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Information on EC 4.2.2.2 - pectate lyase and Organism(s) Bacillus subtilis and UniProt Accession P39116
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4.2.2.2 pectate lyaseIUBMB Comments
Favours pectate, the anion, over pectin, the methyl ester (which is the preferred substrate of EC 4.2.2.10, pectin lyase).
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Word Map
- 4.2.2.2
- erwinia
- chrysanthemi
- lyases
- polygalacturonase
- carotovora
- cellulase
-
macer
-
pectinolytic
-
phytopathogenic
-
soft-rotting
- pectinases
- atroseptica
- homogalacturonan
- polypectate
-
wall-degrading
- pectinesterase
-
textile
-
methylesterase
-
degumming
-
soften
- ramie
- xylanase
-
beta-helix
-
alkaliphilic
- oligogalacturonates
-
4,5-unsaturated
-
enterobacterium
- viridiflava
- digalacturonate
- pectobacterium
- rhamnogalacturonan
-
pectin-degrading
- dickeya
- harpins
- plb
-
plant-parasitic
- dadantii
- gloeosporioides
-
de-esterified
-
bioscouring
- agriculture
- food industry
- biotechnology
- degradation
- industry
-
subventral
- environmental protection
- molecular biology
The taxonomic range for the selected organisms is: Bacillus subtilis
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
pectate lyase, polygalacturonate lyase, pectate lyase c, pectate lyase a, alkaline pectate lyase, pectate lyase b, pel-2, alkaline polygalacturonate lyase, pel9a, pel168, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
alpha-1,4-D-endopolygalacturonic acid lyase
-
-
-
-
EC 4.2.99.3
-
-
-
-
endo-alpha-1,4-polygalacturonic acid lyase
-
-
-
-
endogalacturonate transeliminase
-
-
-
-
endopectin methyltranseliminase
-
-
-
-
lyase, pectate
-
-
-
-
pectate transeliminase
pectic acid lyase
-
-
-
-
pectic acid transeliminase
-
-
-
-
pectic lyase
-
-
-
-
PGA lyase
-
-
-
-
Pla
-
-
-
-
PLB
-
-
-
-
PLC
-
-
-
-
poly(1,4-alpha-D-galacturonide) lyase
-
-
-
-
polygalacturonate lyase
-
-
-
-
polygalacturonic acid lyase
-
-
-
-
polygalacturonic transeliminase
-
-
-
-
PPase-N
-
-
-
-
pectate transeliminase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
elimination
-
-
-
-
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
(1->4)-alpha-D-galacturonan lyase
Favours pectate, the anion, over pectin, the methyl ester (which is the preferred substrate of EC 4.2.2.10, pectin lyase).
CAS REGISTRY NUMBER
COMMENTARY
9015-75-2
-
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
pectin
?
pectate lyases harness anti beta-elimination chemistry to cleave the alpha-1,4 linkage in the homogalacturonan region of plant cell wall pectin
-
-
?
polygalacturonic
?
analysis of polygalacturonic acid degradation products by electrospray ionization-mass spectrometry reveal that the degradation products are unsaturated trigalacturonic acid and unsaturated bigalacturonic acid, which confirms that the enzyme catalyzes a trans-elimination reaction
-
-
?
polygalacturonate
unsaturated oligo-galacturonides
-
the enzyme produces unsaturated oligo-galacturonides including unsaturated tri-galacturonic acid and unsaturated bi-galacturonic acid but not unsaturated mono-galacturonic acid
-
-
?
polygalacturonic acid
unsaturated oligogalacturonate
-
activity decreases when the methoxyl content of the substrate increases
-
-
?
pectin
?
-
of methyl esterification degree from 22% to 89%, maximal activity on 22% esterified citrus pectin
-
-
?
polygalacturonate
unsaturated oligogalacturonides
-
pectate lyase cleaves the alpha-1,4 glycosidic bonds of polygalacturonate via a beta-elimination reaction
-
-
?
additional information
?
-
digalacturonate is not cleaved at an appreciable rate
-
-
?
additional information
?
-
-
digalacturonate is not cleaved at an appreciable rate
-
-
?
additional information
?
-
-
enzyme production is repressed by glucose
-
-
?
additional information
?
-
substrates are 45% methylated pectin or polygalacturonate
-
-
?
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
additional information
?
-
-
enzyme production is repressed by glucose
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Ca2+
additional information
Ca2+
the enzyme in the absence of substrate binds a single calcium ion, two additional calcium ions bind between enzyme and substrate carboxylates occupying the +1 subsite in the Michaelis complex
Ca2+
required, activates the recombinant enzyme from Pichia pastoris by 26%
Ca2+
activity is lost at low pH because protonation of aspartates results in the loss of the two catalytic calcium-ions causing a profound failure to correctly organise the Michaelis complex
Ca2+
activity of wild-type peaks at 1 mM Ca2+, and declines with the increase in Ca2+concentration
Ca2+
presence of Ca2+ stimulates a change in tertiary structure. Binding of Ca2+ and polygalacturonic acid to the active site may occur independently
additional information
no or poor effect on the recombinant enzyme from Pichia pastoris by Sr2+, K+, and Li+
additional information
-
no or poor effect on the recombinant enzyme from Pichia pastoris by Sr2+, K+, and Li+
additional information
Fe2+ and Cu2+ do not significantly affect the activity of Pel-66
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
no or poor effect by Tween-80, methanol, ethanol, isopropyl alcohol at 0.5%
-
additional information
-
no or poor effect by Tween-80, methanol, ethanol, isopropyl alcohol at 0.5%
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
no or poor effect by Tween-80, methanol, ethanol, isopropyl alcohol at 0.5%
-
additional information
-
no or poor effect by Tween-80, methanol, ethanol, isopropyl alcohol at 0.5%
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
Polygalacturonate
Km value of wild-type 0.47 mg/ml, mutant V132F, 0.30 mg/ml, mutant K47E, 0.31 mg/ml, mutant K47E/V132F, 0.30 mg/ml, mutant K47D/V132F, 0.30 mg/ml, mutant K47D/V132F/R272W, 0.29 mg/ml, respectively, pH 9.5, 55°C
additional information
additional information
-
Km for polygalacturonic acid: 0.862 g/l
-
additional information
additional information
-
KM-value is 0.13 mg/ml for 22% esterified pectin, the KM-value is 0.15 mg/ml for polygalacturonic acid
-
additional information
Polygalacturonate
Km value 0.312 mg/ml, pH 9.4, 50°C
additional information
Polygalacturonate
-
Km value 0.312 mg/ml, pH 9.4, 50°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
Polygalacturonate
kcat/Km value of wild-type 513 ml/mg/s, mutant V132F, 1179 ml/mg/s, mutant K47E, 1144 ml/mg/s, mutant K47E/V132F, 1216 ml/mg/s, mutant K47D/V132F, 1318 ml/mg/s, mutant K47D/V132F/R272W, 1568 ml/mg/s, respectively, pH 9.5, 55°C
additional information
Polygalacturonate
kcat/Km value 7372 ml/mg/s, pH 9.4, 50°C
additional information
Polygalacturonate
-
kcat/Km value 7372 ml/mg/s, pH 9.4, 50°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1493
recombinant protein purified from inclusion bodies, pH 9.0, 50°C
3194
recombinant protein purified from soluble fraction, pH 9.0, 50°C
additional information
additional information
pectate lyase activity as high as 100 U/ml is attained in the fermentation broth of Pichia pastoris GS 115, which is about 10 times higher than when the gene is expressed in Escherichia coli
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
9.5
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 9
-
pH 7.0: about 70% of maximal activity, pH 9.0: about 65% of maximal activity
8.3 - 10.3
-
pH 8.3: about 45% of maximal activity, pH 10.3: about 40% of maximal activity
9 - 11
-
pH 9: about 40% of maximal activity, pH 11: about 50% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
60
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 70
40 - 65
-
40°C: about 40% of maximal activity, 65°C: about 65% of maximal activity
40 - 70
-
40°C: about 30% of maximal activity, 45°C: about 55% of maximal activity, 70°C: about 35% of maximal activity
50 - 80
-
50°C: about 60% of maximal activity, 80°C: about 60% of maximal activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
pectate lyase production in Bacilli studied is modulated by the growth phase and by the carbon source present in the medium, high level expression in Bacillus subtilis
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
secreted during the exponential death phase of growth, just before sporulation
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
activity is lost at low pH because protonation of aspartates results in the loss of the two catalytic calcium-ions causing a profound failure to correctly organise the Michaelis complex
evolution
-
the mature Apel is structurally related to the enzymes in the polysaccharide lyase family 1
additional information
additional information
-
implication of Bacillus sp. in the production of pectinolytic enzymes during cocoa fermentation
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
46000
x * 48600-51400, recombinant enzyme from Pichia pastoris, SDS-PAGE, x * 46000, recombinant enzyme from Escherichia coli, SDS-PAGE
38600
-
x * 45498, sequence calculation, x * 38600, mature recombinant enzyme, SDS-PAGE
42000
45498
-
x * 45498, sequence calculation, x * 38600, mature recombinant enzyme, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 48600-51400, recombinant enzyme from Pichia pastoris, SDS-PAGE, x * 46000, recombinant enzyme from Escherichia coli, SDS-PAGE
?
-
x * 45498, sequence calculation, x * 38600, mature recombinant enzyme, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
the enzyme has five putative N-glycosylation sites (Asn-X-Thr/Ser), three near to the N-terminus (N-48, N-127, N-184), and the other two near the C-terminus (N-345, N-351)
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
R279A mutant, streak seeding pre-equilibrated protein drops, using 0.1 M sodium acetate (pH 4.6), 0.2 M ammonium acetate, and 18% (w/v) PEG 4000, supplemented with 20 mM trigalacturonate, 7 mM calcium chloride, and 15% glycerol as a cryoprotectant
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.5 - 11
recombinant enzyme shows a wider pH and thermal stability spectrum than the purified pectate lyase from Bacillus subtilis WSHB04-02
690786
10.5
3 - 10
7 - 11.5
-
purified recombinant enzyme, 2 h, stable up to pH 9.0, inactivation at pH 11.5
729460
3 - 10
pH ranging from 3.0 to 10.0 does not significantly influence the stability of the enzyme, but the enzyme seems to be more stable at its optimum pH
713825
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
55
enzyme is stable to incubation up to 55°C when incubated at various temperatures for 20 min in glycine-NaOH buffer (pH 9.4)
60
purified enzyme, 20 min, recombinant enzyme from Pichia pastoris retaines 26% activity, recombinant enzyme from Escherichia coli is inactivated
40 - 50
45
-
pH 9.4: stable for 300 h. pH 10.0: about 40% loss of activity after 300 h
50
60
70
60
-
purified recombinant enzyme, pH 9.0, half-life is 20 min, inactivation after 80 min
70
-
purified recombinant enzyme, pH 9.0, half-life is about 12 min, inactivation after 60 min
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native Pel-66 from supernatant by ammonium sulfate fractionation and cation exchange chromatography
recombinant enzyme 17.3fold from strain WB600 culture supernatant by ammonium sulfate fractionation, cation exchange chromatography, and gel filtration
-
recombinant protein, both from soluble fraction and from inclusion bodies
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene pel168, enzyme expression in Pichia pastoris strain and in Escherichia coli, the latter shows less glycosylation and thermostability
expression in Escherichia coli
gene Bsu11286Pel, DNA and amino acid sequence determination and analysis, recombinant expression in Bacillus subtilis strain WB600
-
gene encoding pectate lyase is amplified by PCR, fused with a periplasmic secretion signal peptide sequence, pelB, from pET22b(+), cloned and expressed in Escherichia coli cells using a temperature control vector, pHsh
-
pectate lyase gene fused to the pelB gene encoding the periplasmic secretion signal and the fusion gene is expressed under the control of the T7 promoter in a culture of Escherichia coli BL21DE3
-
recombinantly expressed in Pichia pastoris. The ratio of methanol to cell concentration has a significant influence on PGL production. An advanced glycerol exponential feeding strategy is developed for biomass accumulation in cell growth phase, by which cell concentration reaches 140 g/L after 19 h glycerol feeding. In subsequent production phase, a methanol feeding profile is proposed according to the optimal ratio of methanol to cell concentration at a range of 0.163-0.171 g/g, and PGL activity and productivity reaches 430 U/ml and 4.34 U/ml/h, respectively
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
environmental protection
the conventional degumming process of ramie with alkaline treatment at high temperature causes severe environmental pollution. Pectate lyases can be used to remove pectin from ramie in a degumming process with reduced environmental pollution and energy consumption
industry
the conventional degumming process of ramie with alkaline treatment at high temperature causes severe environmental pollution. Pectate lyases can be used to remove pectin from ramie in a degumming process with reduced environmental pollution and energy consumption
biotechnology
-
enhancing PGL production by controlling the optimal ratio provides an alternative approach to enhance heterologous protein production with Pichia pastoris
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Nasser, W.; Awade, A.C.; Reverchon, S.; Robert-Baudouy, J.
Pectate lyase from Bacillus subtilis: molecular characterization of the gene, and properties of the cloned enzyme
FEBS Lett.
335
319-326
1993
Bacillus subtilis
Sakamoto, T.; Hours, R.A.; Sakai, T.
Purification, characterization, and production of two pectic transeliminases with protopectinase activity from Bacillus subtilis
Biosci. Biotechnol. Biochem.
58
353-358
1994
Bacillus subtilis
Nasser, W.; Chalet, F.; Robert-Baudouy, J.
Purification and characterization of extracellular pectate lyase from Bacillus subtilis
Biochimie
72
689-695
1990
Bacillus subtilis, Bacillus subtilis SO113
Matsumoto, T.; Katsura, D.; Kondo, A.; Fukuda, H.
Efficient secretory overexpression of Bacillus subtilis pectate lyase in Escherichia coli and single-step purification
Biochem. Eng. J.
12
175-179
2002
Bacillus subtilis, Bacillus subtilis IFO3134
-
Margesin, R.; Fauster, V.; Fonteyne, P.A.
Characterization of cold-active pectate lyase from psychrophilic Mrakia frigida
Lett. Appl. Microbiol.
40
453-459
2005
Bacillus subtilis, Mrakia frigida
Soriano, M.; Diaz, P.; Pastor, F.I.J.
Pectate lyase C from Bacillus subtilis: a novel endo-cleaving enzyme with activity on highly methylated pectin
Microbiology
152
617-625
2006
Bacillus subtilis
Zhuge, B.; Du, G.C.; Shen, W.; Zhuge, J.; Chen, J.
Efficient secretory expression of an alkaline pectate lyase gene from Bacillus subtilis in E. coli and the purification and characterization of the protein
Biotechnol. Lett.
29
405-410
2007
Bacillus subtilis, Bacillus subtilis WSHB04-02
Zhuge, B.; Du, G.; Shen, W.; Zhuge, J.; Chen, J.
Expression of a Bacillus subtilis pectate lyase gene in Pichia pastoris
Biochem. Eng. J.
40
92-98
2008
Bacillus subtilis (P39116)
-
Wang, Y.; Wang, Z.; Du, G.; Hua, Z.; Liu, L.; Li, J.; Chen, J.
Enhancement of alkaline polygalacturonate lyase production in recombinant Pichia pastoris according to the ratio of methanol to cell concentration
Biores. Technol.
100
1343-1349
2009
Bacillus subtilis
Seyedarabi, A.; To, T.T.; Ali, S.; Hussain, S.; Fries, M.; Madsen, R.; Clausen, M.H.; Teixteira, S.; Brocklehurst, K.; Pickersgill, R.W.
Structural insights into substrate specificity and the anti beta-elimination mechanism of pectate lyase
Biochemistry
49
539-546
2010
Bacillus subtilis (P39116), Bacillus subtilis
Yadav, P.K.; Singh, V.K.; Yadav, S.; Yadav, K.D.; Yadav, D.
In silico analysis of pectin lyase and pectinase sequences
Biochemistry
74
1049-1055
2009
Aspergillus oryzae, Aspergillus clavatus (A1C4B8), Aspergillus fischeri (A1D5E3), Penicillium citrinum (A2I7W3), Aspergillus niger (A2QV36), Bacillus subtilis (A4GRK6), Pectobacterium carotovorum (Q04086), Aspergillus fumigatus (Q4WIT0), Dickeya chrysanthemi (Q59419), Aspergillus nidulans (Q5ATC7)
Payasi, A.; Sanwal, R.; Sanwal, G.
Microbial pectate lyases: Characterization and enzymological properties
World J. Microbiol. Biotechnol.
25
1-14
2009
Alkalihalobacillus alcalophilus, Bacillus licheniformis, Bacillus pumilus, Bacillus pumilus BK2, Bacillus sp. (in: Bacteria), Bacillus sp. (in: Bacteria) KSM-P15, Bacillus sp. (in: Bacteria) P4-N, Bacillus sp. (in: Bacteria) TS 47, Bacillus subtilis, Bacillus subtilis 168, Bacillus subtilis SO113, Cellvibrio japonicus, Clostridium cellulovorans, Dickeya chrysanthemi, Dickeya chrysanthemi (P04959), Dickeya chrysanthemi (P0C1A2), Dickeya chrysanthemi (P11073), Dickeya chrysanthemi (P18209), Fusarium solani, Fusarium verticillioides, Niveispirillum irakense, Pseudomonas fluorescens, Pseudomonas marginalis, Pseudomonas viridiflava, Pseudonocardia sp., Thermobifida fusca
-
Ouattara, H.G.; Reverchon, S.; Niamke, S.L.; Nasser, W.
Biochemical properties of pectate lyases produced by three different Bacillus strains isolated from fermenting cocoa beans and characterization of their cloned genes
Appl. Environ. Microbiol.
76
5214-5220
2010
Lysinibacillus fusiformis (D8X179), Lysinibacillus fusiformis, Bacillus subtilis (D8X180), Bacillus pumilus (D8X181), Bacillus subtilis BS66 (D8X180), Bacillus subtilis BS66, Bacillus pumilus BS22 (D8X181), Bacillus pumilus BS22
Ouattara, H.G.; Reverchon, S.; Niamke, S.L.; Nasser, W.
Molecular identification and pectate lyase production by Bacillus strains involved in cocoa fermentation
Food Microbiol.
28
1-8
2011
Bacillus cereus, Bacillus subtilis, Bacillus pumilus, Lysinibacillus sphaericus, Bacillus thuringiensis, Lysinibacillus fusiformis
Liu, Y.; Chen, G.; Wang, J.; Hao, Y.; Li, M.; Li, Y.; Hu, B.; Lu, F.
Efficient expression of an alkaline pectate lyase gene from Bacillus subtilis and the characterization of the recombinant protein
Biotechnol. Lett.
34
109-115
2012
Bacillus subtilis, Bacillus subtilis TCCC11286
Zhang, C.; Yao, J.; Zhou, C.; Mao, L.; Zhang, G.; Ma, Y.
The alkaline pectate lyase PEL168 of Bacillus subtilis heterologously expressed in Pichia pastoris is more stable and efficient for degumming ramie fiber
BMC Biotechnol.
13
26
2013
Bacillus subtilis (P39116), Bacillus subtilis, Bacillus subtilis 168 (P39116)
Wang, X.; Lu, Z.; Xu, T.; Selvaraj, J.; Yi, L.; Zhang, G.
Improving the specific activity and thermo-stability of alkaline pectate lyase from Bacillus subtilis 168 for bioscouring
Biochem. Eng. J.
129
74-83
2018
Bacillus subtilis (P39116), Bacillus subtilis 168 (P39116)
-
Ali, S.; Sondergaard, C.R.; Teixeira, S.; Pickersgill, R.W.
Structural insights into the loss of catalytic competence in pectate lyase activity at low pH
FEBS Lett.
589
3242-3246
2015
Bacillus subtilis (P39116), Bacillus subtilis 168 (P39116)
Kumar, S.; Jain, K.K.; Singh, A.; Panda, A.K.; Kuhad, R.C.
Characterization of recombinant pectate lyase refolded from inclusion bodies generated in E. coli BL21(DE3)
Protein Expr. Purif.
110
43-51
2015
Bacillus subtilis (I0BWH3), Bacillus subtilis, Bacillus subtilis RCK (I0BWH3)
Zhou, M.; Wu, J.; Wang, T.; Gao, L.; Yin, H.; Lue, X.
The purification and characterization of a novel alkali-stable pectate lyase produced by Bacillus subtilis PB1
World J. Microbiol. Biotechnol.
33
190
2017
Bacillus subtilis (A0A286K338), Bacillus subtilis, Bacillus subtilis PB1 (A0A286K338)
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