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Information on EC 3.2.1.101 - mannan endo-1,6-alpha-mannosidase
for references in articles please use BRENDA:EC3.2.1.101
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EC Tree 3 Hydrolases
3.2 Glycosylases
3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
3.2.1.101 mannan endo-1,6-alpha-mannosidase
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
showSynonyms
endom, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
endo-1,6-alpha-mannanase
endo-alpha(1->6)mannanase
-
-
-
-
endo-alpha-1->6-D-mannanase
-
-
-
-
endo-alpha1->6-D-mannase
-
-
-
-
endo-alpha1->6-mannanase
-
-
-
-
mannanase, endo-1,6-alpha-
-
-
-
-
endo-1,6-alpha-mannanase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(1,6-beta-D-mannopyranosyl)n-1,6-beta-D-mannopyranose + H2O = (1,6-beta-D-mannopyranosyl)n-2-1,6-beta-D-mannopyranose + 6-O-beta-D-mannopyranosyl-beta-D-mannopyranose
(1,6-beta-D-mannopyranosyl)n-1,6-beta-D-mannopyranose + H2O = (1,6-beta-D-mannopyranosyl)n-2-1,6-beta-D-mannopyranose + 6-O-beta-D-mannopyranosyl-beta-D-mannopyranose
enzyme hydrolyzes alpha-1,6-D-mannosidic and not beta-1,6-D-mannosidic linkages
-
(1,6-beta-D-mannopyranosyl)n-1,6-beta-D-mannopyranose + H2O = (1,6-beta-D-mannopyranosyl)n-2-1,6-beta-D-mannopyranose + 6-O-beta-D-mannopyranosyl-beta-D-mannopyranose
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
6-alpha-D-mannan mannanohydrolase
-
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CAS REGISTRY NUMBER
COMMENTARY
58500-56-4
-
98148-86-8
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
alpha-1,6-D-mannohexaose + H2O
D-mannose + alpha-1,6-D-mannobiose
-
Substrates: -
Products: end-product, with intermediate formation of mannose, mannobiose and mannotriose, the latter apparently converts more slowly to the smaller products
Products: end-product, with intermediate formation of mannose, mannobiose and mannotriose, the latter apparently converts more slowly to the smaller products
?
alpha-1,6-D-mannooctaose + H2O
D-mannose + alpha-1,6-D-mannobiose
-
Substrates: largest substrate
Products: end-product, with intermediate formation of mannose, mannobiose and mannotriose, the latter apparently converts more slowly to the smaller products
Products: end-product, with intermediate formation of mannose, mannobiose and mannotriose, the latter apparently converts more slowly to the smaller products
?
alpha-1,6-D-mannopentaose + H2O
D-mannose + alpha-1,6-D-mannobiose
-
Substrates: -
Products: end-product, with intermediate formation of mannose, mannobiose and mannotriose, the latter apparently converts more slowly to the smaller products
Products: end-product, with intermediate formation of mannose, mannobiose and mannotriose, the latter apparently converts more slowly to the smaller products
?
alpha-1,6-D-mannotetraose + H2O
D-mannose + alpha-1,6-D-mannobiose
-
Substrates: -
Products: end-product, with intermediate formation of mannose, mannobiose and mannotriose, the latter apparently converts more slowly to the smaller products
Products: end-product, with intermediate formation of mannose, mannobiose and mannotriose, the latter apparently converts more slowly to the smaller products
?
alpha-1,6-D-mannotriose + H2O
D-mannose + alpha-1,6-D-mannobiose
-
Substrates: smallest substrate
Products: -
Products: -
?
alpha-1,6-mannosylated pro-alpha-factor + H2O
?
-
Substrates: -
Products: -
Products: -
?
alpha-1,6-D-mannan + H2O
D-mannose + alpha-1,6-D-mannobiose
-
Substrates: -
Products: -
Products: -
?
alpha-1,6-D-mannan + H2O
D-mannose + alpha-1,6-D-mannobiose
-
Substrates: unbranched, with more than 80% alpha-1,6-D-mannosidic linkages, best substrate
Products: end-product, with intermediate formation of alpha-1,6-mannooligosaccharides of various sizes
Products: end-product, with intermediate formation of alpha-1,6-mannooligosaccharides of various sizes
?
alpha-1,6-D-mannan + H2O
D-mannose + alpha-1,6-D-mannobiose
-
Substrates: Saccharomyces cerevisiae X2180-1A backbone mannan
Products: end-product, with intermediate formation of alpha-1,6-mannooligosaccharides of various sizes
Products: end-product, with intermediate formation of alpha-1,6-mannooligosaccharides of various sizes
?
alpha-1,6-D-mannan + H2O
D-mannose + alpha-1,6-D-mannobiose
-
Substrates: Saccharomyces cerevisiae X2180-1A-5 mannan
Products: -
Products: -
?
alpha-1,6-D-mannan + H2O
D-mannose + alpha-1,6-D-mannobiose
-
Substrates: Saccharomyces cerevisiae X2180-1A-5 mannan
Products: end-product, with intermediate formation of alpha-1,6-mannooligosaccharides of various sizes
Products: end-product, with intermediate formation of alpha-1,6-mannooligosaccharides of various sizes
?
alpha-1,6-D-mannooligosaccharide + H2O
mannose + alpha-1,6-D-mannobiose
-
Substrates: smallest substrate: alpha-1,6-mannotriose, largest substrate: alpha-1,6-mannooctaose
Products: end-product, with intermediate formation of mannose, mannobiose and mannotriose, the latter apparently converts more slowly to the smaller products
Products: end-product, with intermediate formation of mannose, mannobiose and mannotriose, the latter apparently converts more slowly to the smaller products
?
alpha-1,6-D-mannooligosaccharide + H2O
mannose + alpha-1,6-D-mannobiose
-
Substrates: unbranched alpha-1,6 outer chain of N-linked oligosaccharides
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate specificity
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme hydrolyzes alpha-1,6-D-mannosidic and not beta-1,6-D-mannosidic linkages
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with alpha-1,2-mannosylated pro-alpha-factor
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity on branched alpha-mannan, alpha-1,6-mannans that contain side chains, little or no activity with glucans: amylose, dextran, cellulose, laminarin, alpha-1,6-mannobiose, reduced mannobiose, reduced mannotriose, no activity with methyl alpha-D-mannoside or p-nitrophenyl alpha-D-mannoside, no activity with beta-1,4-D-mannan, methyl alpha-D-mannopyranoside or p-nitrophenyl alpha-D-mannopyranoside
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
p-chloromercuribenzoate
-
1 mM: complete inhibition, 0.001 mM: 50% inhibition
reduced alpha-1,6-mannohexaose
-
54% inhibition, also serves as a substrate
-
[(3R,4R, 5R)-4,5-dihydroxypiperidin-3-yl]methyl 1-thio-alpha-D-mannopyranoside
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[(3S,4R,5R)-4,5-dihydroxypiperidin-3-yl]methyl 6-S-alpha-D-mannopyranosyl-1,6-dithio-alpha-D-mannopyranoside
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line Links Show AA Sequence and Transmembrane Helices (5136 entries)
Longer loading times are possible. Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Longer loading times are possible. Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
the non-hydrolyzable S-linked azasugars, 1,6-alpa-mannosylthio- and 1,6-alpha-mannobiosylthioisofagomine bind with high affinity to the enzyme. X-ray crystallography shows an atypical interaction of the isofagomine nitrogen with the catalytic acid/base. Molecular dynamics simulations reveal that the atypical binding results from sulfur perturbing the most stable form away from the nucleophile interaction preferred for the O-linked congener
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ethanol
-
1% v/v ethanol: stable and slight activation, effect decreases at higher concentrations, at 10% ethanol: inactivation
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-10°C, crude enzyme solution, 0.05 M citrate-phosphate buffer, pH 5.5, 0.001 mM CaCl2
-
4°C, 0.1 M citrate-phosphate buffer, pH 6.0, or 0.1 M potassium phosphate buffer, pH 6.8, 1 mM CaCl2, stable for at least 1 month
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4°C, 1 ml aliquots, 0.1 M citrate-phosphate buffer, pH 6.0, or 0.1 M potassium phosphate buffer, pH 6.8, 1 mM CaCl2, 1 year, 80% original activity retained
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4°C, crude enzyme solution, 0.1 M citrate-phosphate buffer, pH 5.5, more than 1 month, without appreciable loss of activity
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frozen and lyophilized, crude enzyme solution, more than 1 month, without appreciable loss of activity
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
analysis
-
used to determine the structure of mannan-protein linkage region
analysis
-
used to define kinetics of mannosylation of pro-alpha-factor, pro-alphaf, to distinguish alpha-1,6-mannosylated and alpha-1,2-mannosylated forms of glycoproteins
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Nakajima, T.; Maitra, S.K.; Ballou, C.E.
An endo-alpha1 -> 6-D-mannanase from a soil bacterium. Purification, properties, and mode of action
J. Biol. Chem.
251
174-181
1976
Niallia circulans
brenda
Brigance, W.T.; Barlowe, C.; Graham, T.R.
Organization of the yeast golgi complex into at least four functionally distinct compartments
Mol. Biol. Cell
11
171-182
2000
Niallia circulans
brenda
Nakajima, T.; Ballou, C.E.
Structure of the linkage region between the polysaccharide and protein parts of Saccharomyces cerevisiae mannan
J. Biol. Chem.
249
7685-7694
1974
Niallia circulans
brenda
Maruyama, Y.; Nakajima, T.
The aman6 gene encoding a yeast mannan backbone degrading 1,6-alpha-D-mannanase in Bacillus circulans: cloning, sequence analysis, and expression
Biosci. Biotechnol. Biochem.
64
2018-2020
2000
Niallia circulans (Q9Z4P9)
brenda
Belz, T.; Jin, Y.; Coines, J.; Rovira, C.; Davies, G.J.; Williams, S.J.
An atypical interaction explains the high-affinity of a non-hydrolyzable S-linked 1,6-alpha-mannanase inhibitor
Chem. Commun. (Camb.)
53
9238-9241
2017
Niallia circulans (Q9Z4P9)
brenda
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