KEGG   ENZYME: 3.2.1.178
Entry
EC 3.2.1.178                Enzyme                                 
Name
beta-porphyranase;
porphyranase;
PorA;
PorB;
endo-beta-porphyranase
Class
Hydrolases;
Glycosylases;
Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
Sysname
porphyran beta-D-galactopyranose-(1->4)-alpha-L-galactopyranose-6-sulfate 4-glycanohydrolase
Reaction(IUBMB)
Hydrolysis of beta-D-galactopyranose-(1->4)-alpha-L-galactopyranose-6-sulfate linkages in porphyran
Comment
The backbone of porphyran consists largely (~70%) of (1->3)-linked beta-D-galactopyranose followed by (1->4)-linked alpha-L-galactopyranose-6-sulfate [the other 30% are mostly agarobiose repeating units of (1->3)-linked beta-D-galactopyranose followed by (1->4)-linked 3,6-anhydro-alpha-L-galactopyranose] [2]. This enzyme cleaves the (1->4) linkages between beta-D-galactopyranose and alpha-L-galactopyranose-6-sulfate, forming mostly the disaccharide alpha-L-galactopyranose-6-sulfate-(1->3)-beta-D-galactose, although some longer oligosaccharides of even number of residues are also observed. Since the enzyme is inactive on the non-sulfated agarose portion of the porphyran backbone, some agarose fragments are also included in the products [1]. Methylation of the D-galactose prevents the enzyme from Zobellia galactanivorans, but not that from Wenyingzhuangia fucanilytica, from binding at subsite -1 [2,3].
History
EC 3.2.1.178 created 2011
Orthology
K20830  beta-porphyranase
Genes
ASPAOR13_2899
GAGGlaag_3504
PMESFX988_00193
PATPatl_0824
CATEC2869_16030
CATTOLW01_01220 OLW01_17615
CAACaka_0379 Caka_0490 Caka_0603 Caka_0895
VBSEGM51_03300 EGM51_04175
SNEPEnr13x_06970(porB)
PHMPSMK_17630
BUNBun01g_38460
MBASALGA_0084 ALGA_2781
ESTDN752_05265
REKN6H18_16970 N6H18_17100 N6H18_17105
RCGN7E81_10815
PRHOPZB74_15175
GFOGFO_1715
FFAFFWV33_14465 FFWV33_15045 FFWV33_15300
MARMYQ22_01860 YQ22_01900
CAOCelal_2477
CLYCelly_0432 Celly_0436 Celly_2273
CLHIX49_01860 IX49_01880 IX49_11345
CBALM667_09700 M667_09735 M667_13010
CBATM666_09625 M666_09665 M666_12860
COMNPBN93_02200 PBN93_11280
ZGAZOBELLIA_1017(porB) ZOBELLIA_2600(porA) ZOBELLIA_3376(porC) ZOBELLIA_3628(porD) ZOBELLIA_3640(porE)
ZLAQ5W13_24420
PRNBW723_04065 BW723_04095 BW723_04315
TJETJEJU_3809 TJEJU_3841
WFUAXE80_06925 AXE80_06935
FEKC1H87_18395 C1H87_21200
AQBD1818_05000 D1818_13685 D1818_21455
AQAD1815_10455
AQDD1816_05305 D1816_11795
AQENBT05_07425
FBEFF125_18390 FF125_18530
 » show all
Reference
1  [PMID:20376150]
  Authors
Hehemann JH, Correc G, Barbeyron T, Helbert W, Czjzek M, Michel G
  Title
Transfer of carbohydrate-active enzymes from marine bacteria to Japanese gut microbiota.
  Journal
Nature 464:908-12 (2010)
DOI:10.1038/nature08937
  Sequence
Reference
2
  Authors
Correc, G., Hehemann, J.H., Czjzek, M. and Helbert, W.
  Title
Structural analysis of the degradation products of porphyran digested by Zobellia galactanivorans beta-porphyranase A.
  Journal
Carbohydrate Polymers 83:277-283 (2011)
Reference
3  [PMID:32520542]
  Authors
Zhang Y, Chang Y, Shen J, Mei X, Xue C.
  Title
Characterization of a Novel Porphyranase Accommodating Methyl-galactoses at Its Subsites.
  Journal
J Agric Food Chem 68:7032-7039 (2020)
DOI:10.1021/acs.jafc.0c02404
Other DBs
ExplorEnz - The Enzyme Database: 3.2.1.178
IUBMB Enzyme Nomenclature: 3.2.1.178
ExPASy - ENZYME nomenclature database: 3.2.1.178
BRENDA, the Enzyme Database: 3.2.1.178

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