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Reference on EC 4.2.3.2 - ethanolamine-phosphate phospho-lyase

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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Fleshood, H.L.; Pitot, H.C.
The metabolism of O-phosphorylethanolamine in animal tissues. I. O-phosphorylethanolamine phospho-lyase: partial purification and characterization
J. Biol. Chem.
245
4414-4420
1970
Oryctolagus cuniculus, Rattus norvegicus
Manually annotated by BRENDA team
Jones, A.; Faulkner, A.; Turner, J.M.
Microbial metabolism of amino alcohols. Metabolism of ethanolamine and 1-aminopropan-2-ol in species of Erwinia and the roles of amino alcohol kinase and amino alcohol O-phosphate phospho-lyase in aldehyde formation
Biochem. J.
134
959-968
1973
Pantoea agglomerans, Pantoea ananatis, Pectobacterium carotovorum
Manually annotated by BRENDA team
Faulkner, A.; Turner, J.M.
Phosphorylation of ethanolamine in catabolism. Biodegradative adenosine triphosphate-ethanolamine phosphotransferase and related enzymes in bacteria
Biochem. Soc. Trans.
2
133-136
1974
Achromobacter sp., Microbacterium arborescens, Flavobacterium rhenanum
-
Manually annotated by BRENDA team
Veiga-da-Cunha, M.; Hadi, F.; Balligand, T.; Stroobant, V.; Van Schaftingen, E.
Molecular identification of hydroxylysine kinase and of ammoniophospholyases acting on 5-phosphohydroxy-L-lysine and phosphoethanolamine
J. Biol. Chem.
287
7246-7255
2012
Homo sapiens (A2RU49), Homo sapiens
Automatic Mining of ENzyme DAta
Schiroli, D.; Ronda, L.; Peracchi, A.
Kinetic characterization of the human O-phosphoethanolamine phospho-lyase reveals unconventional features of this specialized pyridoxal phosphate-dependent lyase
FEBS J.
282
183-199
2015
BRENDA: Homo sapiens
Textmining: Pisum sativum
Manually annotated by BRENDA teamAutomatic Mining of ENzyme DAta
Schiroli, D; Cirrincione, S; Donini, S; Peracchi, A
Strict reaction and substrate specificity of AGXT2L1, the human O-phosphoethanolamine phospho-lyase.
IUBMB Life
65
645-50
2013
Homo sapiens
Automatic Mining of ENzyme DAta
Santinha, D; Klopot, A; Marques, I; Ellis, E; Jorns, C; Johansson, H; Melo, T; Antonson, P; Jakobsson, T; Flix, V; Gustafsson, J; Domingues, MR; Mode, A; Helguero, LA
Lipidomic analysis of human primary hepatocytes following LXR activation with GW3965 identifies AGXT2L1 as a main target associated to changes in phosphatidylethanolamine.
J Steroid Biochem Mol Biol
198
105558
2019
Homo sapiens
Automatic Mining of ENzyme DAta
Leventoux, N; Augustus, M; Azar, S; Riquier, S; Villemin, JP; Guelfi, S; Falha, L; Bauchet, L; Goz, C; Ritchie, W; Commes, T; Duffau, H; Rigau, V; Hugnot, JP
Transformation Foci in IDH1-mutated Gliomas Show STAT3 Phosphorylation and Downregulate the Metabolic Enzyme ETNPPL, a Negative Regulator of Glioma Growth.
Sci Rep
10
5504
2020
Transformation, Homo sapiens
Automatic Mining of ENzyme DAta
Vettraino, C; Peracchi, A; Donini, S; Parisini, E
Structural characterization of human O-phosphoethanolamine phospho-lyase.
Acta Crystallogr F Struct Biol Commun
76
160-167
2020
Homo sapiens, Pisum sativum, Paenarthrobacter aurescens TC1
Automatic Mining of ENzyme DAta
Wada, N; Yamanaka, S; Shibato, J; Rakwal, R; Hirako, S; Iizuka, Y; Kim, H; Matsumoto, A; Kimura, A; Takenoya, F; Yasunaga, G; Shioda, S
Behavioral and omics analyses study on potential involvement of dipeptide balenine through supplementation in diet of senescence-accelerated mouse prone 8.
Genom Data
10
38-50
2016
Mus musculus
Automatic Mining of ENzyme DAta
Deng, Y; Wu, L; Ding, Q; Yu, H
AGXT2L1 is downregulated in carcinomas of the digestive system.
Oncol Lett
20
1318-1326
2020
Homo sapiens
Automatic Mining of ENzyme DAta
Cuetos, A; Steffen-Munsberg, F; Mangas Sanchez, J; Frese, A; Bornscheuer, UT; Hhne, M; Grogan, G
Structural Basis for Phospholyase Activity of a Class?III Transaminase Homologue.
Chembiochem
17
2308-2311
2016
Homo sapiens
Automatic Mining of ENzyme DAta
White, CJ; Ellis, JM; Wolfgang, MJ
The role of ethanolamine phosphate phospholyase in regulation of astrocyte lipid homeostasis.
J Biol Chem
297
100830
2021
Homo sapiens, Mus sp.
Automatic Mining of ENzyme DAta