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Information on EC 1.14.16.5 - alkylglycerol monooxygenase and Organism(s) Homo sapiens
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1.14.16.5 alkylglycerol monooxygenaseIUBMB Comments
The enzyme cleaves alkylglycerols, but does not cleave alkenylglycerols (plasmalogens). Requires non-heme iron , reduced glutathione and phospholipids for full activity. The product spontaneously breaks down to form a fatty aldehyde and glycerol. The co-product, 4a-hydroxytetrahydropteridine, is rapidly dehydrated to 6,7-dihydropteridine, either spontaneously or by EC 4.2.1.96, 4a-hydroxytetrahydrobiopterin dehydratase.
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Word Map
- 1.14.16.5
- alkylglycerols
- tetrahydrobiopterin
- hydroxylases
- bh4
-
tetrahydrobiopterin-dependent
- biopterin
- pterins
- tetrahydropterins
- dihydropteridine
-
phenylketonuria
- sepiapterin
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
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a 4a-hydroxy-5,6,7,8-tetrahydropteridine
Synonyms
alkylglycerol monooxygenase, glyceryl ether monooxygenase, glyceryl-ether monooxygenase, alkylglycerol mono-oxygenase, o-alkylglycerol monooxygenase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AGMO
alkylglycerol monooxygenase
glyceryl ether hydroxylase
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-
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glyceryl ether monooxygenase
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-
-
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glyceryl ether oxidase
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-
-
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glyceryl ether oxygenase
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-
-
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glyceryl ether-cleaving enzyme
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-
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glyceryl etherase
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-
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glyceryl-ether cleaving enzyme
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-
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O-alkylglycerol monooxygenase
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-
-
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oxygenase, glyceryl ether mono-
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-
-
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alkylglycerol monooxygenase
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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-
-
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redox reaction
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-
-
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reduction
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-
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SYSTEMATIC NAME
IUBMB Comments
1-alkyl-sn-glycerol,tetrahydrobiopteridine:oxygen oxidoreductase
The enzyme cleaves alkylglycerols, but does not cleave alkenylglycerols (plasmalogens). Requires non-heme iron [7], reduced glutathione and phospholipids for full activity. The product spontaneously breaks down to form a fatty aldehyde and glycerol. The co-product, 4a-hydroxytetrahydropteridine, is rapidly dehydrated to 6,7-dihydropteridine, either spontaneously or by EC 4.2.1.96, 4a-hydroxytetrahydrobiopterin dehydratase.
CAS REGISTRY NUMBER
COMMENTARY
37256-82-9
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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
1-alkyl-sn-glycerol + tetrahydrobiopterin + O2
1-O-alkyl-sn-glycerol + dihydrobiopterin + H2O
1-O-pyrenedecyl-sn-glycerol + tetrahydrobiopterin + O2
? + dihydrobiopterin + H2O
-
-
-
-
?
1-O-pyrenedecyl-sn-glycerol + tetrahydrobiopterin + O2
glycerol + pyrenedecanal + 6,7[8H]-dihydrobiopterin + H2O
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-
-
-
?
alkylglycerol + tetrahydrobiopterin + O2
glycerol + fatty aldehyde + 6,7[8H]-dihydrobiopterin + H2O
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after rapid decay of the resulting unstable primary product (hemiacetal)
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?
1-alkyl-sn-glycerol + tetrahydrobiopterin + O2
1-O-alkyl-sn-glycerol + dihydrobiopterin + H2O
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-
-
-
?
1-alkyl-sn-glycerol + tetrahydrobiopterin + O2
1-O-alkyl-sn-glycerol + dihydrobiopterin + H2O
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-
-
?
NATURAL SUBSTRATE
NATURAL 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
1-alkyl-sn-glycerol + tetrahydrobiopterin + O2
1-O-alkyl-sn-glycerol + dihydrobiopterin + H2O
1-alkyl-sn-glycerol + tetrahydrobiopterin + O2
1-O-alkyl-sn-glycerol + dihydrobiopterin + H2O
-
-
-
-
?
1-alkyl-sn-glycerol + tetrahydrobiopterin + O2
1-O-alkyl-sn-glycerol + dihydrobiopterin + H2O
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-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.011
1-O-pyrenedecyl-sn-glycerol
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measured in CHO cells after transfection, pH not specified in the publication, 37°C
0.00258
tetrahydrobiopterin
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measured in CHO cells after transfection, pH not specified in the publication, 37°C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00139
1,10-phenanthroline
Homo sapiens
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pH not specified in the publication, temperature not specified in the publication
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). ALKMO_HUMAN
445
2
51500
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C231A
-
the mutant enzyme activity is not significantly different from wild type
C397A
-
the mutant enzyme activity is not significantly different from wild type
D153A
-
the mutant enzyme activity is not significantly different from wild type
D384A
-
the mutant has significantly reduced, but clearly detectable, enzyme activity
E137A
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the mutation leads to an 18fold increase in the Michaelis-Menten constant for tetrahydrobiopterin. The mutant has an approximately 5fold lower affinity for iron
E152A
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the mutant has significantly reduced, but clearly detectable, enzyme activity
E203A
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the mutant has significantly reduced, but clearly detectable, enzyme activity
E212A
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the mutant has significantly reduced, but clearly detectable, enzyme activity
E324K
the mutation is associated with an autosomal recessive microcephaly
H189A
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the mutant has significantly reduced, but clearly detectable, enzyme activity
H220A
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the mutant enzyme activity is not significantly different from wild type
Q146A
-
the mutant enzyme activity is not significantly different from wild type
Q166A
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the mutant has significantly reduced, but clearly detectable, enzyme activity
Q191A
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the mutant has significantly reduced, but clearly detectable, enzyme activity
R396A
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the mutant has significantly reduced, but clearly detectable, enzyme activity
Y174A
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the mutant has significantly reduced, but clearly detectable, enzyme activity
Y230A
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the mutant enzyme activity is not significantly different from wild type
additional information
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mutation of each of 8 conserved His residues (to alanine) which are all essential for activity
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in CHO cell, expressed in Xenopus laevis oocyte, GFP fusion protein expressed in CHO cell, 6x myc tag version expressed in CHO-K1 cell
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Watschinger, K.; Keller, M.A.; Golderer, G.; Hermann, M.; Maglione, M.; Sarg, B.; Lindner, H.H.; Hermetter, A.; Werner-Felmayer, G.; Konrat, R.; Hulo, N.; Werner, E.R.
Identification of the gene encoding alkylglycerol monooxygenase defines a third class of tetrahydrobiopterin-dependent enzymes
Proc. Natl. Acad. Sci. USA
107
13672-13677
2010
Homo sapiens
Watschinger, K.; Fuchs, J.E.; Yarov-Yarovoy, V.; Keller, M.A.; Golderer, G.; Hermetter, A.; Werner-Felmayer, G.; Hulo, N.; Werner, E.R.
Catalytic residues and a predicted structure of tetrahydrobiopterin-dependent alkylglycerol mono-oxygenase
Biochem. J.
443
279-286
2012
Homo sapiens
Marquet, S.; Bucheton, B.; Reymond, C.; Argiro, L.; El-Safi, S.H.; Kheir, M.M.; Desvignes, J.P.; Beroud, C.; Mergani, A.; Hammad, A.; Dessein, A.J.
Exome sequencing identifies two variants of the alkylglycerol monooxygenase gene as a cause of relapses in visceral leishmaniasis in children, in Sudan
J. Infect. Dis.
216
22-28
2017
Homo sapiens
Alrayes, N.; Mohamoud, H.S.; Ahmed, S.; Almramhi, M.M.; Shuaib, T.M.; Wang, J.; Al-Aama, J.Y.; Everett, K.; Nasir, J.; Jelani, M.
The alkylglycerol monooxygenase (AGMO) gene previously involved in autism also causes a novel syndromic form of primary microcephaly in a consanguineous Saudi family
J. Neurol. Sci.
363
240-244
2016
Homo sapiens (Q6ZNB7), Homo sapiens
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