Glycoside hydrolase family 38

Glycosyl hydrolases family 38 N-terminal domain

golgi alpha-mannosidase ii

Identifiers
Symbol| Glyco_hydro_38
Pfam| PF01074
Pfam clan| CL0158
InterPro| IPR000602
SCOP2| 1o7d / SCOPe / SUPFAM
CAZy| GH38
Membranome| 311
| Available protein structures:

Pfam | structures / ECOD
PDB| RCSB PDB; PDBe; PDBj
PDBsum| structure summary
Alpha mannosidase, middle domain

golgi alpha-mannosidase ii

Identifiers
Symbol| Alpha-mann_mid
Pfam| PF09261
InterPro| IPR015341
SCOP2| 1o7d / SCOPe / SUPFAM
| Available protein structures:

Pfam | structures / ECOD
PDB| RCSB PDB; PDBe; PDBj
PDBsum| structure summary
Glycosyl hydrolases family 38 C-terminal domain

golgi alpha-mannosidase ii

Identifiers
Symbol| Glyco_hydro_38C
Pfam| PF07748
Pfam clan| CL0103
InterPro| IPR011682
SCOP2| 1o7d / SCOPe / SUPFAM
CAZy| GH38
| Available protein structures:

Pfam | structures / ECOD
PDB| RCSB PDB; PDBe; PDBj
PDBsum| structure summary

In molecular biology, glycoside hydrolase family 38 is a family of glycoside hydrolases.

Glycoside hydrolases EC 3.2.1. are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycoside hydrolases, based on sequence similarity, has led to the definition of >100 different families.[1][2][3] This classification is available on the CAZy web site,[4][5] and also discussed at CAZypedia, an online encyclopedia of carbohydrate active enzymes.[6][7]

Glycoside hydrolase family 38 CAZY GH_38 comprises enzymes with only one known activity; alpha-mannosidase (EC 3.2.1.24) (EC 3.2.1.114).

Lysosomal alpha-mannosidase is necessary for the catabolism of N-linked carbohydrates released during glycoprotein turnover. The enzyme catalyzes the hydrolysis of terminal, non-reducing alpha-D-mannose residues in alpha-D-mannosides, and can cleave all known types of alpha-mannosidic linkages. Defects in the gene cause lysosomal alpha-mannosidosis (AM), a lysosomal storage disease characterised by the accumulation of unbranched oligo-saccharide chains.

A domain, which is found in the central region adopts a structure consisting of three alpha helices, in an immunoglobulin/albumin-binding domain-like fold. The domain is predominantly found in the enzyme alpha-mannosidase.[8]

## References[edit]

1. ^ Henrissat B, Callebaut I, Fabrega S, Lehn P, Mornon JP, Davies G (July 1995). "Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases". Proceedings of the National Academy of Sciences of the United States of America. 92 (15): 7090–4. Bibcode:1995PNAS...92.7090H. doi:10.1073/pnas.92.15.7090. PMC 41477. PMID 7624375.
2. ^ Davies G, Henrissat B (September 1995). "Structures and mechanisms of glycosyl hydrolases". Structure. 3 (9): 853–9. doi:10.1016/S0969-2126(01)00220-9. PMID 8535779.
3. ^ Henrissat B, Bairoch A (June 1996). "Updating the sequence-based classification of glycosyl hydrolases". The Biochemical Journal. 316 (Pt 2): 695–6. doi:10.1042/bj3160695. PMC 1217404. PMID 8687420.
4. ^ "Home". CAZy.org. Retrieved 2018-03-06.
5. ^ Lombard V, Golaconda Ramulu H, Drula E, Coutinho PM, Henrissat B (January 2014). "The carbohydrate-active enzymes database (CAZy) in 2013". Nucleic Acids Research. 42 (Database issue): D490-5. doi:10.1093/nar/gkt1178. PMC 3965031. PMID 24270786.
6. ^ "Glycoside Hydrolase Family 38". CAZypedia.org. Retrieved 2018-03-06.
7. ^ CAZypedia Consortium (December 2018). "Ten years of CAZypedia: a living encyclopedia of carbohydrate-active enzymes" (PDF). Glycobiology. 28 (1): 3–8. doi:10.1093/glycob/cwx089. PMID 29040563.
8. ^ Heikinheimo P, Helland R, Leiros HK, Leiros I, Karlsen S, Evjen G, Ravelli R, Schoehn G, Ruigrok R, Tollersrud OK, McSweeney S, Hough E (March 2003). "The structure of bovine lysosomal alpha-mannosidase suggests a novel mechanism for low-pH activation". Journal of Molecular Biology. 327 (3): 631–44. doi:10.1016/S0022-2836(03)00172-4. PMID 12634058.

This article incorporates text from the public domain Pfam and InterPro: IPR000602

This article incorporates text from the public domain Pfam and InterPro: IPR011682

This article incorporates text from the public domain Pfam and InterPro: IPR015341

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Hydrolase: sugar hydrolases (EC 3.2)

3.2.1: Glycoside hydrolases|

| Disaccharidase|

* Sucrase/Sucrase-isomaltase/Invertase
* Maltase
* Trehalase
* Lactase

|

Glucosidases|

* Cellulase
* Alpha-glucosidase
* Acid
* Neutral AB
* Neutral C
* Beta-glucosidase
* cytosolic
* Debranching enzyme

Other|

* Amylase
* Alpha-amylase
* Chitinase
* Lysozyme
* Neuraminidase
* NEU1
* NEU2
* NEU3
* NEU4
* Bacterial neuraminidase
* Viral neuraminidase
* Galactosidases
* Alpha
* Beta
* alpha-Mannosidase
* Glucuronidase
* Klotho
* Hyaluronidase
* Pullulanase
* Glucosylceramidase
* lysosomal
* non-lysosomal
* Galactosylceramidase
* Alpha-N-acetylgalactosaminidase
* NAGA
* Alpha-N-acetylglucosaminidase
* Fucosidase
* Hexosaminidase
* HEXA
* HEXB
* Iduronidase
* Maltase-glucoamylase
* Heparanase
* HPSE2

3.2.2: Hydrolysing
N-Glycosyl compounds|

* DNA glycosylases: Oxoguanine glycosylase

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Enzymes

Activity|

* Active site
* Binding site
* Catalytic triad
* Oxyanion hole
* Enzyme promiscuity
* Diffusion-limited enzyme
* Cofactor
* Enzyme catalysis

Regulation|

* Allosteric regulation
* Cooperativity
* Enzyme inhibitor
* Enzyme activator

Classification|

* EC number
* Enzyme superfamily
* Enzyme family
* List of enzymes

Kinetics|

* Enzyme kinetics
* Eadie–Hofstee diagram
* Hanes–Woolf plot
* Lineweaver–Burk plot
* Michaelis–Menten kinetics

Types|

* EC1 Oxidoreductases (list)
* EC2 Transferases (list)
* EC3 Hydrolases (list)
* EC4 Lyases (list)
* EC5 Isomerases (list)
* EC6 Ligases (list)
* EC7 Translocases (list)

Portal:

* Biology

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