Draft Glycosci Factsheet - Glycosidases

Iain Wilson wilson at edv1.boku.ac.at
Mon May 22 12:54:29 EST 1995

Not being at the Wiener Staatsoper or elsewhere this evening - I thought
I would get round to posting the following:

Dear All,
  As part of the GLYCOSCI newsgroup's original charter, it was hoped 
to create a series of factsheets and other Internet accessible 
resources - indeed a number of people have set up 'glycoscience' 
related WWW pages and presumably that number will grow. I have 
already posted a draft list of cloned glycosyltransferases - that is 
now on the WWW (see separate annoucement). The list below is of 
glycosidase specificities.
  This list is probably highly incomplete, not definitive, not fully 
referenced, and possibly controversial. I post it here so that when 
it finally appears on the WWW it will be, hopefully, as accurate as 
possible. The information is based on papers I have come across 
myself and also from laboratory knowledge I have gained, particularly 
when at the Oxford Glycobiology Institute. There is also a useful article 
in "Glycobiology: A Practical Approach" by Kobata and Takasaki (IRL 
Press, ISBN 0-19-963372-X). I have only included information of relevance to
N- and O- linked oligosaccharides. Others may wish to contribute information
on GPI or proteoglycan structures.
   I am sure there are a large number of people out there with 
experience of glycosidases who can add information to this list - 
please send any corrections, comments, etc to me at wilson at edv1.boku.ac.at
  I do not intend to prepare any more "factsheets" of this type - but 
hope anyone out there with the time and inclination will think of 
more suitable subjects for such treatment. Such factsheet preparation 
can be done in consultation with the discussion leaders. I can think 
of lectins in particular being an important area. I am sure there are 
many areas where pooling of knowledge will help newcomers and well 
established researchers in the field alike.



(Cleave between the two GlcNA residues of the chitobiose core of 
N-linked oligosaccharides: General reference: Maley et al. 
(1989) Anal. Biochem. 180:195-204)

Enzyme:         Endoglucosaminidase CII
Specificity:    Similar to Endo H (see below) but apparently
                requires an alpha 1,3 linked mannose
                to be attached to the beta-linked mannose
                (Tai et al (1977) BBRC 78:434-441)

Enzyme:         Endoglucosaminidase D
Specificity:    Can cleave Man5GlcNAc2Asn and branched 
                Man3GlcNAc2Asn, but reduced activity 
                with Man6GlcNAc2Asn and Man5GlcNAc2-ol

Enzyme:         Endoglucosaminidase F
Specificity:    Will cleave (at varying rates) a wide range of
                structures, including the branched trimannosyl
                core (unlike Endo H) and biantennary complex
                oligosaccharides (again unlike Endo H)

Enzyme:         Endoglucosaminidase H (Endo H)
Specificity:    Trimannosylchitobiose (minimum) (providing
                that there is at least one mannose 
                linked to the alpha 1,6 linked mannose;
                the alpha 1,3 linked mannose is not required;
                can cleave alpha 1,6 core fucosylated hybrid 
                structures but not complex N-linked
Enzyme:         Endoglucosaminidase L
Specificity:    Beta-mannosylchitobiose (trisaccharide)


Enzyme:         Escherichia freundii
Specificity:    A variety of poly-N-acetyllactosamine structures

Enzyme:         Bacteroides fragilis
Specificity:    Linear poly-N-acetyllactosamine structures


Enzyme:         Almond alpha-fucosidase I       
Specificity:    Fuc alpha 1-3/4 (to GlcNAc)

Enzyme:         Almond alpha-fucosidase III
Specificity:    Fuc alpha 1-3/4 (to GlcNAc)
                (Scudder et al (1990) JBC 265:16472-16477
Enzyme:         Bacillus fulminans alpha fucosidase
Specificity:    Fuc alpha 1-2

Enzyme:         Bovine epididymis alpha fucosidase
Specificity:    Fuc alpha 1-3/6
                (will not cleave Fuc alpha 1-3 if a 4
                branch on the same sugar)

Enzyme:         Charonia lampas alpha fucosidase
Specificity:    In order: Fuc alpha 1-2 (to Lac)>>>
                Fuc alpha 1-6 (to GlcNAc) > 
                Fuc alpha 1-2 (to LacNAc) >
                Fuc alpha 1-4 (to GlcNAc) >>>
                Fuc alpha 1-3 (to GlcNAc)
                (Butters et al (1991) BJ 279:189-195


Enzyme:         Aspergillus oryzae beta galactosidase
Specificity:    Gal beta 1-4 

Enzyme:         Aspergillus niger beta galactosidase
Specificity:    Gal beta 1-4 GlcNAc>
                Gal beta 1-6 GlcNAc >
                Gal beta 1-3 GlcNAc

Enzyme:         Bovine testes beta galactosidase
Specificity:    Gal beta 1-3/4 >> beta 1-6 

Enzyme:         Coffee bean alpha galactosidase
Specificity:    Gal alpha 1-*

Enzyme:         E. coli beta galactosidase
Specificity:    Gal beta 1-4 

Enzyme:         Jack bean (Canavalia) beta galactosidase
Specificity:    Gal beta 1-6 GlcNAc>
                Gal beta 1-4 GlcNAc>
                Gal beta 1-3 GlcNAc

Enzyme:         Streptococcus pneumoniae beta galactosidase
Specificity:    Gal beta 1-4 GlcNAc

Enzyme:         Streptococcus 6646K beta galactosidase
Specificity:    Gal beta 1-4 GlcNAc > Gal beta 1-3 GlcNAc
                (can remove galactose from
                the Fc region of intact IgG - ref. e. g.
                Rademacher et al (1994) PNAS 91:6123-6127)


Enzyme:         Pig liver microsomal glucosidase II
Specificity:    Glc alpha 1-3
                (Olafson et al (1990) JBC 265:12240-12247)


Enzyme:         Jack bean (Canavalia) beta hexosaminidase
Specificity     GalNAc/GlcNAc beta 1-*

Enzyme:         Streptococcus pneumoniae beta hexosaminidase
Specificity:    GlcNAc beta 1-2 Man >> 
                GlcNAc beta 1-3 Gal >
                GlcNAc beta 1-6 Gal
                (Yamashita et al (1981) BBRC 100:226-232)
                (steric hindrance if a GlcNAc is beta 1-6 linked to 
                the same mannose as a beta 1-2 and of the GlcNAc on 
                the Man 1-6 arm if a bisecting GlcNAc is present; 
                altered specificity noted at higher enzyme 
                concentrations: refer to Yamashita et al (1983) JBC 258:3099)


Enzyme:         Streptomyces 142 lacto-N-biosidase
Specificity:    Polylactosamine type I
                (producing Gal beta 1-3  GlcNAc)                                  
                (Sano et al (1992) PNAS 89:8512-8516)


Enzyme:         Aspergillus saitoi alpha mannosidase I
Specificity:    Man alpha 1-2 Man
                (Ichishima et al (1981) BBA 658:45-53)

Enzyme:         Helix pomatia beta mannosidase
Specificity:    Man beta 1-4 GlcNAc

Enzyme:         Jack bean (Canavalia) alpha mannosidase
Specificity:    Man alpha 1-* Man
                Concentration and steric effects can result
                in non-removal of apparently free Man                 
                residues (e.g. hybrid N-glycans)
                (Li (1967) JBC 242:5474-5480)

NEURAMINIDASES (also known as sialidases)

Enzyme:         Arthrobacter ureafaciens neuraminidase 
Specificity:    Neu5Ac2,6Gal>

Enzyme:         Clostridium perfingens neuraminidase
Specificity:    Neu5Ac2,3Gal>

Enzyme:         Vibrio cholerae neuraminidase
Specificity:    Neu5Ac2,3Gal>

Enzyme:         Newcastle disease virus
Specificity:    Neu5Ac2,3Gal>
(Comparison of PNGase A and F is presented in Altmann et al. (1995)
Glycoconj. J. 12:84-93)

Enzyme:         PNGaseA (from almond)
Specificity:    Will cleave plant/insect alpha 1-3 core fucosylated 

Enzyme:         PNGaseF (from Flavobacterium)
Specificity:    Will not cleave alpha 1-3 core fucosylated oligosaccharides

Apparently no pure beta 1,2 xylosidases of use for the sequencing of 
plant glycoproteins have been described - but a xylosidase, 
considered to be a co-activity of a beta-glucosidase isoenzyme, has 
been referred to in the literature - Kiss et al. (1981) BBRC 
98:792-799 (referred to in Kubelka et al. (1993) EJB 213:1193-1204, 
but not checked on by myself).

Iain Wilson                        Institut für Chemie           
Tel: 43-1-47654-6065               Universität für Bodenkultur   
Fax: 43-1-310-5176                 Gregor-Mendel-Straße 33
E-mail: wilson at edv1.boku.ac.at     A-1180, WIEN, Austria

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