Entry |
|
Name |
protein O-GlcNAcase;
OGA;
glycoside hydrolase O-GlcNAcase;
O-GlcNAcase;
BtGH84;
O-GlcNAc hydrolase
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Class |
Hydrolases;
Glycosylases;
Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
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Sysname |
[protein]-3-O-(N-acetyl-beta-D-glucosaminyl)-L-serine/threonine N-acetylglucosaminyl hydrolase
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Reaction(IUBMB) |
(1) [protein]-3-O-(N-acetyl-beta-D-glucosaminyl)-L-serine + H2O = [protein]-L-serine + N-acetyl-D-glucosamine [RN: R09672];
(2) [protein]-3-O-(N-acetyl-beta-D-glucosaminyl)-L-theronine + H2O = [protein]-L-threonine + N-acetyl-D-glucosamine [RN: R09673]
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Reaction(KEGG) |
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Substrate |
[protein]-3-O-(N-acetyl-beta-D-glucosaminyl)-L-serine [CPD: C19802];
H2O [CPD: C00001];
[protein]-3-O-(N-acetyl-beta-D-glucosaminyl)-L-theronine
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Product |
[protein]-L-serine [CPD: C02189];
N-acetyl-D-glucosamine [CPD: C00140];
[protein]-L-threonine [CPD: C19803]
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Comment |
Within higher eukaryotes post-translational modification of protein serines/threonines with N-acetylglucosamine (O-GlcNAc) is dynamic, inducible and abundant, regulating many cellular processes by interfering with protein phosphorylation. EC 2.4.1.255 (protein O-GlcNAc transferase) transfers GlcNAc onto substrate proteins and EC 3.2.1.169 (protein O-GlcNAcase) cleaves GlcNAc from the modified proteins.
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History |
EC 3.2.1.169 created 2011
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Orthology |
K15719 | protein O-GlcNAcase / histone acetyltransferase |
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Genes |
» show all
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Reference |
|
Authors |
Gao Y, Wells L, Comer FI, Parker GJ, Hart GW |
Title |
Dynamic O-glycosylation of nuclear and cytosolic proteins: cloning and characterization of a neutral, cytosolic beta-N-acetylglucosaminidase from human brain. |
Journal |
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Sequence |
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Reference |
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Authors |
Wells L, Gao Y, Mahoney JA, Vosseller K, Chen C, Rosen A, Hart GW |
Title |
Dynamic O-glycosylation of nuclear and cytosolic proteins: further characterization of the nucleocytoplasmic beta-N-acetylglucosaminidase, O-GlcNAcase. |
Journal |
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Sequence |
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Reference |
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Authors |
Cetinbas N, Macauley MS, Stubbs KA, Drapala R, Vocadlo DJ |
Title |
Identification of Asp174 and Asp175 as the key catalytic residues of human O-GlcNAcase by functional analysis of site-directed mutants. |
Journal |
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Reference |
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Authors |
Dennis RJ, Taylor EJ, Macauley MS, Stubbs KA, Turkenburg JP, Hart SJ, Black GN, Vocadlo DJ, Davies GJ |
Title |
Structure and mechanism of a bacterial beta-glucosaminidase having O-GlcNAcase activity. |
Journal |
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Sequence |
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Reference |
|
Authors |
Kim EJ, Kang DO, Love DC, Hanover JA |
Title |
Enzymatic characterization of O-GlcNAcase isoforms using a fluorogenic GlcNAc substrate. |
Journal |
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Reference |
|
Authors |
Dong DL, Hart GW |
Title |
Purification and characterization of an O-GlcNAc selective N-acetyl-beta-D-glucosaminidase from rat spleen cytosol. |
Journal |
J Biol Chem 269:19321-30 (1994) |
Sequence |
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Other DBs |
ExPASy - ENZYME nomenclature database: | 3.2.1.169 |
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