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Literature summary extracted from

  • Carapito, R.; Imberty, A.; Jeltsch, J.M.; Byrns, S.C.; Tam, P.H.; Lowary, T.L.; Varrot, A.; Phalip, V.
    Molecular basis of arabinobio-hydrolase activity in phytopathogenic fungi: crystal structure and catalytic mechanism of Fusarium graminearum GH93 exo-alpha-L-arabinanase (2009), J. Biol. Chem., 284, 12285-12296.
    View publication on PubMedView publication on EuropePMC

Application

EC Number Application Comment Organism
3.2.1.55 industry alpha-L-arabinanases are essential glycosyl hydrolases participating in the complete hydrolysis of hemicellulose, a natural resource for various industrial processes, such as bioethanol or pharmaceuticals production Fusarium graminearum
3.2.1.55 synthesis alpha-L-arabinanases are essential glycosyl hydrolases participating in the complete hydrolysis of hemicellulose, a natural resource for various industrial processes, such as bioethanol or pharmaceuticals production Fusarium graminearum

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.55 gene fg03054.1, expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain TOP10 Fusarium graminearum

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.2.1.55 purified recombinant free enzyme and in complex with alpha-1,5-L-arabinobiose, hanging drop vapor diffusion method, mixing of 0.001 ml of protein solution, containing 7.8 mg/ml protein, with an equal volume of reservoir solution containing 10% PEG 20000, 100 mM Tris, pH 8.5, and 100 mM MgCl2, 20°C. Selenomethionine crystals are obtained from a solution containing 25% PEG 550 MME, 100 mM HEPES, pH 7.5, and at 11.6 mg/ml protein. The complex of selenomethionine-substituted crystals with alpha-L-arabinobiose is obtained from 22% PEG 4000, 100 mM HEPES, pH 7.5, and 50 mM ammonium sulfate, for 2 h at room temperature mixed with 1 mM alpha-methyl-1,5-arabinotetraose, the precursor of alpha-1,5-L-arabinose. X-ray diffraction structure determination and analysis at 1.85 A and 2.05 A resolution, respectively Fusarium graminearum

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.55 E170A site-directed mutagenesis of a catalytic residue, inactive mutant Fusarium graminearum
3.2.1.55 E242A site-directed mutagenesis of a catalytic residue, the mutant shows 7% of wild-type enzyme activity Fusarium graminearum
3.2.1.55 Y337A site-directed mutagenesis of a catalytic residue, inactive mutant Fusarium graminearum

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.55 additional information
-
 additional information kinetics Fusarium graminearum
3.2.1.55 2.03
-
 alpha-1,5-L-arabinohexaose pH 5.0, 40°C, wild-type enzyme Fusarium graminearum
3.2.1.55 3.56
-
 alpha-1,5-L-arabinotriose pH 5.0, 40°C, wild-type enzyme Fusarium graminearum
3.2.1.55 3.96
-
 alpha-1,5-L-arabinopentaose pH 5.0, 40°C, wild-type enzyme Fusarium graminearum
3.2.1.55 9.26
-
 alpha-1,5-L-arabinotetraose pH 5.0, 40°C, wild-type enzyme Fusarium graminearum

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.2.1.55 alpha-L-arabinan + H2O Fusarium graminearum the enzyme is highly active and displays a strict substrate specificity for linear alpha-1,5-L-arabinan alpha-1,5-L-arabinobiose + ? the enzyme releases alpha-1,5-L-arabinobiose from the nonreducing end of the polysaccharide ?

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.55 Fusarium graminearum
-
 gene fg03054.1
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.55 recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain TOP10 by metal affinity and anion exchange chromatography Fusarium graminearum

Reaction

EC Number Reaction Comment Organism Reaction ID
3.2.1.55 1,5-alpha-L-arabinofuranohexaose + 5 H2O = 6 alpha-L-arabinofuranose catalytic mechanism and substrate binding structure, overview Fusarium graminearum
a

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.2.1.55 113
-
 substrate sugar beet arabinan Fusarium graminearum
3.2.1.55 1065
-
 substrate sugar beet debranched alpha-1,5-L-arabinan Fusarium graminearum

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.55 alpha-1,5-L-arabinohexaose + H2O
-
 Fusarium graminearum alpha-1,5-L-arabinobiose + alpha-1,5-L-arabinotetraose
-
 ?
3.2.1.55 alpha-1,5-L-arabinopentaose + H2O
-
 Fusarium graminearum alpha-1,5-L-arabinobiose + alpha-1,5-L-arabinotriose
-
 ?
3.2.1.55 alpha-1,5-L-arabinotetraose + H2O
-
 Fusarium graminearum alpha-1,5-L-arabinobiose
-
 ?
3.2.1.55 alpha-1,5-L-arabinotriose + H2O
-
 Fusarium graminearum alpha-1,5-L-arabinobiose + alpha-L-arabinose
-
 ?
3.2.1.55 alpha-L-arabinan + H2O the enzyme is highly active and displays a strict substrate specificity for linear alpha-1,5-L-arabinan Fusarium graminearum alpha-1,5-L-arabinobiose + ? the enzyme releases alpha-1,5-L-arabinobiose from the nonreducing end of the polysaccharide ?
3.2.1.55 alpha-L-arabinan + H2O
-
 Fusarium graminearum oligo-alpha-1,5-L-arabinose + ? the enzyme releases alpha-1,5-L-arabinobiose from the nonreducing end of the polysaccharide ?
3.2.1.55 additional information no activity with 4-nitrophenyl-alpha-L-arabinofuranoside, wheat arabinoxylan, and alpha-L-arabinobiose, the configuration of bound arabinobiose is consistent with the retaining mechanism proposed for the GH93 family Fusarium graminearum ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.2.1.55 monomer Arb93A has a six-bladed beta-propeller fold Fusarium graminearum

Synonyms

EC Number Synonyms Comment Organism
3.2.1.55 Arb93A
-
 Fusarium graminearum
3.2.1.55 exo-alpha-L-arabinanase
-
 Fusarium graminearum
3.2.1.55 More the enzyme belongs to the glycosylhydrolase family GH93 Fusarium graminearum

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.55 40
-
-
 Fusarium graminearum

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.2.1.55 20 60 over 80% of maximal activity at 30-50°C Fusarium graminearum

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.2.1.55 81000
-
 alpha-1,5-L-arabinopentaose pH 5.0, 40°C, wild-type enzyme Fusarium graminearum
3.2.1.55 94000
-
 alpha-1,5-L-arabinohexaose pH 5.0, 40°C, wild-type enzyme Fusarium graminearum
3.2.1.55 105000
-
 alpha-1,5-L-arabinotetraose pH 5.0, 40°C, wild-type enzyme Fusarium graminearum
3.2.1.55 113000
-
 alpha-1,5-L-arabinotriose pH 5.0, 40°C, wild-type enzyme Fusarium graminearum

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.55 5
-
-
 Fusarium graminearum

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.2.1.55 3 9 over 80% of maximal activity at pH 4.0-6.0 Fusarium graminearum

General Information

EC Number General Information Comment Organism
3.2.1.55 physiological function alpha-L-arabinanases are essential glycosyl hydrolases participating in the complete hydrolysis of hemicellulose Fusarium graminearum

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
3.2.1.55 11300
-
 alpha-1,5-L-arabinotetraose pH 5.0, 40°C, wild-type enzyme Fusarium graminearum
3.2.1.55 20500
-
 alpha-1,5-L-arabinopentaose pH 5.0, 40°C, wild-type enzyme Fusarium graminearum
3.2.1.55 31700
-
 alpha-1,5-L-arabinotriose pH 5.0, 40°C, wild-type enzyme Fusarium graminearum
3.2.1.55 46600
-
 alpha-1,5-L-arabinohexaose pH 5.0, 40°C, wild-type enzyme Fusarium graminearum