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3.5.1.26: N4-(beta-N-acetylglucosaminyl)-L-asparaginase

This is an abbreviated version!
For detailed information about N4-(beta-N-acetylglucosaminyl)-L-asparaginase, go to the full flat file.

Word Map on EC 3.5.1.26

Reaction

N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine
+
H2O
=
N-acetyl-beta-D-glucosaminylamine
 +
L-aspartate

Synonyms

1-aspartamido-beta-N-acetylglucosamine amidohydrolase, 4-L-aspartylglucosylamine amido hydrolase, AGA, amidase-1, amidase-2, amidase-3, aspartylglucosaminidase, aspartylglucosylaminase, aspartylglucosylamine deaspartylase, aspartylglycosylamine amidohydrolase, AtAGA, beta-aspartylglucosylamine amidohydrolase, EC 3.5.1.37, GA, glucosylamidase, glycoasparaginase, glycosylasparaginase, LhAGA, More, N-aspartyl-beta-glucosaminidase, N4-(N-acetyl-beta-glucosaminyl)-L-asparagine amidase

ECTree

     3 Hydrolases
         3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
             3.5.1 In linear amides
                3.5.1.26 N4-(beta-N-acetylglucosaminyl)-L-asparaginase

Engineering

Engineering on EC 3.5.1.26 - N4-(beta-N-acetylglucosaminyl)-L-asparaginase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D151N
-
mutation completely abolishes autoproteolysis, mutation eradicates the backbone distortion near the scissile peptide bond
T152A
-
autoproteolytically deficient, no hydrolase activity
T152C
-
mutant with lower turnover number to get a crystall in complex with natural substrate
G172D
the naturally occuring point mutation results in misprocessing of its precursor and is deficient in hydrolyzing glycoasparagines, the mutant can be stabilized by L-aspartic acid beta-hydroxamate for crystallization against proteolysis by other enzymes
T203I
the naturally occuring point mutation results in misprocessing of its precursor and is deficient in hydrolyzing glycoasparagines. The mutant shows increased thermostability but 93% reduced enzyme activity compared to the wild-type enzyme. The mutant is unstable to proteolysis by other enzymes
T152C
-
the autoproteolysis-active precursor is kinetically slower than the wild type enzyme
C140S
the substitution is the causative mutation for enzyme deficiency. In addition to preventing the disulfide bond formation between C140 and C156, the C140S substitution also causes destabilization of the unique/longer loop structure in the human sequence and thus prevent dimerization of GA essential for autoproteolytic activation
D200A
87% of wild-type activity, study of folding, transport and catalytic kinetics of mutant AGA
D201A
93% of wild-type activity, study of folding, transport and catalytic kinetics of mutant AGA
D205G
-
essential for activation by autocatalytic proteolytic processing
D70A
44% of wild-type activity, study of folding, transport and catalytic kinetics of mutant AGA
G172D
G203D
G226A
inactive mutant, study of folding, transport and catalytic kinetics of mutant AGA
G226D
G258A
inactive mutant, study of folding, transport and catalytic kinetics of mutant AGA
H124R
-
reduced dimerization of the precursor polypeptide, total secretion into the medium
H124W
-
reduced dimerization of the precursor polypeptide, total secretion into the medium
K230A
86% of wild-type activity, study of folding, transport and catalytic kinetics of mutant AGA
L15R
naturally occuring L15R, mutating the signal sequence, causes aspartylglucosaminuria and affects translocation of aspartylglucosaminidase
N225A
45% of wild-type activity, study of folding, transport and catalytic kinetics of mutant AGA
N308D
-
less than 10% of wild-type activity, misprocessing of precursor
N38D
-
30% of wild-type activity, proper processing to its mature lysosomal form
R138Q
the single mutation does not affect either the enzyme's autoproteolysis or its hydrolase activity
R138Q/C140S
naturally occuring mutation in Finnish population causing aspartylglucosaminuria (AGU). Due to a founder effect, AGU incidence in Finland is unexcelled, with one major allele (denoted AGUFIN) found in 98% of the AGU patients. The AGUFIN allele carries the two concurrent substitutions R138Q andC140S
R161Q/C163S
naturally occuring mutation, the AGUFin-major mutation is a combination of two missense mutations, abolishing a disulfide bond and destabilizing the AGA structure. The pathogenic C163S substitution is always combined with a functionally neutral Arg161Gln substitution. Mutations in the AGA gene result in aspartylglucosaminuria (AGU, OMIM 208400), a lysosomal storage disorder that is characterized by progressive loss of intellectual capabilities and some skeletal abnormalities. AGU patients are born seemingly normal, but the progressive course of the disease manifests in, e.g. developmental delay, loss of speech and coarse facial features early in childhood. In adulthood, most AGU patients are severely retarded and require special care
R234A
-
nearly complete decrease of activity, misprocessing of precursor in ER
R234L
-
nearly complete decrease of activity, misprocessing of precursor in ER
R234Q
-
nearly complete decrease of activity, misprocessing of precursor in ER
S238A
40% of wild-type activity, study of folding, transport and catalytic kinetics of mutant AGA
T122K
T203I
T224A
-
nearly complete decrease of activity
T224S
-
nearly complete decrease of activity
T234I
T257A
T257I
naturally occuring mutation in Canadian population causing aspartylglucosaminuria (AGU), the mutant lacks the signal peptide
T310A
-
less than 10% of wild-type activity, more properly cleaved form than N308D
T33A
48% of wild-type activity, study of folding, transport and catalytic kinetics of mutant AGA
T33S
same activity as wild-type AGA
additional information