Glycoside Hydrolase Family 49 - Revision history

Takatsugu Miyazaki at 09:19, 30 September 2025

2025-09-30T09:19:03Z

Takatsugu Miyazaki at 09:14, 30 September 2025

2025-09-30T09:14:54Z

Takatsugu Miyazaki at 09:09, 30 September 2025

2025-09-30T09:09:33Z

Takatsugu Miyazaki at 09:07, 30 September 2025

2025-09-30T09:07:38Z

Takatsugu Miyazaki at 08:50, 30 September 2025

2025-09-30T08:50:57Z

Takatsugu Miyazaki at 03:08, 14 April 2023

2023-04-14T03:08:30Z

Takatsugu Miyazaki at 03:05, 14 April 2023

2023-04-14T03:05:21Z

Takatsugu Miyazaki at 08:00, 13 April 2023

2023-04-13T08:00:20Z

Harry Brumer: added User:Takatsugu Miyazaki as co-author, according to email request from User:Takashi Tonozuka

2023-01-10T15:50:02Z

added User:Takatsugu Miyazaki as co-author, according to email request from User:Takashi Tonozuka

Harry Brumer: Text replacement - "\^\^\^(.*)\^\^\^" to "$1"

2021-12-18T21:17:16Z

Text replacement - "\^\^\^(.*)\^\^\^" to "$1"

@@ Line 29: / Line 29: @@
 == Substrate specificities ==
-[[File:Fig1_GH49_substrates.png|thumb|300px|right|'''Figure 1. Substrates of GH49 enzymes.''' All enzymes except dextran 1,6-&alpha;-isomaltotriosidase are endo-acting glycoside hydrolases. Sulfated arabinan contains sulfate groups at 2- and 3-OH (3S) of L-arabinopyranose residue and possesses side chains of galactose and xylose, which are not shown in this figure.]]
+[[File:Fig1_GH49_substrates.png|thumb|600px|right|'''Figure 1. Substrates of GH49 enzymes.''' All enzymes except dextran 1,6-&alpha;-isomaltotriosidase are endo-acting glycoside hydrolases. Sulfated arabinan contains sulfate groups at 2- and 3-OH (3S) of L-arabinopyranose residue and possesses side chains of galactose and xylose, which are not shown in this figure.]]
 [[Glycoside hydrolases]] of GH49 cleave &alpha;-(1→6)-glucosidic linkages or &alpha;-(1→4)-glucosidic linkages of polysaccharides and oligosaccharides containing &alpha;-(1→6)-glucosidic linkages, such as dextran and pullulan. The major activities reported for this family of glycoside hydrolases are dextranase (EC [{{EClink}}3.2.1.11 3.2.1.11]), and a dextranase from ''Talaromyces minioluteum'' (formerly known as ''Penicillium minioluteum''), Dex49A, is currently the most characterized enzyme. GH49 dextranases have been found in some bacteria and fungi. Dextran 1,6-&alpha;-isomaltotriosidase (EC [{{EClink}}3.2.1.95 3.2.1.95]) from ''Brevibacterium fuscum'' var. ''dextranlyticum'' is an exo-acting enzyme that hydrolyzes dextran from the non-reducing ends to produce isomaltotriose <cite>Mizuno1999</cite>. Isopullulanase (EC [{{EClink}}3.2.1.57 3.2.1.57])from ''Aspergillus brasiliensis'' ATCC 9642 (formerly ''Aspergillus niger'' ATCC 9642) hydrolyzes α-(1→4)-linkages of pullulan to produce isopanose <cite>Sakano1971</cite>. 4-''O''-&alpha;-D-Isomaltooligosaccharylmaltooligosaccharide 1,4-&alpha;-isomaltooligosaccharohydrolase (IMM-4IH, EC 3.2.1.-) from ''Sarocladium kiliense'' possesses more strict substrate specificity than isopullulanase and cannot hydrolyze pullulan <cite>Kitagawa2023</cite>. As an exception, endo-acting sulfated-arabinan hydrolase (EC 3.2.1-) from ''Phocaeicola plebeius'' degrades sulfated arabinan produced by green algae ''Chaetomorpha'' sp. and ''Cladophora'' sp. <cite>Helbert2019</cite>.
@@ Line 40: / Line 40: @@
 == Three-dimensional structures ==
-[[File:Fig2_GH49_structures.png|thumb|600px|center|'''Figure 2. Overall structures of GH49 enzymes.''' (Left to right) ''Aspergillus brasiliensis'' isopullulanase (IPU) in complex with isopanose (PDB ID [{{PDBlink}}2z8g 2Z8G]), ''Talaromyces minioluteum'' dextranase (Dex49A) in complex with isomaltose (PDB ID [{{PDBlink}}1ogm 1OGM]), and ''Arthrobacter oxydans'' dextranase (AoDex) (PDB ID [{{PDBlink}}6nzs 6NZS]).]]
+[[File:Fig2_GH49_structures.png|thumb|800px|center|'''Figure 2. Overall structures of GH49 enzymes.''' (Left to right) ''Aspergillus brasiliensis'' isopullulanase (IPU) in complex with isopanose (PDB ID [{{PDBlink}}2z8g 2Z8G]), ''Talaromyces minioluteum'' dextranase (Dex49A) in complex with isomaltose (PDB ID [{{PDBlink}}1ogm 1OGM]), and ''Arthrobacter oxydans'' dextranase (AoDex) (PDB ID [{{PDBlink}}6nzs 6NZS]).]]
-[[File:Fig3_GH49_activesites.png|thumb|300px|right|'''Figure 3. Active sites of GH49 enzymes.''' (A-C) Molecular surfaces of Dex49A (A), IPU (B), and AoDex (C) are shown in gray. Amino acid residues and ligands are shown as stick models: catalytic residues, slate blue; residues forming active site clefts: yellow (C-terminal domain) and pink (N-terminal domain); isomaltose and isopanose, green. In (B), the isomaltose molecule (dark green) bound in N448A variant of IPU (PDB ID [{{PDBlink}}3WWG 3WWG] <cite>Miyazaki2015</cite>) is superimposed. (D) The superimposition of the catalytic residues of the three GH49 enzymes. Water molecules interacting with two general base candidates (asterisk) are shown as red sphere.]]
+[[File:Fig3_GH49_activesites.png|thumb|600px|right|'''Figure 3. Active sites of GH49 enzymes.''' (A-C) Molecular surfaces of Dex49A (A), IPU (B), and AoDex (C) are shown in gray. Amino acid residues and ligands are shown as stick models: catalytic residues, slate blue; residues forming active site clefts: yellow (C-terminal domain) and pink (N-terminal domain); isomaltose and isopanose, green. In (B), the isomaltose molecule (dark green) bound in N448A variant of IPU (PDB ID [{{PDBlink}}3WWG 3WWG] <cite>Miyazaki2015</cite>) is superimposed. (D) The superimposition of the catalytic residues of the three GH49 enzymes. Water molecules interacting with two general base candidates (asterisk) are shown as red sphere.]]
 Three structures of GH49 enzymes are available so far <cite>Larsson2003 Mizuno2008 Ren2019</cite>, and they display a two-domain structure. The N-terminal domain is a &beta;-sandwich and the C-terminal domain adopts a right-handed parallel &beta;-helix. Although GH49, [[GH28]], [[GH87]], and [[GH110]] families contain enzymes with distinct substrate specificities and exhibit low overall sequence homology, they share similar &beta;-helix folds and the three catalytic Asp residues are completely conserved <cite>Larsson2003 Mizuno2008 Itoh2020 McGuire2020</cite>. Each coil forming the cylindrical &beta;-helix fold is composed of three &beta;-sheets, which are named PB1, PB2, and PB3, following the original definition for a PL1 enzyme, pectate lyase C <cite>Yoder1993</cite>.

@@ Line 31: / Line 31: @@
 [[File:Fig1_GH49_substrates.png|thumb|300px|right|'''Figure 1. Substrates of GH49 enzymes.''' All enzymes except dextran 1,6-&alpha;-isomaltotriosidase are endo-acting glycoside hydrolases. Sulfated arabinan contains sulfate groups at 2- and 3-OH (3S) of L-arabinopyranose residue and possesses side chains of galactose and xylose, which are not shown in this figure.]]
-[[Glycoside hydrolases]] of GH49 cleave &alpha;-(1→6)-glucosidic linkages or &alpha;-(1→4)-glucosidic linkages of polysaccharides and oligosaccharides containing &alpha;-(1→6)-glucosidic linkages, such as dextran and pullulan. The major activities reported for this family of glycoside hydrolases are dextranase (EC [{{EClink}}3.2.1.11 3.2.1.11]), and a dextranase from ''Talaromyces minioluteum'' (formerly known as ''Penicillium minioluteum''), Dex49A, is currently the most characterized enzyme. GH49 dextranases have been found in some bacteria and fungi. Dextran 1,6-&alpha;-isomaltotriosidase (EC [{{EClink}}3.2.1.95 3.2.1.95]) from ''Brevibacterium fuscum'' var. ''dextranlyticum'' is an exo-acting enzyme that hydrolyzes dextran from the non-reducing ends to produce isomaltotriose <cite>Mizuno1999</cite>. Isopullulanase (EC [{{EClink}}3.2.1.57 3.2.1.57])from ''Aspergillus brasiliensis'' ATCC 9642 (formerly ''Aspergillus niger'' ATCC 9642) hydrolyzes α-(1→4)-linkages of pullulan to produce isopanose <cite>Sakano1971</cite>. 4-''O''-&alpha;-D-Isomaltooligosaccharylmaltooligosaccharide 1,4-&alpha;-isomaltooligosaccharohydrolase (EC 3.2.1.-) from ''Sarocladium kiliense'' possesses more strict substrate specificity than isopullulanase and cannot hydrolyze pullulan <cite>Kitagawa2023</cite>. As an exception, endo-acting sulfated-arabinan hydrolase (EC 3.2.1-) from ''Phocaeicola plebeius'' degrades sulfated arabinan produced by green algae ''Chaetomorpha'' sp. and ''Cladophora'' sp. <cite>Helbert2019</cite>.
+[[Glycoside hydrolases]] of GH49 cleave &alpha;-(1→6)-glucosidic linkages or &alpha;-(1→4)-glucosidic linkages of polysaccharides and oligosaccharides containing &alpha;-(1→6)-glucosidic linkages, such as dextran and pullulan. The major activities reported for this family of glycoside hydrolases are dextranase (EC [{{EClink}}3.2.1.11 3.2.1.11]), and a dextranase from ''Talaromyces minioluteum'' (formerly known as ''Penicillium minioluteum''), Dex49A, is currently the most characterized enzyme. GH49 dextranases have been found in some bacteria and fungi. Dextran 1,6-&alpha;-isomaltotriosidase (EC [{{EClink}}3.2.1.95 3.2.1.95]) from ''Brevibacterium fuscum'' var. ''dextranlyticum'' is an exo-acting enzyme that hydrolyzes dextran from the non-reducing ends to produce isomaltotriose <cite>Mizuno1999</cite>. Isopullulanase (EC [{{EClink}}3.2.1.57 3.2.1.57])from ''Aspergillus brasiliensis'' ATCC 9642 (formerly ''Aspergillus niger'' ATCC 9642) hydrolyzes α-(1→4)-linkages of pullulan to produce isopanose <cite>Sakano1971</cite>. 4-''O''-&alpha;-D-Isomaltooligosaccharylmaltooligosaccharide 1,4-&alpha;-isomaltooligosaccharohydrolase (IMM-4IH, EC 3.2.1.-) from ''Sarocladium kiliense'' possesses more strict substrate specificity than isopullulanase and cannot hydrolyze pullulan <cite>Kitagawa2023</cite>. As an exception, endo-acting sulfated-arabinan hydrolase (EC 3.2.1-) from ''Phocaeicola plebeius'' degrades sulfated arabinan produced by green algae ''Chaetomorpha'' sp. and ''Cladophora'' sp. <cite>Helbert2019</cite>.
 == Kinetics and Mechanism ==

@@ Line 43: / Line 43: @@
-[[File:Fig3_GH49_activesites.png|thumb|300px|right|'''Figure 3. Active sites of GH49 enzymes.''' (A-C) Molecular surfaces of Dex49A (A), IPU (B), and AoDex (C) are shown in gray. Amino acid residues and ligands are shown as stick models: catalytic residues, slate blue; residues forming active site clefts: yellow (C-terminal domain) and pink (N-terminal domain); isomaltose and isopanose, green. In (B), the isomaltose molecule (dark green) bound in N448A variant of IPU (PDB ID [{{PDBlink}}3WWG 3WWG]) is superimposed. (D) The superimposition of the catalytic residues of the three GH49 enzymes. Water molecules interacting with two general base candidates (asterisk) are shown as red sphere.]]
+[[File:Fig3_GH49_activesites.png|thumb|300px|right|'''Figure 3. Active sites of GH49 enzymes.''' (A-C) Molecular surfaces of Dex49A (A), IPU (B), and AoDex (C) are shown in gray. Amino acid residues and ligands are shown as stick models: catalytic residues, slate blue; residues forming active site clefts: yellow (C-terminal domain) and pink (N-terminal domain); isomaltose and isopanose, green. In (B), the isomaltose molecule (dark green) bound in N448A variant of IPU (PDB ID [{{PDBlink}}3WWG 3WWG] <cite>Miyazaki2015</cite>) is superimposed. (D) The superimposition of the catalytic residues of the three GH49 enzymes. Water molecules interacting with two general base candidates (asterisk) are shown as red sphere.]]
 Three structures of GH49 enzymes are available so far <cite>Larsson2003 Mizuno2008 Ren2019</cite>, and they display a two-domain structure. The N-terminal domain is a &beta;-sandwich and the C-terminal domain adopts a right-handed parallel &beta;-helix. Although GH49, [[GH28]], [[GH87]], and [[GH110]] families contain enzymes with distinct substrate specificities and exhibit low overall sequence homology, they share similar &beta;-helix folds and the three catalytic Asp residues are completely conserved <cite>Larsson2003 Mizuno2008 Itoh2020 McGuire2020</cite>. Each coil forming the cylindrical &beta;-helix fold is composed of three &beta;-sheets, which are named PB1, PB2, and PB3, following the original definition for a PL1 enzyme, pectate lyase C <cite>Yoder1993</cite>.
@@ Line 66: / Line 66: @@
 #Sakano1971 Sakano Y, Masuda N, and Kobayashi T. (1971). ''Hydrolysis of Pullulan by a Novel Enzyme from Aspergillus niger'', ''Agric Biol Chem'' 1971;35(6):971-973. https://doi.org/10.1271/bbb1961.35.971
 #Helbert2019 pmid=30850540
 #Ren2019 pmid=30919632
 #Itoh2020 pmid=31788942

@@ Line 29: / Line 29: @@
 == Substrate specificities ==
-[[Glycoside hydrolases]] of GH49 cleave &alpha;-(1→6)-glucosidic linkages or &alpha;-(1→4)-glucosidic linkages of polysaccharides and oligosaccharides containing &alpha;-(1→6)-glucosidic linkages, such as dextran and pullulan. The major activities reported for this family of glycoside hydrolases are dextranase (EC [{{EClink}}3.2.1.11 3.2.1.11]), and a dextranase from ''Talaromyces minioluteum'' (formerly known as ''Penicillium minioluteum''), Dex49A, is currently the most characterized enzyme. GH49 dextranases have been found in some bacteria and fungi. Dextran 1,6-&alpha;-isomaltotriosidase (EC [{{EClink}}3.2.1.95 3.2.1.95]) from ''Brevibacterium fuscum'' var. ''dextranlyticum'' is an exo-acting enzyme that hydrolyzes dextran from the non-reducing ends to produce isomaltotriose <cite>Mizuno1999</cite>. Isopullulanase (EC [{{EClink}}3.2.1.57 3.2.1.57])from ''Aspergillus brasiliensis'' ATCC 9642 (formerly ''Aspergillus niger'' ATCC 9642) hydrolyzes α-(1→4)-linkages of pullulan to produce isopanose <cite>Sakano1971</cite>. 4-O-&alpha;-D-Isomaltooligosaccharylmaltooligosaccharide 1,4-&alpha;-isomaltooligosaccharohydrolase (EC 3.2.1.-) from ''Sarocladium kiliense'' possesses more strict substrate specificity than isopullulanase and cannot hydrolyze pullulan <cite>Kitagawa2023</cite>. As an exception, endo-acting sulfated-arabinan hydrolase (EC 3.2.1-) from ''Phocaeicola plebeius'' degrades sulfated arabinan produced by green algae ''Chaetomorpha'' sp. and ''Cladophora'' sp. <cite>Helbert2019</cite>.
+[[File:Fig1_GH49_substrates.png|thumb|300px|right|'''Figure 1. Substrates of GH49 enzymes.''' All enzymes except dextran 1,6-&alpha;-isomaltotriosidase are endo-acting glycoside hydrolases. Sulfated arabinan contains sulfate groups at 2- and 3-OH (3S) of L-arabinopyranose residue and possesses side chains of galactose and xylose, which are not shown in this figure.]]
 == Kinetics and Mechanism ==
@@ Line 38: / Line 40: @@
 == Three-dimensional structures ==
 Three structures of GH49 enzymes are available so far <cite>Larsson2003 Mizuno2008 Ren2019</cite>, and they display a two-domain structure. The N-terminal domain is a &beta;-sandwich and the C-terminal domain adopts a right-handed parallel &beta;-helix. Although GH49, [[GH28]], [[GH87]], and [[GH110]] families contain enzymes with distinct substrate specificities and exhibit low overall sequence homology, they share similar &beta;-helix folds and the three catalytic Asp residues are completely conserved <cite>Larsson2003 Mizuno2008 Itoh2020 McGuire2020</cite>. Each coil forming the cylindrical &beta;-helix fold is composed of three &beta;-sheets, which are named PB1, PB2, and PB3, following the original definition for a PL1 enzyme, pectate lyase C <cite>Yoder1993</cite>.

@@ Line 29: / Line 29: @@
 == Substrate specificities ==
-[[Glycoside hydrolases]] of family 49 cleave &alpha;-1,6-glucosidic linkages or &alpha;-1,4-glucosidic linkages of polysaccharides containing &alpha;-1,6-glucosidic linkages, dextran and pullulan. The major activities reported for this family of glycoside hydrolases are dextranase (EC [{{EClink}}3.2.1.11 3.2.1.11]), and a dextranase from ''Talaromyces minioluteum'' (formerly known as ''Penicillium minioluteum''), Dex49A, is currently the most characterized enzyme. Dextran 1,6-&alpha;-isomaltotriosidase (EC [{{EClink}}3.2.1.95 3.2.1.95]) <cite>Mizuno1999</cite>, isopullulanase (EC [{{EClink}}3.2.1.57 3.2.1.57]) <cite>Sakano1971</cite>, endo-acting sulfated-arabinan hydrolase (EC 3.2.1-) <cite>Helbert2019</cite>, and 4-''O''-α-D-isomaltooligosaccharylmaltooligosaccharide 1,4-α-isomaltooligosaccharohydrolase (EC 3.2.1.-) <cite>Kitagawa2023</cite> have also been described.
+[[Glycoside hydrolases]] of GH49 cleave &alpha;-(1→6)-glucosidic linkages or &alpha;-(1→4)-glucosidic linkages of polysaccharides and oligosaccharides containing &alpha;-(1→6)-glucosidic linkages, such as dextran and pullulan. The major activities reported for this family of glycoside hydrolases are dextranase (EC [{{EClink}}3.2.1.11 3.2.1.11]), and a dextranase from ''Talaromyces minioluteum'' (formerly known as ''Penicillium minioluteum''), Dex49A, is currently the most characterized enzyme. GH49 dextranases have been found in some bacteria and fungi. Dextran 1,6-&alpha;-isomaltotriosidase (EC [{{EClink}}3.2.1.95 3.2.1.95]) from ''Brevibacterium fuscum'' var. ''dextranlyticum'' is an exo-acting enzyme that hydrolyzes dextran from the non-reducing ends to produce isomaltotriose <cite>Mizuno1999</cite>. Isopullulanase (EC [{{EClink}}3.2.1.57 3.2.1.57])from ''Aspergillus brasiliensis'' ATCC 9642 (formerly ''Aspergillus niger'' ATCC 9642) hydrolyzes α-(1→4)-linkages of pullulan to produce isopanose <cite>Sakano1971</cite>. 4-O-&alpha;-D-Isomaltooligosaccharylmaltooligosaccharide 1,4-&alpha;-isomaltooligosaccharohydrolase (EC 3.2.1.-) from ''Sarocladium kiliense'' possesses more strict substrate specificity than isopullulanase and cannot hydrolyze pullulan <cite>Kitagawa2023</cite>. As an exception, endo-acting sulfated-arabinan hydrolase (EC 3.2.1-) from ''Phocaeicola plebeius'' degrades sulfated arabinan produced by green algae ''Chaetomorpha'' sp. and ''Cladophora'' sp. <cite>Helbert2019</cite>.
 == Kinetics and Mechanism ==
-Family GH49 &alpha;-glycosidases are [[inverting]] enzymes, as first shown by NMR on a dextranase Dex49A from ''Talaromyces minioluteum'' <cite>Larsson2003</cite> .
+Family GH49 &alpha;-glycosidases are [[inverting]] enzymes, as first shown by NMR on a dextranase Dex49A from ''Talaromyces minioluteum'' <cite>Larsson2003</cite> . Optical rotation analysis of the hydrolysis of panose by isopullulanase supported the inverting mechanism <cite>Akeboshi2004</cite>.
 == Catalytic Residues ==
-Three Asp residues (Asp376, Asp395, and Asp396 in Dex49A) are conserved in the catalytic centre of members of clan GH-N, GH49 and [[GH28]] enzymes <cite>Larsson2003 Mizuno2008</cite>, and all three of the Asp mutants of a GH49 enzyme, isopullulanase, lost their activities <cite>Akeboshi2004</cite>. The [[general acid]] was first identified in Dex49A from ''Talaromyces minioluteum'' as Asp395 following the three-dimensional structure determination. To date, it is unclear whether either (or both) of the Asp residues (Asp376 and Asp396 in Dex49A) acts as a [[general base]] in the reaction of GH49 and [[GH28]] enzymes <cite>Larsson2003 vanSanten1999 Shimizu2002</cite>.
+Three Asp residues (Asp376, Asp395, and Asp396 in Dex49A) are conserved in the catalytic center of clan GH-N members, GH49 and [[GH28]] enzymes <cite>Larsson2003 Mizuno2008</cite>, which is also the case for [[GH87]] and [[GH110]]. All three of the Asp mutants of ''A. brasiliensis'' isopullulanase, lost their activities <cite>Akeboshi2004</cite>. The [[general acid]] was first identified in Dex49A from ''Talaromyces minioluteum'' as Asp395 following the three-dimensional structure determination. To date, it is unclear whether either (or both) of the Asp residues (Asp376 and Asp396 in Dex49A) acts as a [[general base]] in the reaction of GH49 and [[GH28]] enzymes <cite>Larsson2003 vanSanten1999 Shimizu2002</cite>.
 == Three-dimensional structures ==
-Two structures of GH49 enzymes are available so far <cite>Larsson2003 Mizuno2008</cite>, and they display a two domain structure. The N-terminal domain is a &beta;-sandwich and the C-terminal domain adopts a right-handed parallel &beta;-helix. The similarity of the &beta;-helix fold between GH49 and [[GH28]] enzymes has been described, although almost none of the amino acid residues other than the three catalytic Asp residues is conserved between the two families <cite>Larsson2003 Mizuno2008</cite>. Each coil forming the cylindrical &beta;-helix fold is composed of three &beta;-sheets, which are named PB1, PB2, and PB3, following the original definition for a PL1 enzyme, pectate lyase C <cite>Yoder1993</cite>.
+Three structures of GH49 enzymes are available so far <cite>Larsson2003 Mizuno2008 Ren2019</cite>, and they display a two-domain structure. The N-terminal domain is a &beta;-sandwich and the C-terminal domain adopts a right-handed parallel &beta;-helix. Although GH49, [[GH28]], [[GH87]], and [[GH110]] families contain enzymes with distinct substrate specificities and exhibit low overall sequence homology, they share similar &beta;-helix folds and the three catalytic Asp residues are completely conserved <cite>Larsson2003 Mizuno2008 Itoh2020 McGuire2020</cite>. Each coil forming the cylindrical &beta;-helix fold is composed of three &beta;-sheets, which are named PB1, PB2, and PB3, following the original definition for a PL1 enzyme, pectate lyase C <cite>Yoder1993</cite>.
 == Family Firsts ==
 ;First gene cloning: Dextranase from ''Arthrobacter'' sp. CB-8 <cite>Okushima1991</cite>.
-;First sterochemistry determination: Dextranase (Dex49A) from ''Talaromyces minioluteum'' <cite>Larsson2003</cite>.
+;First stereochemistry determination: Dextranase (Dex49A) from ''Talaromyces minioluteum'' <cite>Larsson2003</cite>.
 ;First general acid residue identification: Dextranase (Dex49A) from ''Talaromyces minioluteum'' <cite>Larsson2003</cite>.
-;First 3-D structure: Dextranase (Dex49A) from ''Talaromyces minioluteum'' by X-ray crystallography (PDB ID [{{PDBlink}}1ogm 1ogm]) <cite>Larsson2003</cite>.
+;First 3-D structure: Dextranase (Dex49A) from ''Talaromyces minioluteum'' by X-ray crystallography (PDB ID [{{PDBlink}}1ogm 1OGM]) <cite>Larsson2003</cite>.
 == References ==
@@ Line 58: / Line 59: @@
 #Sakano1971 Sakano Y, Masuda N, and Kobayashi T. (1971). ''Hydrolysis of Pullulan by a Novel Enzyme from Aspergillus niger'', ''Agric Biol Chem'' 1971;35(6):971-973. https://doi.org/10.1271/bbb1961.35.971
 #Helbert2019 pmid=30850540
+#Ren2019 pmid=30919632
 #Kitagawa2023 pmid=36592961

@@ Line 29: / Line 29: @@
 == Substrate specificities ==
-[[Glycoside hydrolases]] of family 49 cleave &alpha;-1,6-glucosidic linkages or &alpha;-1,4-glucosidic linkages of polysaccharides containing &alpha;-1,6-glucosidic linkages, dextran and pullulan. The major activities reported for this family of glycoside hydrolases are dextranase (EC [{{EClink}}3.2.1.11 3.2.1.11]), and a dextranase from ''Penicillium minioluteum'', Dex49A, is currently the most characterised enzyme. Dextran 1,6-&alpha;-isomaltotriosidase (EC [{{EClink}}3.2.1.95 3.2.1.95]) <cite>Mizuno1999</cite> and isopullulanase (EC [{{EClink}}3.2.1.57 3.2.1.57]) activities have also been described.
+[[Glycoside hydrolases]] of family 49 cleave &alpha;-1,6-glucosidic linkages or &alpha;-1,4-glucosidic linkages of polysaccharides containing &alpha;-1,6-glucosidic linkages, dextran and pullulan. The major activities reported for this family of glycoside hydrolases are dextranase (EC [{{EClink}}3.2.1.11 3.2.1.11]), and a dextranase from ''Talaromyces minioluteum'' (formerly known as ''Penicillium minioluteum''), Dex49A, is currently the most characterized enzyme. Dextran 1,6-&alpha;-isomaltotriosidase (EC [{{EClink}}3.2.1.95 3.2.1.95]) <cite>Mizuno1999</cite>, isopullulanase (EC [{{EClink}}3.2.1.57 3.2.1.57]) <cite>Sakano1971</cite>, endo-acting sulfated-arabinan hydrolase (EC 3.2.1-) <cite>Helbert2019</cite>, and 4-O-α-D-isomaltooligosaccharylmaltooligosaccharide 1,4-α-isomaltooligosaccharohydrolase (EC 3.2.1.-) <cite>Kitagawa2023</cite> have also been described.
 == Kinetics and Mechanism ==
@@ Line 56: / Line 56: @@
 #Yoder1993 pmid=8502994
 #Okushima1991 pmid=1859672
 </biblio>
 [[Category:Glycoside Hydrolase Families|GH049]]

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 <!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption -->
 {{CuratorApproved}}
-* [[Author]]: [[User:Takashi Tonozuka|Takashi Tonozuka]]
+* [[Author]]: [[User:Takashi Tonozuka|Takashi Tonozuka]] and [[User:Takatsugu Miyazaki|Takatsugu Miyazaki]]
 * [[Responsible Curator]]:  [[User:Takashi Tonozuka|Takashi Tonozuka]]
 ----
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 {| {{Prettytable}}
 |-
-|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GHnn'''
+|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH49'''
 |-
 |'''Clan'''