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Information on EC 3.2.1.78 - mannan endo-1,4-beta-mannosidase and Organism(s) Solanum lycopersicum and UniProt Accession Q6YM50
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3.2.1.78 mannan endo-1,4-beta-mannosidaseSpecify your search results
Word Map
- 3.2.1.78
- mannans
- galactomannans
- locust
- glucomannans
- guar
- konjac
- mannobiose
- alpha-galactosidase
- reesei
- manno-oligosaccharides
- carob
- radicle
-
micropylar
-
mannan-degrading
-
ivory
-
kraft
- mannotetraose
- beta-mannans
- mannopentaose
-
hemicellulase
-
softwood
-
endohydrolases
- cellulosome
- cellvibrio
- endo-1,4-beta-glucanase
-
copra
-
thermomonospora
-
mannan-binding
- food industry
- agriculture
- synthesis
- pharmacology
- degradation
- biotechnology
- paper production
- nutrition
- medicine
- industry
- drug development
The taxonomic range for the selected organisms is: Solanum lycopersicum
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
Synonyms
beta-mannanase, endo-beta-mannanase, man5a, endo-mannanase, manb-1601, endo-beta-1,4-mannanase, man26a, man26b, man5c, caman, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1,4-beta-D-mannan mannanohydrolase
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beta-1,4-mannan 4-mannanohydrolase
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beta-D-mannanase
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Beta-mannanase
beta-mannanase B
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endo-1,4-beta-mannanase
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endo-1,4-mannanase
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endo-beta-1,4-mannase
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endo-beta-mannanase
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LeMAN4a
mannanase, endo-1,4-beta-
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Beta-mannanase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
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SYSTEMATIC NAME
IUBMB Comments
4-beta-D-mannan mannanohydrolase
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CAS REGISTRY NUMBER
COMMENTARY
37288-54-3
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
galactoglucomannan + oligosaccharide
[3H]-labelled polysaccharide
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transglucosylation
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-
?
Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man + H2O
Manbeta(1-4)Manbeta(1-4)Man + Manbeta(1-4)Man + Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man + mannose
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?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
isoform Man4a is expressed in the fruit cell wall at all ripening stages, but it is not active during the initial green stage. This is not due to the presence of inhibitors of its activity, nor due to changes in its mRNA sequence
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
transient expression in onion epidermal cells of endo-beta-mannanase trancripts fused to green fluorescent protein results in the expressed enzyme being localized to the cell walls. This occurs initially during ripening in the skin and outer pericarp of the fruit, and later in the skin and throughout the pericarp
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
when endo-beta-mannanase activity is much reduced by RNAi and antisense RNA strategies, their firmness is higher compared to those of control fruits at the turning and orange-color stages, but at the red-ripe stage firmness is similar between the two fruit-types
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MAN5_SOLLC
414
1
46835
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
amino acid sequence contains a signal peptide cleavage site between residues 21-22, targeting sequence for cell wall
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
molecular dynamic simulation of wild-type and mutant lacking the C-terminal amino acid residues 394-399, SerLysLeuSer. The inactive form has a lower stability than the active one. The loss of amino acids from the C-terminal end of the protein indirectly affects the conformation of the catalytic Glu318 residue and stability of active site because of interactions between residues at the C-terminus and the rest of protein
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
the cultivar Walter displays an inactive enzyme due to the absence of the C-terminal four amino acid residues 394-399, SerLysLeuSer. The inactive form has a lower stability than the active one. The loss of amino acids from the C-terminal end of the protein indirectly affects the conformation of the catalytic Glu318 residue and stability of active site because of interactions between residues at the C-terminus and the rest of protein
additional information
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the cultivar Walter displays an inactive enzyme due to the absence of the C-terminal four amino acid residues 394-399, SerLysLeuSer. The inactive form has a lower stability than the active one. The loss of amino acids from the C-terminal end of the protein indirectly affects the conformation of the catalytic Glu318 residue and stability of active site because of interactions between residues at the C-terminus and the rest of protein
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Arabidopsis thaliana transformed with Agrobacterium tumefaciens
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
agriculture
when endo-beta-mannanase activity is much reduced by RNAi and antisense RNA strategies, their firmness is higher compared to those of control fruits at the turning and orange-color stages, but at the red-ripe stage firmness is similar between the two fruit-types
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Groot, S.P.C.; Kieliszewska-Rokicka, B.; Vermeer, E.; Karsson, C.M.
Gibberellin-induced hydrolysis of endosperm cell walls in gibberellin-deficient tomato seeds prior to radicle protrusion
Planta
174
500-504
1988
Solanum lycopersicum
Bewley, J.D.; Burton, R.A.; Morohashi, Y.; Fincher, G.B.
Molecular cloning of a cDNA encoding a (1->4)-beta-mannan endohydrolase from the seeds of germinated tomato (Lycopersicon esculentum)
Planta
203
454-459
1997
Solanum lycopersicum (Q8L5J1), Solanum lycopersicum
Carrington, C.M.S.; Vendrell, M.; Dominguez-Puigjaner, E.
Characterisation of an endo-(1,4)-b-mannanase (LeMAN4) expressed in ripening tomato fruit
Plant Sci.
163
599-606
2002
Solanum lycopersicum (Q8L5J1)
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Filichkin, S.A.; Leonard, J.M.; Monteros, A.; Liu, P.P.; Nonogaki, H.
A novel endo-beta-mannanase gene in tomato LeMAN5 is associated with anther and pollen development
Plant Physiol.
134
1080-1087
2004
Solanum lycopersicum (Q6YM50), Solanum lycopersicum
Schroeder, R.; Wegrzyn, T.F.; Sharma, N.N.; Atkinson, R.G.
LeMAN4 endo-beta-mannanase from ripe tomato fruit can act as a mannan transglycosylase or hydrolase
Planta
224
1091-1102
2006
Solanum lycopersicum
Bourgault, R.; Oakley, A.J.; Bewley, J.D.; Wilce, M.C.
Three-dimensional structure of (1,4)-beta-D-mannan mannanohydrolase from tomato fruit
Protein Sci.
14
1233-1241
2005
Solanum lycopersicum (Q8L5J1), Solanum lycopersicum
Li, J.; Bewley, J.D.; Hua, Z.; Zheng, W.; Wang, A.
Model and molecular dynamic simulations of active and inactive endo-beta-1,4-mannanase in tomato fruit
Protein J.
27
363-370
2008
Solanum lycopersicum (Q8L5J1), Solanum lycopersicum
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