Accepted Name |
mannosyl-oligosaccharide 1,2-alpha-mannosidase
|
Alternative Name(s) |
Man9-mannosidase |
ManI |
mannosidase 1A |
mannosidase 1B |
Reaction catalysed |
- 4 H2O + N(4)-(alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 9A1,2,3B1,2,3) = 4 beta-D-mannose + N(4)-(alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 5A1,2)
- 3 H2O + N(4)-(alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 8A1,2,3B1,3) = 3 beta-D-mannose + N(4)-(alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 5A1,2)
|
Comment(s) |
- This family of mammalian enzymes, located in the Golgi system,
participates in the maturation process of N-glycans that leads to
formation of hybrid and complex structures.
- The enzymes catalyze the hydrolysis of the four (1->2)-linked alpha-
D-mannose residues from the Man9GlcNAc2 oligosaccharide attached to
target proteins.
- Alternatively, the enzymes act on the Man8GlcNAc2 isomer formed by
EC 3.2.1.209.
- The enzymes are type II membrane proteins, require Ca(2+), and use an
inverting mechanism.
- While all three human enzymes can catalyze the reactions listed here,
some of the enzymes can additionally catalyze hydrolysis in an
alternative order, generating additional isomeric intermediates,
although the final product is the same.
- The names of the isomers listed here are based on a nomenclature
system proposed by Prien et al.
|
Cross-references |
BRENDA | 3.2.1.113 |
EC2PDB | 3.2.1.113 |
ExplorEnz | 3.2.1.113 |
PRIAM enzyme-specific profiles | 3.2.1.113 |
KEGG Ligand Database for Enzyme Nomenclature | 3.2.1.113 |
IUBMB Enzyme Nomenclature | 3.2.1.113 |
IntEnz | 3.2.1.113 |
MEDLINE | Find literature relating to 3.2.1.113 |
MetaCyc | 3.2.1.113 |
Rhea expert-curated reactions | 3.2.1.113 |
UniProtKB/Swiss-Prot |
Q9BZQ6, EDEM3_HUMAN | Q2HXL6, EDEM3_MOUSE | Q6GQB9, EDEM3_XENLA |
P53624, MA1A1_DROME | P33908, MA1A1_HUMAN | P45700, MA1A1_MOUSE |
O02773, MA1A1_PIG | P45701, MA1A1_RABIT | O18498, MA1A1_SPOFR |
O60476, MA1A2_HUMAN | P39098, MA1A2_MOUSE | Q9UKM7, MA1B1_HUMAN |
A2AJ15, MA1B1_MOUSE | B2GUY0, MA1B1_RAT | Q9NR34, MA1C1_HUMAN |
Q18788, MAN12_CAEEL | P31723, MAN12_PENCI | D4AV26, MNS1B_ARTBC |
A1CP08, MNS1B_ASPCL | B0XMT4, MNS1B_ASPFC | B8N417, MNS1B_ASPFN |
Q4WRZ5, MNS1B_ASPFU | A2QAS2, MNS1B_ASPNC | Q2ULB2, MNS1B_ASPOR |
Q12563, MNS1B_ASPPH | Q0D076, MNS1B_ASPTN | E9CXX8, MNS1B_COCPS |
Q5BF93, MNS1B_EMENI | A1D1W1, MNS1B_NEOFI | Q9C512, MNS1_ARATH |
Q8J0Q0, MNS1_CANAX | Q9P7C3, MNS1_SCHPO | P32906, MNS1_YEAST |
Q8H116, MNS2_ARATH | Q93Y37, MNS3_ARATH |
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