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Enzyme Nomenclature
Information on EC 2.4.1.319 - beta-1,4-mannooligosaccharide phosphorylase
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EC Tree
2.4.1.319 beta-1,4-mannooligosaccharide phosphorylaseIUBMB Comments
The enzyme, isolated from the ruminal bacterium Ruminococcus albus, catalyses the reversible phosphorolysis of beta-1,4-mannooligosaccharide with a minimum size of three monomers.
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The enzyme appears in viruses and cellular organisms
Reaction Schemes
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
MP2
RaMp2
Rumal_0099
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
[(1->4)-beta-D-mannosyl]n + phosphate = [(1->4)-beta-D-mannosyl]n-1 + alpha-D-mannose 1-phosphate
[(1->4)-beta-D-mannosyl]n + phosphate = [(1->4)-beta-D-mannosyl]n-1 + alpha-D-mannose 1-phosphate
-
-
-
-
[(1->4)-beta-D-mannosyl]n + phosphate = [(1->4)-beta-D-mannosyl]n-1 + alpha-D-mannose 1-phosphate
n>=3, sequential bi-bi mechanism
[(1->4)-beta-D-mannosyl]n + phosphate = [(1->4)-beta-D-mannosyl]n-1 + alpha-D-mannose 1-phosphate
n>=3, sequential bi-bi mechanism
-
-
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PATHWAY SOURCE
PATHWAYS
-
-
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SYSTEMATIC NAME
IUBMB Comments
1,4-beta-D-mannooligosaccharide:phosphate alpha-D-mannosyltransferase
The enzyme, isolated from the ruminal bacterium Ruminococcus albus, catalyses the reversible phosphorolysis of beta-1,4-mannooligosaccharide with a minimum size of three monomers.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-O-beta-D-mannosyl-D-glucose + phosphate
D-glucose + alpha-D-mannosyl 1-phosphate
-
-
-
?
beta-D-Man-(1->4)-beta-D-Man-(1->4)-beta-D-Man-(1->4)-beta-D-Man-(1->4)-beta-D-Man-(1->4)-D-Man + alpha-D-mannose 1-phosphate
beta-D-Man-(1->4)-beta-D-Man-(1->4)-beta-D-Man-(1->4)-beta-D-Man-(1->4)-beta-D-Man-(1->4)-beta-D-Man-(1->4)-D-Man + phosphate
-
-
-
r
beta-D-Man-(1->4)-beta-D-Man-(1->4)-beta-D-Man-(1->4)-beta-D-Man-(1->4)-D-Man + alpha-D-mannose 1-phosphate
beta-D-Man-(1->4)-beta-D-Man-(1->4)-beta-D-Man-(1->4)-beta-D-Man-(1->4)-beta-D-Man-(1->4)-D-Man + phosphate
-
-
-
r
beta-D-Man-(1->4)-beta-D-Man-(1->4)-beta-D-Man-(1->4)-beta-D-Man-(1->4)-D-Man + phosphate
beta-D-Man-(1->4)-beta-D-Man-(1->4)-beta-D-Man-(1->4)-D-Man + alpha-D-mannose 1-phosphate
-
-
-
r
beta-D-Man-(1->4)-beta-D-Man-(1->4)-beta-D-Man-(1->4)-D-Man + alpha-D-mannose 1-phosphate
beta-D-Man-(1->4)-beta-D-Man-(1->4)-beta-D-Man-(1->4)-beta-D-Man-(1->4)-D-Man + phosphate
best substrate for the synthetic reaction
-
-
r
beta-D-Man-(1->4)-beta-D-Man-(1->4)-beta-D-Man-(1->4)-D-Man + phosphate
beta-D-Man-(1->4)-beta-D-Man-(1->4)-D-Man + alpha-D-mannose 1-phosphate
-
-
-
r
beta-D-Man-(1->4)-beta-D-Man-(1->4)-D-Man + alpha-D-mannose 1-phosphate
beta-D-Man-(1->4)-beta-D-Man-(1->4)-beta-D-Man-(1->4)-D-Man + phosphate
-
-
-
r
beta-D-Man-(1->4)-beta-D-Man-(1->4)-D-Man + phosphate
beta-D-mannopyranosyl-(1->4)-D-mannopyranose + alpha-D-mannose 1-phosphate
-
-
-
r
beta-D-mannopyranosyl-(1->4)-beta-D-mannopyranosyl-(1->4)-D-mannopyranose + phosphate
beta-D-mannopyranosyl-(1->4)-D-mannopyranose + alpha-D-mannose 1-phosphate
-
-
-
r
beta-D-mannopyranosyl-(1->4)-D-mannopyranose + alpha-D-mannose 1-phosphate
beta-D-mannopyranosyl-(1->4)-beta-D-mannopyranosyl-(1->4)-D-mannopyranose + phosphate
-
-
-
r
beta-D-mannopyranosyl-(1->4)-D-mannopyranose + phosphate
D-mannose + alpha-D-mannose 1-phosphate
-
-
-
r
[(1->4)-beta-D-mannosyl]2 + alpha-D-mannose 1-phosphate
[(1->4)-beta-D-mannosyl]3 + phosphate
-
-
-
?
[(1->4)-beta-D-mannosyl]2 + phosphate
D-mannose + alpha-D-mannose 1-phosphate
-
-
-
?
[(1->4)-beta-D-mannosyl]3 + alpha-D-mannose 1-phosphate
[(1->4)-beta-D-mannosyl]4 + phosphate
-
-
-
?
[(1->4)-beta-D-mannosyl]3 + phosphate
[(1->4)-beta-D-mannosyl]2 + alpha-D-mannose 1-phosphate
-
-
-
?
[(1->4)-beta-D-mannosyl]4 + alpha-D-mannose 1-phosphate
[(1->4)-beta-D-mannosyl]5 + phosphate
-
-
-
?
[(1->4)-beta-D-mannosyl]4 + phosphate
[(1->4)-beta-D-mannosyl]3 + alpha-D-mannose 1-phosphate
-
-
-
?
[(1->4)-beta-D-mannosyl]5 + alpha-D-mannose 1-phosphate
[(1->4)-beta-D-mannosyl]6 + phosphate
-
-
-
?
[(1->4)-beta-D-mannosyl]5 + phosphate
[(1->4)-beta-D-mannosyl]4 + alpha-D-mannose 1-phosphate
-
-
-
?
[(1->4)-beta-D-mannosyl]6 + alpha-D-mannose 1-phosphate
[(1->4)-beta-D-mannosyl]7 + phosphate
-
-
-
?
[(1->4)-beta-D-mannosyl]6 + phosphate
[(1->4)-beta-D-mannosyl]5 + alpha-D-mannose 1-phosphate
-
-
-
?
[(1->4)-beta-D-mannosyl]n + phosphate
[(1->4)-beta-D-mannosyl]n-1 + alpha-D-mannose 1-phosphate
[(1->4)-beta-D-mannosyl]n-1 + alpha-D-mannose 1-phosphate
[(1->4)-beta-D-mannosyl]n + phosphate
the enzyme catalyses the reversible phosphorolysis of beta-1,4-mannooligosaccharide with a minimum size of three monomers. It acts on D-glucose derivatives at the C2- and C3-positions, including deoxy- and deoxyfluoro-analogues and epimers, but not on those substituted at the C6-position. It shows high synthetic activity toward the following oligosaccharides: beta-linked glucobioses, maltose, N,N'-diacetylchitobiose, and beta-1,4-mannooligosaccharides. Particularly, beta-1,4-mannooligosaccharides serve as significantly better acceptor substrates for the enzyme than D-glucose. In the phosphorolytic reactions, RaMP2 has weak activity toward beta-1,4-mannobiose but efficiently degrades beta-1,4-mannooligosaccharides longer than beta-1,4-mannobiose. It is thought to catalyze the phosphorolysis of beta-1,4-mannooligosaccharides longer than beta-1,4-mannobiose to produce alpha-D-mannose 1-phosphate and beta-1,4-mannobiose
-
-
r
additional information
?
-
The enzyme also catalyzes the reaction of EC 2.4.1.281, 4-O-beta-D-mannosyl-D-glucose phosphorylase
-
-
?
[(1->4)-beta-D-mannosyl]n + phosphate
[(1->4)-beta-D-mannosyl]n-1 + alpha-D-mannose 1-phosphate
-
-
-
r
[(1->4)-beta-D-mannosyl]n + phosphate
[(1->4)-beta-D-mannosyl]n-1 + alpha-D-mannose 1-phosphate
the enzyme is involved in the metabolic pathway of mannan
-
-
r
[(1->4)-beta-D-mannosyl]n + phosphate
[(1->4)-beta-D-mannosyl]n-1 + alpha-D-mannose 1-phosphate
the enzyme catalyses the reversible phosphorolysis of beta-1,4-mannooligosaccharide with a minimum size of three monomers. It acts on D-glucose derivatives at the C2- and C3-positions, including deoxy- and deoxyfluoro-analogues and epimers, but not on those substituted at the C6-position. It shows high synthetic activity toward the following oligosaccharides: beta-linked glucobioses, maltose, N,N'-diacetylchitobiose, and beta-1,4-mannooligosaccharides. Particularly, beta-1,4-mannooligosaccharides serve as significantly better acceptor substrates for the enzyme than D-glucose. In the phosphorolytic reactions, RaMP2 has weak activity toward beta-1,4-mannobiose but efficiently degrades beta-1,4-mannooligosaccharides longer than beta-1,4-mannobiose. It is thought to catalyze the phosphorolysis of beta-1,4-mannooligosaccharides longer than beta-1,4-mannobiose to produce alpha-D-mannose 1-phosphate and beta-1,4-mannobiose
-
-
r
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
[(1->4)-beta-D-mannosyl]n + phosphate
[(1->4)-beta-D-mannosyl]n-1 + alpha-D-mannose 1-phosphate
[(1->4)-beta-D-mannosyl]n + phosphate
[(1->4)-beta-D-mannosyl]n-1 + alpha-D-mannose 1-phosphate
-
-
-
r
[(1->4)-beta-D-mannosyl]n + phosphate
[(1->4)-beta-D-mannosyl]n-1 + alpha-D-mannose 1-phosphate
the enzyme is involved in the metabolic pathway of mannan
-
-
r
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
28.4
4-O-beta-D-mannosyl-D-glucose
pH 6.5, 37°C, cosubstrate: phosphate, phosphorolysis reaction
4.48
beta-D-Man-(1->4)-beta-D-Man-(1->4)-beta-D-Man-(1->4)-beta-D-Man-(1->4)-beta-D-Man-(1->4)-D-Man
pH 6.5, 37°C, synthetic reaction, cosubstrate alpha-D-mannose 1-phosphate
4.48
[(1->4)-beta-D-mannosyl]6
pH 6.5, 37°C, cosubstrate: alpha-D-mannose 1-phosphate, synthetic reaction
4.55
beta-D-Man-(1->4)-beta-D-Man-(1->4)-beta-D-Man-(1->4)-beta-D-Man-(1->4)-D-Man
pH 6.5, 37°C, phosphorolytic reaction, cosubstrate phosphate
5.29
beta-D-Man-(1->4)-beta-D-Man-(1->4)-beta-D-Man-(1->4)-beta-D-Man-(1->4)-D-Man
pH 6.5, 37°C, synthetic reaction, cosubstrate alpha-D-mannose 1-phosphate
3.21
beta-D-Man-(1->4)-beta-D-Man-(1->4)-beta-D-Man-(1->4)-D-Man
pH 6.5, 37°C, phosphorolytic reaction, cosubstrate phosphate
7.59
beta-D-Man-(1->4)-beta-D-Man-(1->4)-beta-D-Man-(1->4)-D-Man
pH 6.5, 37°C, synthetic reaction, cosubstrate alpha-D-mannose 1-phosphate
7.94
beta-D-Man-(1->4)-beta-D-Man-(1->4)-D-Man
pH 6.5, 37°C, phosphorolytic reaction, cosubstrate phosphate
13.3
beta-D-Man-(1->4)-beta-D-Man-(1->4)-D-Man
pH 6.5, 37°C, synthetic reaction, cosubstrate alpha-D-mannose 1-phosphate
30.7
beta-D-mannopyranosyl-(1->4)-D-mannopyranose
pH 6.5, 37°C, synthetic reaction, cosubstrate alpha-D-mannose 1-phosphate
44.5
beta-D-mannopyranosyl-(1->4)-D-mannopyranose
pH 6.5, 37°C, phosphorolytic reaction, cosubstrate phosphate
30.7
[(1->4)-beta-D-mannosyl]2
pH 6.5, 37°C, cosubstrate: alpha-D-mannose 1-phosphate, synthetic reaction
44.5
[(1->4)-beta-D-mannosyl]2
pH 6.5, 37°C, cosubstrate: phosphate, phosphorolysis reaction
7.94
[(1->4)-beta-D-mannosyl]3
pH 6.5, 37°C, cosubstrate: phosphate, phosphorolysis reaction
13.3
[(1->4)-beta-D-mannosyl]3
pH 6.5, 37°C, cosubstrate: alpha-D-mannose 1-phosphate, synthetic reaction
3.21
[(1->4)-beta-D-mannosyl]4
pH 6.5, 37°C, cosubstrate: phosphate, phosphorolysis reaction
7.59
[(1->4)-beta-D-mannosyl]4
pH 6.5, 37°C, cosubstrate: alpha-D-mannose 1-phosphate, synthetic reaction
4.55
[(1->4)-beta-D-mannosyl]5
pH 6.5, 37°C, cosubstrate: phosphate, phosphorolysis reaction
5.29
[(1->4)-beta-D-mannosyl]5
pH 6.5, 37°C, cosubstrate: alpha-D-mannose 1-phosphate, synthetic reaction
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
20.7
4-O-beta-D-mannosyl-D-glucose
pH 6.5, 37°C, cosubstrate: phosphate, phosphorolysis reaction
16
beta-D-Man-(1->4)-beta-D-Man-(1->4)-beta-D-Man-(1->4)-beta-D-Man-(1->4)-beta-D-Man-(1->4)-D-Man
pH 6.5, 37°C, synthetic reaction, cosubstrate alpha-D-mannose 1-phosphate
16
[(1->4)-beta-D-mannosyl]6
pH 6.5, 37°C, cosubstrate: alpha-D-mannose 1-phosphate, synthetic reaction
20.5
beta-D-Man-(1->4)-beta-D-Man-(1->4)-beta-D-Man-(1->4)-beta-D-Man-(1->4)-D-Man
pH 6.5, 37°C, synthetic reaction, cosubstrate alpha-D-mannose 1-phosphate
31.9
beta-D-Man-(1->4)-beta-D-Man-(1->4)-beta-D-Man-(1->4)-beta-D-Man-(1->4)-D-Man
pH 6.5, 37°C, phosphorolytic reaction, cosubstrate phosphate
31.2
beta-D-Man-(1->4)-beta-D-Man-(1->4)-beta-D-Man-(1->4)-D-Man
pH 6.5, 37°C, synthetic reaction, cosubstrate alpha-D-mannose 1-phosphate
33.1
beta-D-Man-(1->4)-beta-D-Man-(1->4)-beta-D-Man-(1->4)-D-Man
pH 6.5, 37°C, phosphorolytic reaction, cosubstrate phosphate
27.5
beta-D-Man-(1->4)-beta-D-Man-(1->4)-D-Man
pH 6.5, 37°C, phosphorolytic reaction, cosubstrate phosphate
34.6
beta-D-Man-(1->4)-beta-D-Man-(1->4)-D-Man
pH 6.5, 37°C, synthetic reaction, cosubstrate alpha-D-mannose 1-phosphate
7.06
beta-D-mannopyranosyl-(1->4)-D-mannopyranose
pH 6.5, 37°C, phosphorolytic reaction, cosubstrate phosphate
45.1
beta-D-mannopyranosyl-(1->4)-D-mannopyranose
pH 6.5, 37°C, synthetic reaction, cosubstrate alpha-D-mannose 1-phosphate
7.06
[(1->4)-beta-D-mannosyl]2
pH 6.5, 37°C, cosubstrate: phosphate, phosphorolysis reaction
45.1
[(1->4)-beta-D-mannosyl]2
pH 6.5, 37°C, cosubstrate: alpha-D-mannose 1-phosphate, synthetic reaction
27.5
[(1->4)-beta-D-mannosyl]3
pH 6.5, 37°C, cosubstrate: phosphate, phosphorolysis reaction
34.6
[(1->4)-beta-D-mannosyl]3
pH 6.5, 37°C, cosubstrate: alpha-D-mannose 1-phosphate, synthetic reaction
31.2
[(1->4)-beta-D-mannosyl]4
pH 6.5, 37°C, cosubstrate: alpha-D-mannose 1-phosphate, synthetic reaction
33.1
[(1->4)-beta-D-mannosyl]4
pH 6.5, 37°C, cosubstrate: phosphate, phosphorolysis reaction
20.5
[(1->4)-beta-D-mannosyl]5
pH 6.5, 37°C, cosubstrate: alpha-D-mannose 1-phosphate, synthetic reaction
31.9
[(1->4)-beta-D-mannosyl]5
pH 6.5, 37°C, cosubstrate: phosphate, phosphorolysis reaction
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.729
4-O-beta-D-mannosyl-D-glucose
pH 6.5, 37°C, cosubstrate: phosphate, phosphorolysis reaction
3.57
[(1->4)-beta-D-mannosyl]6
pH 6.5, 37°C, cosubstrate: alpha-D-mannose 1-phosphate, synthetic reaction
0.159
[(1->4)-beta-D-mannosyl]2
pH 6.5, 37°C, cosubstrate: phosphate, phosphorolysis reaction
1.47
[(1->4)-beta-D-mannosyl]2
pH 6.5, 37°C, cosubstrate: alpha-D-mannose 1-phosphate, synthetic reaction
2.6
[(1->4)-beta-D-mannosyl]3
pH 6.5, 37°C, cosubstrate: alpha-D-mannose 1-phosphate, synthetic reaction
3.46
[(1->4)-beta-D-mannosyl]3
pH 6.5, 37°C, cosubstrate: phosphate, phosphorolysis reaction
4.11
[(1->4)-beta-D-mannosyl]4
pH 6.5, 37°C, cosubstrate: alpha-D-mannose 1-phosphate, synthetic reaction
10.3
[(1->4)-beta-D-mannosyl]4
pH 6.5, 37°C, cosubstrate: phosphate, phosphorolysis reaction
3.87
[(1->4)-beta-D-mannosyl]5
pH 6.5, 37°C, cosubstrate: alpha-D-mannose 1-phosphate, synthetic reaction
7.01
[(1->4)-beta-D-mannosyl]5
pH 6.5, 37°C, cosubstrate: phosphate, phosphorolysis reaction
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
the enzyme is involved in the metabolic pathway of mannan
physiological function
-
the enzyme is involved in the metabolic pathway of mannan
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MOSP_RUMA7
Ruminococcus albus (strain ATCC 27210 / DSM 20455 / JCM 14654 / NCDO 2250 / 7)
335
0
38311
Swiss-Prot
-
A0A5J4P4Q8_9ZZZZ
98
0
11337
TrEMBL
other Location (Reliability: 2)
A0A5J4QHW4_9ZZZZ
342
0
38996
TrEMBL
other Location (Reliability: 1)
A0A5J4T318_9ZZZZ
343
0
39151
TrEMBL
other Location (Reliability: 1)
A0A4Z0Y997_9FIRM
353
0
39819
TrEMBL
-
A0A5M8NY49_9BACT
343
0
39301
TrEMBL
-
A0A5J4S1R1_9ZZZZ
343
0
39279
TrEMBL
other Location (Reliability: 1)
A0A5J4SAU4_9ZZZZ
343
0
39138
TrEMBL
other Location (Reliability: 2)
A0A5J4PRU0_9ZZZZ
132
0
14798
TrEMBL
other Location (Reliability: 2)
A0A5J4PPD2_9ZZZZ
319
0
36518
TrEMBL
other Location (Reliability: 1)
A0A259UP10_9FIRM
335
0
37875
TrEMBL
-
A0A645FT38_9ZZZZ
253
0
29102
TrEMBL
other Location (Reliability: 1)
A0A7W7IYH9_9FLAO
321
0
36463
TrEMBL
-
A0A4Z0YN29_9FIRM
322
0
36737
TrEMBL
-
A0A5J4SKS3_9ZZZZ
343
0
39140
TrEMBL
other Location (Reliability: 2)
A0A5J4PE67_9ZZZZ
93
0
10184
TrEMBL
other Location (Reliability: 2)
A0A1J5Q129_9ZZZZ
498
0
54152
TrEMBL
Mitochondrion (Reliability: 3)
A0A1J5T409_9ZZZZ
490
0
54574
TrEMBL
Mitochondrion (Reliability: 5)
A0A5M8P5W4_9BACT
342
0
38913
TrEMBL
-
A0A1J5SLC2_9ZZZZ
330
0
37318
TrEMBL
other Location (Reliability: 2)
A0A5M8NSP7_9BACT
343
0
39203
TrEMBL
-
A0A5J4S206_9ZZZZ
343
0
39139
TrEMBL
other Location (Reliability: 1)
A0A259UF21_9FIRM
335
0
37931
TrEMBL
-
A0A5M8NVP4_9BACT
343
0
39282
TrEMBL
-
A0A5J4PHR2_9ZZZZ
55
0
6129
TrEMBL
other Location (Reliability: 2)
A0A1J5THH5_9ZZZZ
388
0
43917
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1J5P7K6_9ZZZZ
300
0
34456
TrEMBL
other Location (Reliability: 2)
A0A1S9CWD7_9GAMM
495
0
54264
TrEMBL
-
A0A2H5Y639_9CHLR
312
0
34917
TrEMBL
-
A0A5J4P655_9ZZZZ
37
0
4120
TrEMBL
other Location (Reliability: 1)
A0A5J4RT75_9ZZZZ
343
0
39267
TrEMBL
other Location (Reliability: 1)
A0A5J4Q2N3_9ZZZZ
261
0
29968
TrEMBL
other Location (Reliability: 1)
A0A1J5QLB9_9ZZZZ
215
0
24235
TrEMBL
other Location (Reliability: 1)
A0A1J5QF06_9ZZZZ
156
0
17490
TrEMBL
other Location (Reliability: 3)
A0A5J4SZS7_9ZZZZ
291
0
33410
TrEMBL
other Location (Reliability: 1)
A0A5J4PHB8_9ZZZZ
90
0
9920
TrEMBL
other Location (Reliability: 2)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
38000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homohexamer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in presence and absence of beta-(1->4)-mannobiose, and comparison with 4-O-beta-D-mannosyl-D-glucose phosphorylase MP1. The structures of the two enzymes differ at the +1 subsite of the substrate-binding pocket. Three loops are proposed to determine the different substrate specificities. Loop2 restricts the derivatives at the C6 position of the +1 substrate residue in beta-(1,4)-mannooligosaccharide phosphorylase MP2
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.5 - 9.5
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
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