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4.2.2.3: mannuronate-specific alginate lyase

This is an abbreviated version!
For detailed information about mannuronate-specific alginate lyase, go to the full flat file.

Word Map on EC 4.2.2.3

Reaction

R2-beta-D-mannuronic acid-R1
=
R2-OH
 +
4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl-R1

Synonyms

(poly alpha-l-guluronate) lyase, A1 alginate lyase, A1-II, A1-III, A1-IV', A1m, A1mU, A9mC, A9mL, A9mT, AAlyase, AkAly30, AL2, alg, ALG-5, Alg-A, Alg17C, Alg2A, Alg7D, AlgA, AlgB, AlgE7, AlgI, alginase I, alginate lyase, alginate lyase A, alginate lyase A1-II, alginate lyase A1-II', alginate lyase A1-III, alginate lyase AlyPEEC, alginate lyase Atu3025, alginate lyase B, alginate lyase C, alginate lyase I, alginate lyase VI, alginate lyase1-III, AlgL, ALY, ALY-1, Aly-SJ02, Aly1, Aly2, Aly28, Aly30, Aly32, Aly33, Aly35, Aly7B, AlyA, AlyA1, AlyA2, AlyA3, AlyA5, AlyB, AlyDW11, ALYIII, alyPEEC, AlyPI, AlyPM, AlyQ, AlyV5, AlyVI, Atu3025, AXE80_11190, CL2, EC 4.2.99.4, endo-type alginate lyase, endolytic poly(M) lyase, endolytic polymannuronate lyase, exotype alginate lyase, HdAlex, hdalex-1, HdAly, KJ-2 alginate lyase, LbAly28, lyase AlyA, lyase, alginate, Lysis protein, M block-specific polymannuronate lyase, mannuronate alginate lyase, MJ-3 alginate lyase, More, MY04_2544, NIS_0185, Oal17A, oligoalginate lyase, PL-5 alginate lyase, PM lyase, poly(1,4-beta-D-mannuronide) lyase, poly(beta-D-1,4-mannuronide) lyase, Poly(beta-D-mannuronate) lyase, poly(M) lyase, poly(M)lyase, Poly(mana) alginate lyase, poly(mana)alginate lyase, polymannuronate lyase, polyMG-specific alginate lyase, protein PA1167, SP2, V12B01_24254, V12B01_24259, WP_053404615

ECTree

     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.2 Acting on polysaccharides
                4.2.2.3 mannuronate-specific alginate lyase

Engineering

Engineering on EC 4.2.2.3 - mannuronate-specific alginate lyase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H311A
0.3% of wild-type activity
R199A
4.3% of wild-type activity
W467A
0.45% of wild-type activity
Y365F
0.011% of wild-type activity
C115A/C124G
strong loss of activity
G118N
almost complete loss of activity
K99A
site-directed mutagenesis, the mutation highly reduces the enzyme activity compared to the wild-type enzyme
N120H
site-directed mutagenesis, reverse replacement of N120 by His in recAkAly30 increases the activity at pH 10.0 from 8 U/mg to 93 U/mg. However, the activity level at pH 7.0, i.e., 774.8 U/mg, is still much higher than that at pH 10.0
R128A
site-directed mutagenesis, the mutation highly reduces the enzyme activity compared to the wild-type enzyme
S126A
site-directed mutagenesis, the mutation highly reduces the enzyme activity compared to the wild-type enzyme
Y140F
Y142F
D152G
T185N
NCR-truncated protein, mutant has lost its M-producing capability but retained the ability to yield L-guluronate units by almost completely degrading 2-aminobenzamide-labeled tetra(L-guluronate) chains. Mutant T185N can degrade 2-aminobenzamide-labeled penta(L-guluronate) and 2-aminobenzamide-labeled penta(D-mannuronate) fractions at greater proportions than wild-type
T282N
deletion of the noncatalytic region, 1.5fold increase in specific activity compared to wild-type
D139A
mutation in subsite +2, decrease in activity
K158F
increase in activity under acidic conditions
K158H
increase in activity under acidic conditions
K158L
increase in activity under acidic conditions
K158N
increase in activity under acidic conditions
K158W
mutation increases the liberation of disaccharides and 4-deoxy-L-erythro-5-hexoseulose uronic acid but does not show complete exolytic activity. Decrease in optimum pH value
K158Y
increase in activity under acidic conditions
S28D
no change in specific activity toward alginate
S28E
no change in specific activity toward alginate
T12K
mutation in subsite +3, decrease in activity
T12K/T14Q/S28E/T70S/D139A
mutation does not improve the poly(G) preference compared to wild-type
T12R
mutation in subsite +3, decrease in activity
T14Q/N
mutation in subsite +3, decrease in activity
T70S
no change in specific activity toward alginate
T70S/D139A
mutation decreases the relative activity of poly(alpha-1,4-L guluronate) toward poly(beta-1,4-D-mannuronate)
Y233F
K162A
-
mutant shows comparable activity to wild-type enzyme
K196A
-
mutant shows comparable activity to wild-type enzyme
K95A
-
mutant is completely inactive
R110A
-
mutation causes 65% or more inactivation
R119A
-
mutation causes 65% or more inactivation
R92A
-
mutation causes 65% or more inactivation
A78S/T89I
A78S/T89I/A217E
G26E/P39H
G304V
I51M/T89I
I51M/T89I/G304V
S35R/P39T
S35R/P39T/A224V
V6I/T85A
T89I
-
activity against poly(beta-D-mannuronic acid/alpha-L-guluronic acid) is 218 U/mg, against poly(alpha-L-guluronic acid) 31 U/mg. Ratio of activities 0.1
-
K94A
site-directed mutagenesis, the enzyme shows reduced activity compared to the wild-type enzyme
K97A
site-directed mutagenesis, the enzyme shows reduced activity compared to the wild-type enzyme
R123A
site-directed mutagenesis, the enzyme shows reduced activity compared to the wild-type enzyme
T121A
site-directed mutagenesis, the enzyme shows reduced activity compared to the wild-type enzyme, the replacement of T121 by Ala changes the substrate preference of LbAly28
Y135A
site-directed mutagenesis, the enzyme shows reduced activity compared to the wild-type enzyme
Y137A
site-directed mutagenesis, the enzyme shows reduced activity compared to the wild-type enzyme
H202Q
-
inactive mutant
Y256F
-
inactive mutant
H202L
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
H415A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
N201A
site-directed mutagenesis, inactive mutant
Q149A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
R260A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
R438A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
Y258A
site-directed mutagenesis, inactive mutant
Y450A
site-directed mutagenesis, inactive mutant
H202L
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
-
H415A
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
-
N201A
-
site-directed mutagenesis, inactive mutant
-
Y258A
-
site-directed mutagenesis, inactive mutant
-
Y450A
-
site-directed mutagenesis, inactive mutant
-
A270C
A328C
E148A
-
mutant protein is insoluble
G60A
site-directed active site mutagenesis, the mutant shows 41.4% reduced activity compared to the wild-type enzyme
H188A
site-directed mutagenesis, the mutation switches the histidine 188 GTG codon to a CGC codon
H191A
-
Vmax is 7230fold lower than wild-type value
H191N/Y284F
-
crystal structure of mutant H191N/Y284F complexed with a tetrasaccharide bound at subsites -1 to +3 suggests that Gln189 functions as a neutralizer for the substrate carboxyl group, His191 as a general base, and Tyr284 as a general acid
H192A
K280A
-
Vmax is 243fold lower than wild-type value
M62P
site-directed active site mutagenesis, two components of M62P, intactM62P and nicked M62P, are found during purification of the mutant enzyme, the nicked form is inactive, the intact form shows 56% reduced activity compared to the wild-type enzyme
N141C/N199C
Q189A
-
Vmax is 185080fold lower than wild-type value
R146A
-
Vmax is 193fold lower than wild-type value
R150A
-
Vmax is 2103fold lower than wild-type value
R67A
site-directed active site mutagenesis, the mutant shows 92.5% reduced activity compared to the wild-type enzyme
Y242F
site-directed mutagenesis, the mutation replaces the tyrosine 242 GTA codon with a GAA codon
Y246F
site-directed active site mutagenesis, almost inactive mutant
Y278F
-
Vmax is 1.3fold higher than wild-type value
Y284F
Y68F
site-directed active site mutagenesis, the mutant shows 95% reduced activity compared to the wild-type enzyme
Y80F
site-directed active site mutagenesis, the mutant shows 47% reduced activity compared to the wild-type enzyme
D226G
-
site-directed mutagenesis, the mutant shows similar activity compared to the wild-type enzyme
H200A
-
site-directed mutagenesis, inactive mutant
K308A
-
site-directed mutagenesis, inactive mutant
L224V
-
site-directed mutagenesis, the mutant shows wild-type enzyme activity
L224V/D226G
-
site-directed mutagenesis, the mutant shows 2fold increased activity compared to the wild-type enzyme
N138S
-
site-directed mutagenesis, the mutant shows similar activity compared to the wild-type enzyme
N217D
-
site-directed mutagenesis, the mutant shows slightly increased activity compared to the wild-type enzyme
T136S
-
site-directed mutagenesis, the mutant shows wild-type enzyme activity
W165A
-
site-directed mutagenesis, inactive mutant
Y306F
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y312A
-
site-directed mutagenesis, inactive mutant
Y312F
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
H200A
-
site-directed mutagenesis, inactive mutant
-
K308A
-
site-directed mutagenesis, inactive mutant
-
N138S
-
site-directed mutagenesis, the mutant shows similar activity compared to the wild-type enzyme
-
Y312A
-
site-directed mutagenesis, inactive mutant
-
additional information