4.2.2.2: pectate lyase
This is an abbreviated version!
For detailed information about pectate lyase, go to the full flat file.
Word Map on EC 4.2.2.2
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4.2.2.2
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erwinia
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chrysanthemi
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lyases
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polygalacturonase
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carotovora
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cellulase
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macer
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pectinolytic
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phytopathogenic
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soft-rotting
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pectinases
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atroseptica
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homogalacturonan
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polypectate
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wall-degrading
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pectinesterase
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textile
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methylesterase
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degumming
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soften
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ramie
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xylanase
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beta-helix
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alkaliphilic
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oligogalacturonates
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4,5-unsaturated
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enterobacterium
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viridiflava
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digalacturonate
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pectobacterium
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rhamnogalacturonan
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pectin-degrading
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dickeya
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harpins
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plb
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plant-parasitic
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dadantii
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gloeosporioides
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de-esterified
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bioscouring
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agriculture
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food industry
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biotechnology
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degradation
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industry
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subventral
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environmental protection
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molecular biology
- 4.2.2.2
- erwinia
- chrysanthemi
- lyases
- polygalacturonase
- carotovora
- cellulase
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macer
-
pectinolytic
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phytopathogenic
-
soft-rotting
- pectinases
- atroseptica
- homogalacturonan
- polypectate
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wall-degrading
- pectinesterase
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textile
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methylesterase
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degumming
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soften
- ramie
- xylanase
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beta-helix
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alkaliphilic
- oligogalacturonates
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4,5-unsaturated
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enterobacterium
- viridiflava
- digalacturonate
- pectobacterium
- rhamnogalacturonan
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pectin-degrading
- dickeya
- harpins
- plb
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plant-parasitic
- dadantii
- gloeosporioides
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de-esterified
-
bioscouring
- agriculture
- food industry
- biotechnology
- degradation
- industry
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subventral
- environmental protection
- molecular biology
Reaction
Synonyms
alkaline pectate lyase, alkaline polygalacturonate lyase, alpha-1,4-D-endopolygalacturonic acid lyase, Apel, Athe_1854, AtPLL, Bsp165PelA, BxPEL1, BxPEL2, C0W65_13990, Calkro_0863, Cthe_2179, DKS1 pectate lyase, EC 4.2.99.3, endo-alpha-1,4-polygalacturonic acid lyase, endo-polygalacturonate trans-eliminase, endogalacturonate transeliminase, endopectin methyltranseliminase, FcPL1, Gr-PEL-2, Gr-PEL2, Hb-PEL-1, Hspel1, Hspel2, lyase, pectate, MdPL1, More, neutral-alkaline pectate lyase, NPLase, PATE, PCPEL2, pectate lyase, pectate lyase 10A, pectate lyase 2, pectate lyase 9A, pectate lyase A, pectate lyase B, pectate lyase C, pectate lyase E, pectate lyase I, pectate lyase L, pectate lyase Pel10A, pectate lyase Pel9A, pectate lyase PL 47, pectate transeliminase, pectic acid lyase, pectic acid transeliminase, pectic lyase, Pel, Pel I, Pel II, Pel III, Pel SWU, Pel-15, Pel-15E, Pel-15H, pel-2, Pel-20, Pel-22, Pel-66, Pel-90, Pel-BL11, Pel1, Pel10A, PEL168, Pel9A, PelA, PelB, pelC, PelD, PelE, PelI, PelN, PGA lyase, PGL, PL, PL D, PL I, PL-3, PL-STR, PL1B, Pla, PLB, PLC, PLE, poly(1,4-alpha-D-galacturonide) lyase, poly-galacturonic acid trans-eliminase, polygalacturonate lyase, polygalacturonic acid lyase, polygalacturonic transeliminase, PPase-N, ScPL NP_626147, ScPL NP_627050, XcPL NP_636037, XcPL NP_638163
ECTree
4.2.2.2 pectate lyaseAdvanced search results
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results (Engineering
Engineering on EC 4.2.2.2 - pectate lyase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
I140V
Aspergillus luchuensis var. saitoi KBN 2022
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about 25% decrease in catalytic efficiency
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V197D
Aspergillus luchuensis var. saitoi KBN 2022
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about 25% decrease in catalytic efficiency
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R227W
EDW21517
increase in expression and specific activity, no increase in thermostability
R227W/S145C/T206A
EDW21517
increase in specific activity and thermostability
R227W/T206A/T222T
EDW21517
increase in specific activity and thermostability
R227W
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increase in expression and specific activity, no increase in thermostability
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D126N
the ratio of turnover number to Km-value is 57.5% of the wild-type value
D80N
the ratio of turnover number to Km-value is 93% of the wild-type value
D84N
the ratio of turnover number to Km-value is 28.6% of the wild-type value
E47Q
mutant enzyme retains almost full activity relative to wild-type enzyme
H66A
the ratio of turnover number to Km-value is 70.4% of the wild-type value
K182A
mutant enzyme retains almost full activity relative to wild-type enzyme
K185A
mutant enzyme retains almost full activity relative to wild-type enzyme
K20A
mutant enzyme retains almost full activity relative to wild-type enzyme
K41A
the ratio of turnover number to Km-value is 105% of the wild-type value
K89A
the ratio of turnover number to Km-value is 31.5% of the wild-type value
R152A
mutant enzyme retains almost full activity relative to wild-type enzyme
W78F
the ratio of turnover number to Km-value is identical to wild-type value
W78Y
mutant enzyme with slightly increased activity relative to wild-type enzyme
Y174A
the ratio of turnover number to Km-value is 90.7% of the wild-type value
D80N
Bacillus sp. (in: Bacteria) KSM-P15
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the ratio of turnover number to Km-value is 93% of the wild-type value
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D84N
Bacillus sp. (in: Bacteria) KSM-P15
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the ratio of turnover number to Km-value is 28.6% of the wild-type value
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K41A
Bacillus sp. (in: Bacteria) KSM-P15
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the ratio of turnover number to Km-value is 105% of the wild-type value
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K89A
Bacillus sp. (in: Bacteria) KSM-P15
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the ratio of turnover number to Km-value is 31.5% of the wild-type value
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E124I/T178A/N186D/I211V/A254T/S271G/N289H
140fold increase in the t50 value at 50°C, accompanied by an 84.3% decrease in activity
N186D/I211V/A254T/S271G/N289H
24fold increase in the t50 value at 50°C, with a 23.3% increase in activity
D173A
the mutation results in approximately 40% of wild type activity
D173A/N180A/K247A
the mutation results in approximately 0.2% of wild type activity
D173A/N180N
the mutation results in approximately 5% of wild type activity
K47D/V132F
2.2fold improvement in specific activity compared to wild-type
K47D/V132F/R272W
specific activity is significantly improved by about 400% in the presence of 1 mM Ca2+. Half-life at 50°C is extended to 330 min. Mutant can significantly improve the wettability and softness of fabrics
K47E
displays 1.8fold increase in activity, and half-life increased by 2.0fold at 50°C
K47E/V132F
3.9fold improvement in specific activity compared to wild-type
N180A
the mutation results in approximately 30% of wild type activity
V132F
mutant shows 1.7fold increase in activity with wider pH stability
K47D/V132F/R272W
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specific activity is significantly improved by about 400% in the presence of 1 mM Ca2+. Half-life at 50°C is extended to 330 min. Mutant can significantly improve the wettability and softness of fabrics
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K47E
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displays 1.8fold increase in activity, and half-life increased by 2.0fold at 50°C
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D154E
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mutant enzyme with 44% of the activity of the wild-type enzyme, the Km-value for the substrate lime pectin (with 75% methyl esterification) is 1.2fold higher than the Km-value of the wild-type enzyme
D154N
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mutant enzyme with 44% of the activity of the wild-type enzyme, the Km-value for the substrate lime pectin (with 75% methyl esterification) is 2.3fold higher than the Km-value of the wild-type enzyme. The pH-optimum is higher than that of the wild-type enzyme
K249R
mutant shows 40-60% of wild-type activity. At a higher Ca2+ concentration in the substrate medium, enzymatic activities of K249R and R252K mutants are less affected
N215S/T217S/S219G/A220S
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the four residues in the T1.5 loop region of PelA are mutated to match the structurally analogous T1.5 loop of PelE. Mutant enzyme shows a conformational change in the T1.5 loop from PelA conformation to that observed in pelE. The pH-optimum of the mutant enzyme is identical to that of PelA, but the T1.5 mutant has an increased specific activity that is comparable to that of PelE
R218K
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inactive mutant enzyme R218K. Crystals of mutant enzyme R218K are isomorphous with wild-type PelC crystals and belong to space group P2(1)2(1)2(1) with unit cell parameters of a = 72.14 A, b = 78.32 A and c = 94.43 A
R252K
mutant shows 6-9% of wild-type activity. At a higher Ca2+ concentration in the substrate medium, enzymatic activities of K249R and R252K mutants are less affected
N215S/T217S/S219G/A220S
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the four residues in the T1.5 loop region of PelA are mutated to match the structurally analogous T1.5 loop of PelE. Mutant enzyme shows a conformational change in the T1.5 loop from PelA conformation to that observed in pelE. The pH-optimum of the mutant enzyme is identical to that of PelA, but the T1.5 mutant has an increased specific activity that is comparable to that of PelE
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K93I
1.75fold increase in specific activity, folding free energy decreases by 1.03 kcal/ml
additional information
additional information
chimeric enzyme composed of Ala1 to Tyr105 of Pel-15 in the N-terminal regions, Asp133 to Arg 159 of pectate lyase B from Fusarium solani in the internal regions, and Gln133 to Tyr197 of Pel-15 in the C-terminal regions: the ratio of turnover number to Km-value is 5.1% of the wild-type value
additional information
Bacillus sp. (in: Bacteria) KSM-P15
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chimeric enzyme composed of Ala1 to Tyr105 of Pel-15 in the N-terminal regions, Asp133 to Arg 159 of pectate lyase B from Fusarium solani in the internal regions, and Gln133 to Tyr197 of Pel-15 in the C-terminal regions: the ratio of turnover number to Km-value is 5.1% of the wild-type value
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additional information
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construction of CcpelA gene-disrupted mutants, the mutants show reduced aggressiveness towards tomato fruits and impaired pectate lyase secretion and extracellular activity
additional information
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regulation of pectate lyase secretion by knocking out PAC1, which encodes the PacC transcription factor that regulates gene products with pH-sensitive activities is studied. Loss-of-function PAC1 mutants show 85% reduction of PELB transcript expression, delayed pectate lyase secretion and dramatically reduced virulence, as detected in infection assays with avocado fruits. PELB is up-regulated in the presence of carbon sources. When glucose is used as a carbon source in the medium for the WT strain and the knock out pac1 mutant PELB transcript expression and PL secretion are activated
additional information
genetic inactivation, function of the pecCl1 gene is assessed using the genetic inactivation strategy known as split-marker, protoplast transformation, molecular phenotype, overview
additional information
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genetic inactivation, function of the pecCl1 gene is assessed using the genetic inactivation strategy known as split-marker, protoplast transformation, molecular phenotype, overview
additional information
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in a gacA deletion mutant the production of pectate lyase, protease, and cellulase is diminished in mutant cells compared with the wild-type cells
additional information
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construction of mutants, type II secretion system-deficient mutant of Dickeya dadantii 3937, A1919, DELTA ouC, loses the capability to promote the multiplication of EDL933, whereas Ech159, DELTApoS, a stress-responsive sigma-factor RpoS-deficient mutant, increases EDL933 proliferation on lettuce leaves 2fold mor than the wild-type strain. Mutant A1919 is completely deficient in the secretion of pectate lyases, which play a major role in plant tissue maceration
additional information
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construction of mutants, type II secretion system-deficient mutant of Dickeya dadantii 3937, A1919, DELTA ouC, loses the capability to promote the multiplication of EDL933, whereas Ech159, DELTApoS, a stress-responsive sigma-factor RpoS-deficient mutant, increases EDL933 proliferation on lettuce leaves 2fold mor than the wild-type strain. Mutant A1919 is completely deficient in the secretion of pectate lyases, which play a major role in plant tissue maceration
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additional information
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transgenic lines exhibiting a greater than 90% reduction in pectate lyase transcript abundance are generated. Wall extracts from transgenic fruits show a reduction in pectin solubility and decreased depolymerization of more tightly bound polyuronides. Additional patterns of differential extraction of other wall-associated pectin subclasses are apparent, particularly in the sodium carbonate and chelator-soluble polymers. Microscopic studies reveal that the typical ripening-associated loss of cell-cell adhesion is substantially reduced in the transgenic fruits
additional information
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improvement of thermostability and activity of pectate lyase in the presence of hydroxyapatite nanoparticles
additional information
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improvement of thermostability and activity of pectate lyase in the presence of hydroxyapatite nanoparticles
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