl phosphate
-
-
?
ATP + H2O
?
-
wild-type activity is 15.4% of wild-type activity with 4-nitrophenyl phosphate. Activity with mutant os-1 enzyme is 6.9fold higher than activity from wild-type enzyme
-
-
?
beta-glycerophosphate + H2O
glycerol + phosphate
-
20% of activity with p-nitrophenyl phosphate
-
-
?
beta-glycerophosphate + H2O
glycerol + phosphate
-
20% of activity with p-nitrophenyl phosphate
-
-
?
beta-glycerophosphate + H2O
glycerol + phosphate
uranium precipitation assay: uranyl carbonate solution in carbonate-bicarbonate buffer, supplemented with beta-glycerophosphate as the substrate at 30°C under static nongrowing conditions in a final volume of 5 ml
-
-
?
beta-glyceryl phosphate + H2O
glycerol + phosphate
-
-
-
?
bis(p-nitrophenyl) phosphate + H2O
?
6.1% of the activity with 4-nitrophenyl phosphate
-
-
?
bis(p-nitrophenyl) phosphate + H2O
?
6.1% of the activity with 4-nitrophenyl phosphate
-
-
?
casein + H2O
?
-
enzyme shows protein phosphatase activity
-
?
casein + H2O
?
-
enzyme shows protein phosphatase activity
-
?
D-fructose 6-phosphate + H2O
D-fructose + phosphate
-
36% of the activity with 4-nitrophenyl phosphate
-
-
?
D-fructose 6-phosphate + H2O
D-fructose + phosphate
-
5.2% of the activity with 4-nitrophenyl phosphate
-
-
?
D-fructose 6-phosphate + H2O
D-fructose + phosphate
-
wild-type activity is 2.2% of wild-type activity with 4-nitrophenyl phosphate. Activity with mutant os-1 enzyme is 52fold higher than activity from wild-type enzyme
-
-
?
D-glucose 1-phosphate + H2O
D-glucose + phosphate
-
32% of the activity with 4-nitrophenyl phosphate
-
-
?
D-glucose 1-phosphate + H2O
D-glucose + phosphate
-
wild-type activity is 9.6% of wild-type activity with 4-nitrophenyl phosphate. Activity with mutant os-1 enzyme is 21fold higher than activity from wild-type enzyme
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
60% of the activity with 4-nitrophenyl phosphate
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
19.4% of the activity with 4-nitrophenyl phosphate
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
wild-type activity is 6.6% of wild-type activity with 4-nitrophenyl phosphate. Activity with mutant os-1 enzyme is 34.5fold higher than activity from wild-type enzyme
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
glucose 1-phosphate + H2O
glucose + phosphate
-
93% of the activity with 4-nitrophenyl phosphate
-
-
?