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4.2.2.1: hyaluronate lyase

This is an abbreviated version!
For detailed information about hyaluronate lyase, go to the full flat file.

Word Map on EC 4.2.2.1

Reaction

[hyaluronate]n
=
(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine-[hyaluronate]n-m-1
 + 2 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine +
hyaluronate

Synonyms

acidic hyase, bacterial HAse, bacterial hyaluronidase, bacterial spreading factor, bacteriophage-associated hyaluronate lyase, Cumulase, EC 4.2.99.1, GBS HA lyase, GBS hyase, glucuronoglycosaminoglycan lyase, h-SD, h-SH, HA lyase, HL, Hyal, Hyal-1, Hyal-2, HYAL1, Hyal2, HYAL3, hyaluronan lyase, hyaluronate lyase, hyaluronate lyase HylA, hyaluronate lyase HylP2, hyaluronidase, hyaluronidase 3, hyaluronidase SD, hyaluronidase SH, hyaluronidase-1, hyaluronidase-2, hyaluronoglucosaminidase-1, hyaluronoglucosaminidase-2, HYase, HylA7, hylB, hylB4755, HylP, Hylp2, LUCA-1, LUCA-2, lyase, glucuronoglycosaminoglycan, lyase, hyaluronate, More, mucinase, protein SEQ2045, rHuPH20, SagHL, SagHyal, spnHL, SpnHyal, spreading factor, SP_0314

ECTree

     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.2 Acting on polysaccharides
                4.2.2.1 hyaluronate lyase

Engineering

Engineering on EC 4.2.2.1 - hyaluronate lyase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A425K
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
A487S
-
site-directed mutagenesis, unaltered activity compared to the wild-type enzyme
D170A
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
D170E
-
site-directed mutagenesis, slightly reduced activity compared to the wild-type enzyme
D373H
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
D373H/K466Y/D478Q
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
D432A
-
site-directed mutagenesis, mutation of a residue in the putative EF hand motif, reduced activity compared to the wild-type enzyme
D473E
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
D473G
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
D478Q
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
D494T
-
site-directed mutagenesis, slightly reduced activity compared to the wild-type enzyme
D494T/K466Y
-
site-directed mutagenesis, slightly reduced activity compared to the wild-type enzyme
D537A
-
site-directed mutagenesis, mutation of a residue in the putative EF hand motif, reduced activity compared to the wild-type enzyme
E366S
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
E366S/G367R
-
site-directed mutagenesis, slightly reduced activity compared to the wild-type enzyme
E440V
-
site-directed mutagenesis, mutation of a residue in the putative EF hand motif, slightly reduced activity compared to the wild-type enzyme
G367R
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
G434A
-
site-directed mutagenesis, mutation of a residue in the putative EF hand motif, slightly reduced activity compared to the wild-type enzyme
G541A
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
H479A
-
site-directed mutagenesis, inactive mutant
H479G
-
site-directed mutagenesis, inactive mutant
I544D
-
site-directed mutagenesis, mutation of a residue in the putative EF hand motif, reduced activity compared to the wild-type enzyme
K437A
-
site-directed mutagenesis, mutation of a residue in the putative EF hand motif, reduced activity compared to the wild-type enzyme
K437A/R542A
-
site-directed mutagenesis, mutation of residues in the putative EF hand motif, reduced activity compared to the wild-type enzyme
K466Y
-
site-directed mutagenesis, slightly reduced activity compared to the wild-type enzyme
K466Y/D478Q
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
K466Y/D478Q/K725L/T726W
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
K725L/T726W
-
site-directed mutagenesis, slightly reduced activity compared to the wild-type enzyme
K861E
-
site-directed mutagenesis, slightly reduced activity compared to the wild-type enzyme
M659G/D661K
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
M659G/D661K/K725L/T726W
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
N312A
-
site-directed mutagenesis, slightly reduced activity compared to the wild-type enzyme
N370A
-
site-directed mutagenesis, slightly reduced activity compared to the wild-type enzyme
N429A
-
site-directed mutagenesis, inactive mutant
N660A
-
site-directed mutagenesis, inactive mutant
R321L/R322Q
-
site-directed mutagenesis, slightly reduced activity compared to the wild-type enzyme
R380Q
-
site-directed mutagenesis, unaltered activity compared to the wild-type enzyme
R380Q/A478S
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
R540A
-
site-directed mutagenesis, mutation of a residue in the putative EF hand motif, reduced activity compared to the wild-type enzyme
R542A
-
site-directed mutagenesis, mutation of a residue in the putative EF hand motif, reduced activity compared to the wild-type enzyme
R546A
-
site-directed mutagenesis, mutation of a residue in the putative EF hand motif, reduced activity compared to the wild-type enzyme
S539A
-
site-directed mutagenesis, mutation of a residue in the putative EF hand motif, unaltered activity compared to the wild-type enzyme
S545V
-
site-directed mutagenesis, mutation of a residue in the putative EF hand motif, slightly reduced activity compared to the wild-type enzyme
W371A
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
W371A/W372A
-
site-directed mutagenesis, inactive mutant
W372A
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
Y484F
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
Y488F
-
site-directed mutagenesis, inactive mutant
Y488L
-
site-directed mutagenesis, inactive mutant
Y488T
-
site-directed mutagenesis, inactive mutant
D171A
catalytic mutant, 8% activity
Y183A
catalytic mutant, 13% activity
F343V
site-directed mutagensis, residue of the hydrophobic patch involved in substrate positioning during catalysis, reduced activity, crystallization for structure determination
H399A
N349A
N580G
R243V
R462A
modeling of site directed mutagenesis simulations of R462A and R462Q. The energetic profiles for the reaction processes are essentially the same as that in wild type enzyme, but the mutation accelerates the overall enzymatic activity. R462A can reduce the barrier height by about 2.8 kcal/mol. The positive charge on the R462 guanidino side chain group plays a negative role in the catalysis
R462Q
modeling of site directed mutagenesis simulations of R462A and R462Q. The energetic profiles for the reaction processes are essentially the same as that in wild type enzyme, but the mutation accelerates the overall enzymatic activity. R462Q can reduce the barrier height by about 2.9 kcal/mol. The positive charge on the R462 guanidino side chain group plays a negative role in the catalysis
W291A/W292A
site-directed mutagensis, residues of the hydrophobic patch involved in substrate positioning during catalysis, inactive mutant, crystallization for structure determination
W291A/W292A/F343V
site-directed mutagensis, residues of the hydrophobic patch involved in substrate positioning during catalysis, inactive mutant, crystallization for structure determination
W292A
site-directed mutagensis, residue of the hydrophobic patch involved in substrate positioning during catalysis, highly reduced activity, crystallization for structure determination
W292A/F343V
site-directed mutagensis, residues of the hydrophobic patch involved in substrate positioning during catalysis, highly reduced activity, crystallization for structure determination
Y408F
M179V/M181V
-
mutations in the hot spot region of HylP, lead to fibrillation with the seeding of prefibrils
V147A
-
mutation in the hot spot region, abolishes fibril formation in HylP2
D170T
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
Q295E
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
W19F
site-directed mutagenesis, denaturation profile with guanidinium hydrochloride is similar to the wild-type enzyme
Y182F
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
Y298F
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
V199D
additional information