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Information on EC 4.2.2.2 - pectate lyase and Organism(s) Thermotoga maritima and UniProt Accession Q9WYR4
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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: Thermotoga maritima
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
-
-
-
-
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
additional information
?
-
the enzyme is involved in degradation of the pectate portion of the primary plant cell wall
-
?
additional information
?
-
-
the enzyme is involved in degradation of the pectate portion of the primary plant cell wall
-
?
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
?
-
the enzyme is involved in degradation of the pectate portion of the primary plant cell wall
-
?
additional information
?
-
-
the enzyme is involved in degradation of the pectate portion of the primary plant cell wall
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystallization of mutant enzyme C132I/C156N/C194L, hanging-drop vapour-diffusion method
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60 - 95
-
the enzyme keeps stable, possesses a high level of activity at 60°C and a half-life of almost 2 h at 95°C
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
McDonough, M.A.; Ryttersgaard, C.; Bjornvad, M.E.; Lo Leggio, L.; Schulein, M.; Schroder Glad, S.O.; Larsen, S.
Crystallization and preliminary X-ray characterization of a thermostable pectate lyase from Thermotoga maritima
Acta Crystallogr. Sect. D
58
709-711
2002
Thermotoga maritima (Q9WYR4), Thermotoga maritima
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