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3.2.1.99: arabinan endo-1,5-alpha-L-arabinanase

This is an abbreviated version!
For detailed information about arabinan endo-1,5-alpha-L-arabinanase, go to the full flat file.

Word Map on EC 3.2.1.99

Reaction

alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara
+
H2O
=
alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara
+
alpha-L-arabinofuranosyl-(1-5)-O-alpha-L-arabinofuranose

Synonyms

1,5-alpha-arabinanase A, ABN, ABN A, ABN-TS, Abn1, Abn2, ABNA, abnA1, abnA2, ABNase, Abnc, AbnS1, AbnZ1, alpha-1,5-L-endo-arabinanase, alpha-L-arabinohydrolase, ARA, ARA1, araban 5-alpha-L-arabinohydrolase, arabinanase A, arabinase, endo-1,5-alpha-L-, arase, Arb43A, Arb43B, arbA, BlAbn1, CEDAase, cold-adapted endo-arabinanase, endo-(1,5)-alpha-L-arabinanase, endo-(1->5)-alpha-L-arabinanase, endo-1,5-alpha-arabinanase, endo-1,5-alpha-L-arabinanase, endo-1,5-alpha-L-arabinase, endo-1,5-alpha-L-arabinase A, endo-1,5-arabinanase, endo-1,5-arabinase, endo-ABA, endo-alpha-(1->5)-L-arabinanase, endo-alpha-1,5-arabanase, endo-alpha-1,5-L-arabinanase, endo-alpha-arabinanase, endo-ara, endo-arabanase, endo-arabinanase, endo-arabinase, endo-D-arabinase, endo-L-arabinanase, endoarabinanase, endoarabinase, GH43 arabinanase, GH43 endo-arabinanase, More, PPase-C, protopectinase C, protopectinase-C, Tpet_0637

ECTree

     3 Hydrolases
         3.2 Glycosylases
             3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
                3.2.1.99 arabinan endo-1,5-alpha-L-arabinanase

Engineering

Engineering on EC 3.2.1.99 - arabinan endo-1,5-alpha-L-arabinanase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D171A
the mutant of isoform Arb43B displays no measurable activity
D38A
the mutant of isoform Arb43B displays no measurable activity
E224A
the mutant of isoform Arb43B displays no measurable activity
H318A
the mutant of isoform Arb43B displays a drastic decrease in enzymatic activity
H318Q
D147A
site-directed mutagenesis, structure comparison with the wild-type enzyme
E201A
site-directed mutagenesis, structure comparison with the wild-type enzyme
D147A
-
site-directed mutagenesis, structure comparison with the wild-type enzyme
-
E201A
-
site-directed mutagenesis, structure comparison with the wild-type enzyme
-
D147N
inactive mutant enzyme
D27A
inactive mutant enzyme
DELTAV2-W17
H218D
the mutant shows higher catalytic efficiency, kcat is improved about 45% versus that of the wild type enzyme
H218E
the mutant is active, but it does not change the enzymatic property obviously under acidic condition compared with the wild type enzyme
H218R
-
inactive
-
H48D
-
inactive
-
H48E
-
inactive
-
H48K
-
inactive
-
H48R
-
inactive
-
additional information