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Literature summary for 3.2.1.178 extracted from

  • Hehemann, J.H.; Correc, G.; Thomas, F.; Bernard, T.; Barbeyron, T.; Jam, M.; Helbert, W.; Michel, G.; Czjzek, M.
    Biochemical and structural characterization of the complex agarolytic enzyme system from the marine bacterium Zobellia galactanivorans (2012), J. Biol. Chem., 287, 30571-30584.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.2.1.178

Cloned(Commentary)

Cloned (Comment) Organism
gene porA, phylogenetic analysis, expression of N-terminal His6-tagged enzyme in Escherichia coli strain BL21(DE3) Zobellia galactanivorans
gene porB, phylogenetic analysis, expression N-terminal His6-tagged enzyme in Escherichia coli strain BL21(DE3) Zobellia galactanivorans

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant catalytic domain of PorA, hanging drop vapour diffusion method, mixing of 0.002 ml of 2.6 mg/ml protein solution with 0.001 ml of crytallization solution and equilibration against a 0.5 ml reservoir, X-ray diffraction structure determination and analysis at 1.1 A resolution, molecular replacement Zobellia galactanivorans

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Zobellia galactanivorans beta-porphyranases degrade the sulfated polymers found in various quantities in natural agars. PorA displays a strict requirement for C6-sulfate in the -2- and +1-binding subsites, it does not accept methylation of the galactose unit in the -1 subsite ?
-
 ?
additional information Zobellia galactanivorans beta-porphyranases degrade the sulfated polymers found in various quantities in natural agars. PorB tolerates the presence of 3-6-anhydro-L-galactose in subsite -2 it does not accept methylation of the galactose unit in the -1 subsite ?
-
 ?
additional information Zobellia galactanivorans DSM 12802 beta-porphyranases degrade the sulfated polymers found in various quantities in natural agars. PorB tolerates the presence of 3-6-anhydro-L-galactose in subsite -2 it does not accept methylation of the galactose unit in the -1 subsite ?
-
 ?
additional information Zobellia galactanivorans DSM 12802 beta-porphyranases degrade the sulfated polymers found in various quantities in natural agars. PorA displays a strict requirement for C6-sulfate in the -2- and +1-binding subsites, it does not accept methylation of the galactose unit in the -1 subsite ?
-
 ?

Organism

Organism UniProt Comment Textmining
Zobellia galactanivorans D7GXF9 gene porB
-
Zobellia galactanivorans D7GXG0 gene porA
-
Zobellia galactanivorans DSM 12802 D7GXF9 gene porB
-
Zobellia galactanivorans DSM 12802 D7GXG0 gene porA
-

Purification (Commentary)

Purification (Comment) Organism
recombinant N-terminal His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, ultrafiltration, and gel filtration Zobellia galactanivorans

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
agarose + H2O
-
 Zobellia galactanivorans ?
-
 ?
agarose + H2O
-
 Zobellia galactanivorans DSM 12802 ?
-
 ?
additional information beta-porphyranases degrade the sulfated polymers found in various quantities in natural agars. PorA displays a strict requirement for C6-sulfate in the -2- and +1-binding subsites, it does not accept methylation of the galactose unit in the -1 subsite Zobellia galactanivorans ?
-
 ?
additional information beta-porphyranases degrade the sulfated polymers found in various quantities in natural agars. PorB tolerates the presence of 3-6-anhydro-L-galactose in subsite -2 it does not accept methylation of the galactose unit in the -1 subsite Zobellia galactanivorans ?
-
 ?
additional information beta-porphyranases degrade the sulfated polymers found in various quantities in natural agars. PorB tolerates the presence of 3-6-anhydro-L-galactose in subsite -2 it does not accept methylation of the galactose unit in the -1 subsite Zobellia galactanivorans DSM 12802 ?
-
 ?
additional information beta-porphyranases degrade the sulfated polymers found in various quantities in natural agars. PorA displays a strict requirement for C6-sulfate in the -2- and +1-binding subsites, it does not accept methylation of the galactose unit in the -1 subsite Zobellia galactanivorans DSM 12802 ?
-
 ?
natural agar + H2O extracted from Porphyra umbilicalis or from Gracilaria sp. Zobellia galactanivorans ?
-
 ?
natural agar + H2O extracted from Porphyra umbilicalis or from Gracilaria sp. Zobellia galactanivorans DSM 12802 ?
-
 ?

Synonyms

Synonyms Comment Organism
PORA
-
 Zobellia galactanivorans
PORB
-
 Zobellia galactanivorans

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Zobellia galactanivorans

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Zobellia galactanivorans

General Information

General Information Comment Organism
evolution the marine Bacteroidetes possesses a complex agarolytic system comprising four beta-agarases and five beta-porphyranases, all belonging to the glycoside hydrolase family 16, GH16, degradation patterns and structure comparisons, overview Zobellia galactanivorans
evolution the marine Bacteroidetes possesses a complex agarolytic system comprising four betaa-agarases and five beta-porphyranases, all belonging to the glycoside hydrolase family 16, GH16, degradation patterns and structure comparisons, overview Zobellia galactanivorans
additional information most intriguing feature in native PorAcat is the presence of a short loop insertion (residues 238-245), that protrudes into the active site cleft and binds at place of the -1-binding site Zobellia galactanivorans