EC number:3.1.3.2

Enzyme

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     3. Hydrolases
        3.1 Acting on ester bonds
            3.1.3 Phosphoric-monoester hydrolases
ID:3.1.3.2
Description:Acid phosphatase.
Alternative Name: Phosphomonoesterase.
Glycerophosphatase.
Acid phosphomonoesterase.
Prosite: PDOC00891; PDOC00538;
PDB:
PDBScop
2HPA 8031373; 8043751; 8031373; 8043751; 8031373; 8043751; 8031373; 8043751;
1ND6 8031373; 8043751; 8031373; 8043751; 8031373; 8043751; 8031373; 8043751;
1ND5 8031373; 8043751; 8031373; 8043751; 8031373; 8043751; 8031373; 8043751;
1CVI 8031373; 8043751; 8031373; 8043751; 8031373; 8043751; 8031373; 8043751;
1WEI 8030371; 8042750;
 » show all
Cath: 1.20.144.10; 3.60.21.10; 3.40.50.1000; 3.40.50.1240; 3.40.50.2300; 2.60.40.380;

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 3.1.3.2
BRENDA Enzyme Link: BRENDA 3.1.3.2
KEGG Enzyme Link: KEGG3.1.3.2
BioCyc Enzyme Link: BioCyc 3.1.3.2
ExPASy Enzyme Link: ExPASy3.1.3.2
EC2PDB Enzyme Link: EC2PDB 3.1.3.2
ExplorEnz Enzyme Link: ExplorEnz 3.1.3.2
PRIAM enzyme-specific profiles Link: PRIAM 3.1.3.2
IntEnz Enzyme Link: IntEnz 3.1.3.2
MEDLINE Enzyme Link: MEDLINE 3.1.3.2

EC number:3.1.3.2

MSA:

3.1.3.2;
Phylogenetic Tree:

3.1.3.2;
Uniprot:
M-CSA:
RHEA:15017 a phosphate monoester + H2O = an alcohol + phosphate
RULE(radius=1) [*:1]-[O;H0;+0:2]-[*;H0;+0:3].[OH2;+0:4]>>[*;H0;+0:3]-[OH;+0:4].[*:1]-[OH;+0:2]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
The nucleotide sequence of the yeast PHO5 gene: a putative precursor of repressible acid phosphatase contains a signal peptide.Arima K, Oshima T, Kubota I, Nakamura N, Mizunaga T, Toh-e A1983 Mar 256300772
Studies on human placental alkaline phosphatase. II. Kinetic properties and studies on the apoenzyme.Harkness DR1968 Aug4970479
Reciprocal regulation of the tandemly duplicated PHO5/PHO3 gene cluster within the acid phosphatase multigene family of Saccharomyces cerevisiae.Tait-Kamradt AG, Turner KJ, Kramer RA, Elliott QD, Bostian SJ, Thill GP, Rogers DT, Bostian KA1986 Jun3537710
Crystal structure of rat intestinal alkaline phosphatase--role of crown domain in mammalian alkaline phosphatases.Ghosh K, Mazumder Tagore D, Anumula R, Lakshmaiah B, Kumar PP, Singaram S, Matan T, Kallipatti S, Selvam S, Krishnamurthy P, Ramarao M2013 Nov24076154
Crystal structures and biochemical studies of human lysophosphatidic acid phosphatase type 6.Li J, Dong Y, Lü X, Wang L, Peng W, Zhang XC, Rao Z2013 Jul23807634
Molecular cloning and expression of a cDNA encoding the membrane-associated rat intestinal alkaline phosphatase.Lowe M, Strauss AW, Alpers R, Seetharam S, Alpers DH1990 Feb 92155025
A soluble form of phosphatase in Saccharomyces cerevisiae capable of converting farnesyl diphosphate into E,E-farnesol.Song L2006 Feb16484724
Prostatic acid phosphatase degrades lysophosphatidic acid in seminal plasma.Tanaka M, Kishi Y, Takanezawa Y, Kakehi Y, Aoki J, Arai H2004 Jul 3015280042
PURIFICATION AND CRYSTALLIZATION OF THE ALKALINE PHOSPHATASE OF ESCHERICHIA COLI.MALAMY MH, HORECKER BL1964 Dec14269306
Studies on calf-intestinal alkaline phosphatase. I. Chromatographic purification, microheterogeneity and some other properties of the purified enzyme.ENGSTROM L1961 Sep 213890304
Isolation of a cDNA encoding human lysophosphatidic acid phosphatase that is involved in the regulation of mitochondrial lipid biosynthesis.Hiroyama M, Takenawa T1999 Oct 810506173