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Information on EC 3.13.1.1 - UDP-sulfoquinovose synthase
for references in articles please use BRENDA:EC3.13.1.1
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EC Tree 3 Hydrolases
3.13 Acting on carbon-sulfur bonds
3.13.1 Acting on carbon-sulfur bonds
3.13.1.1 UDP-sulfoquinovose synthase
IUBMB Comments
Requires NAD+, which appears to oxidize UDP-α-D-glucose to UDP-4-dehydroglucose, which dehydrates to UDP-4-dehydro-6-deoxygluc-5-enose, to which sulfite is added. The reaction is completed when the substrate is rehydrogenated at C-4. The enzyme from Arabidopsis thaliana is specific for UDP-Glc and sulfite.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
- 3.13.1.1
- sulfolipid
- sulfoquinovosyldiacylglycerols
- thylakoid
-
sulfoquinovosyl
- phosphatidylglycerol
- elongatus
- environmental protection
- acidocaldarius
-
photosystem
-
exohydrolase
- monogalactosyldiacylglycerols
-
loosening
-
perennial
- energy production
-
bentgrass
- glucan
-
creeping
- stolonifera
-
penncross
-
irrigated
-
sulfur-containing
- medicine
Synonyms
udp-sulfoquinovose synthase, more
top
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Agl3
Desulfinase
DszB
SQD1
sulfite:UDP-glucose sulfotransferase
synthase, uridine diphosphosulfoquinovose
-
-
-
-
UDP-sulfoquinovose synthase
sulfite:UDP-glucose sulfotransferase
-
-
-
-
UDP-sulfoquinovose synthase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
UDP-alpha-D-sulfoquinovopyranose + H2O = UDP-alpha-D-glucose + sulfite
a decrease in the internal phosphate concentration shows a corresponding increase in the relative amount of sulfolipid with UDP-sulfoquinovose as precursor
UDP-alpha-D-sulfoquinovopyranose + H2O = UDP-alpha-D-glucose + sulfite
contains characteristic conserved Y-XXX-K and glycine-rich sequence patterns
UDP-alpha-D-sulfoquinovopyranose + H2O = UDP-alpha-D-glucose + sulfite
sequence similarity to sugar nucleotide modifying enzymes, Thr228 seems to be catalytically important
-
UDP-alpha-D-sulfoquinovopyranose + H2O = UDP-alpha-D-glucose + sulfite
short-chain dehydrogenase/reductase family
-
UDP-alpha-D-sulfoquinovopyranose + H2O = UDP-alpha-D-glucose + sulfite
short-chain dehydrogenase/reductase family
UDP-alpha-D-sulfoquinovopyranose + H2O = UDP-alpha-D-glucose + sulfite
requires NAD+, which appears to oxidize the substrate to UDP-4-dehydroglucose, which dehydrates to UDP-4-dehydro-6-deoxygluc-5-enose, to which sufite can add. The reaction is completed when the substrate is rehydrogenated at C-4. The enzyme from Arabidopsis thaliana is specific for UDP-Glc and sulfite
-
-
-
UDP-alpha-D-sulfoquinovopyranose + H2O = UDP-alpha-D-glucose + sulfite
required NAD+ appears to oxidize the substrate to UDP-4-dehydroglucose, which dehydrates to UDP-4-dehydro-6-deoxygluc-5-enose, to which sulfite can add, the reaction is completed when the substrate is rehydrogenated at C-4
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of C-S bond
-
-
-
-
hydrolysis of sulfonic acid
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
sulfoquinovosyl diacylglycerol biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
UDP-6-sulfo-6-deoxyglucose sulfohydrolase
Requires NAD+, which appears to oxidize UDP-alpha-D-glucose to UDP-4-dehydroglucose, which dehydrates to UDP-4-dehydro-6-deoxygluc-5-enose, to which sulfite is added. The reaction is completed when the substrate is rehydrogenated at C-4. The enzyme from Arabidopsis thaliana is specific for UDP-Glc and sulfite.
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CAS REGISTRY NUMBER
COMMENTARY
337378-74-2
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
UDP-alpha-D-sulfoquinovopyranose + H2O
UDP-alpha-D-glucose + sulfite
Substrates: the enzyme catalyzes the reverse reaction
Products: -
Products: -
?
UDP-glucose + ?
UDP-sulfoquinovose + H2O
-
Substrates: first step of sulfolipid biosynthesis, unknown sulfur donor
Products: -
Products: -
?
2-hydroxybiphenyl + sulfite
2'-hydroxybiphenyl-2-sulfinate + H2O
-
Substrates: -
Products: -
Products: -
?
2-hydroxybiphenyl + sulfite
2'-hydroxybiphenyl-2-sulfinate + H2O
-
Substrates: -
Products: -
Products: -
?
2-hydroxybiphenyl + sulfite
2'-hydroxybiphenyl-2-sulfinate + H2O
-
Substrates: -
Products: -
Products: -
?
2-hydroxybiphenyl + sulfite
2'-hydroxybiphenyl-2-sulfinate + H2O
-
Substrates: the microbial conversion of DBT into 2-HBP is accomplished by the 4S pathway, consisting of two monooxygenases, DszC and DszA, and one desulfinase, DszB, which are encoded by the dsz operon
Products: -
Products: -
?
UDP-alpha-D-glucose + sulfite
UDP-alpha-D-sulfoquinovopyranose + H2O
-
Substrates: -
Products: -
Products: -
?
UDP-alpha-D-glucose + sulfite
UDP-alpha-D-sulfoquinovopyranose + H2O
-
Substrates: -
Products: -
Products: -
?
UDP-alpha-D-glucose + sulfite
UDP-alpha-D-sulfoquinovopyranose + H2O
-
Substrates: -
Products: -
Products: -
?
UDP-alpha-D-glucose + sulfite
UDP-alpha-D-sulfoquinovopyranose + H2O
-
Substrates: -
Products: -
Products: -
?
UDP-alpha-D-glucose + sulfite
UDP-alpha-D-sulfoquinovopyranose + H2O
Substrates: -
Products: -
Products: -
?
UDP-alpha-D-glucose + sulfite
UDP-alpha-D-sulfoquinovopyranose + H2O
Substrates: the enzyme plays an important role in building up the glycans, which are attached to the S-layer and the flagellin proteins
Products: -
Products: -
?
UDP-alpha-D-glucose + sulfite
UDP-alpha-D-sulfoquinovopyranose + H2O
Substrates: the activated form of sulfoquinovose is required for its incorporation into glycoconjugates
Products: -
Products: -
?
UDP-alpha-D-glucose + sulfite
UDP-alpha-D-sulfoquinovopyranose + H2O
Substrates: final hydride transfer occurs to C-4 rather than C-6 of the enone form of UDP-4-dehydro-D-glucose, leaving this carbon accessible for the subsequent addition of sulfite
Products: -
Products: -
?
UDP-alpha-D-glucose + sulfite
UDP-alpha-D-sulfoquinovopyranose + H2O
Substrates: the activated form of sulfoquinovose is required for its incorporation into glycoconjugates
Products: -
Products: -
?
UDP-alpha-D-glucose + sulfite
UDP-alpha-D-sulfoquinovopyranose + H2O
Substrates: final hydride transfer occurs to C-4 rather than C-6 of the enone form of UDP-4-dehydro-D-glucose, leaving this carbon accessible for the subsequent addition of sulfite
Products: -
Products: -
?
UDP-alpha-D-glucose + sulfite
UDP-alpha-D-sulfoquinovopyranose + H2O
-
Substrates: -
Products: -
Products: -
?
UDP-glucose + sulfite
UDP-6-sulfoquinovose + H2O
-
Substrates: -
Products: -
Products: -
?
UDP-glucose + sulfite
UDP-6-sulfoquinovose + H2O
Substrates: -
Products: -
Products: -
?
UDP-glucose + sulfite
UDP-6-sulfoquinovose + H2O
Substrates: key enzyme in formation of the sulfolipid head group precursor UDP-sulfoquinovose, sulfoquinovosyldiacylglycerol is a polar lipid present in photosynthetic membranes, enzyme is complexed in vivo with accessory proteins
Products: -
Products: -
?
UDP-glucose + sulfite
UDP-sulfoquinovose + H2O
-
Substrates: -
Products: -
Products: -
?
UDP-glucose + sulfite
UDP-sulfoquinovose + H2O
Substrates: -
Products: -
Products: -
?
UDP-glucose + sulfite
UDP-sulfoquinovose + H2O
Substrates: -
Products: increase in the relative amount of sulfolipid under phosphate limitation caused by increased gene expression
Products: increase in the relative amount of sulfolipid under phosphate limitation caused by increased gene expression
?
UDP-glucose + sulfite
UDP-sulfoquinovose + H2O
-
Substrates: sulfolipid biosynthesis
Products: -
Products: -
?
UDP-glucose + sulfite
UDP-sulfoquinovose + H2O
Substrates: sulfolipid biosynthesis
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
UDP-alpha-D-sulfoquinovopyranose + H2O
UDP-alpha-D-glucose + sulfite
Substrates: the enzyme catalyzes the reverse reaction
Products: -
Products: -
?
UDP-glucose + ?
UDP-sulfoquinovose + H2O
-
Substrates: first step of sulfolipid biosynthesis, unknown sulfur donor
Products: -
Products: -
?
UDP-glucose + sulfite
UDP-6-sulfoquinovose + H2O
Substrates: key enzyme in formation of the sulfolipid head group precursor UDP-sulfoquinovose, sulfoquinovosyldiacylglycerol is a polar lipid present in photosynthetic membranes, enzyme is complexed in vivo with accessory proteins
Products: -
Products: -
?
2-hydroxybiphenyl + sulfite
2'-hydroxybiphenyl-2-sulfinate + H2O
-
Substrates: -
Products: -
Products: -
?
2-hydroxybiphenyl + sulfite
2'-hydroxybiphenyl-2-sulfinate + H2O
-
Substrates: -
Products: -
Products: -
?
2-hydroxybiphenyl + sulfite
2'-hydroxybiphenyl-2-sulfinate + H2O
-
Substrates: the microbial conversion of DBT into 2-HBP is accomplished by the 4S pathway, consisting of two monooxygenases, DszC and DszA, and one desulfinase, DszB, which are encoded by the dsz operon
Products: -
Products: -
?
UDP-alpha-D-glucose + sulfite
UDP-alpha-D-sulfoquinovopyranose + H2O
-
Substrates: -
Products: -
Products: -
?
UDP-alpha-D-glucose + sulfite
UDP-alpha-D-sulfoquinovopyranose + H2O
-
Substrates: -
Products: -
Products: -
?
UDP-alpha-D-glucose + sulfite
UDP-alpha-D-sulfoquinovopyranose + H2O
-
Substrates: -
Products: -
Products: -
?
UDP-alpha-D-glucose + sulfite
UDP-alpha-D-sulfoquinovopyranose + H2O
-
Substrates: -
Products: -
Products: -
?
UDP-alpha-D-glucose + sulfite
UDP-alpha-D-sulfoquinovopyranose + H2O
Substrates: -
Products: -
Products: -
?
UDP-alpha-D-glucose + sulfite
UDP-alpha-D-sulfoquinovopyranose + H2O
Substrates: the enzyme plays an important role in building up the glycans, which are attached to the S-layer and the flagellin proteins
Products: -
Products: -
?
UDP-alpha-D-glucose + sulfite
UDP-alpha-D-sulfoquinovopyranose + H2O
Substrates: the activated form of sulfoquinovose is required for its incorporation into glycoconjugates
Products: -
Products: -
?
UDP-alpha-D-glucose + sulfite
UDP-alpha-D-sulfoquinovopyranose + H2O
Substrates: the activated form of sulfoquinovose is required for its incorporation into glycoconjugates
Products: -
Products: -
?
UDP-alpha-D-glucose + sulfite
UDP-alpha-D-sulfoquinovopyranose + H2O
-
Substrates: -
Products: -
Products: -
?
UDP-glucose + sulfite
UDP-sulfoquinovose + H2O
-
Substrates: -
Products: -
Products: -
?
UDP-glucose + sulfite
UDP-sulfoquinovose + H2O
-
Substrates: sulfolipid biosynthesis
Products: -
Products: -
?
UDP-glucose + sulfite
UDP-sulfoquinovose + H2O
Substrates: sulfolipid biosynthesis
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
-
tightly bound, enzyme binds 1 NAD+ per monomer, side-chain chemistry and hydrogen-bonding patterns in the NAD+ site
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
sulfate, APS, PAPS, sulfite, thiosulfate, sufide or sulfoglutathione are tested to determine whether they could stimulate the formation of UDP-sulfoquinovose
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
Km values for UDP-glucose are indistinguishable for the native and the recombinant enzyme, but the Km value for sulfite is over 4fold lower for the native enzyme
-
additional information
additional information
-
Km values for UDP-glucose are indistinguishable for the native and the recombinant enzyme, but the Km value for sulfite is over 4fold lower for the native enzyme
-
additional information
additional information
-
the affinity for sulfite of the native enzyme is at least 4fold higher compared to the recombinant spinach SQD1, whereas that for UDP-glucose is similar
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
desulfurization activity in strain CECT5279 over time in vivo
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 10
-
pH 7.0: about 50% of maximal activity, pH 10.0: about 35% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene agl3, or Saci0423, of the sulfoquinovose biosynthesis operon
-
-
brenda
gene agl3, or Saci0423, of the sulfoquinovose biosynthesis operon
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
SQD1 is a plastid UDP-glucose pyrophosphorylase
brenda
native SoSQD1 is primarily present in the stroma
brenda
-
SQDG1 is a soluble plastid UDP-glucose pyrophosphorylase
brenda
-
SQD1 is a soluble plastid UDP-glucose pyrophosphorylase
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
additional information
malfunction
in-frame deletion of agl3 results in a decreased molecular mass of the S-layer glycoprotein SlaA and the flagellin FlaB, indicating a change in the N-glycan composition with reduced trisaccharide structure composed of Man1GlcNAc2, missing the sulfoquinovose, a mannose and glucose. Cells lacking agl3 had a significantly lower growth rate at elevated salt concentrations compared with the background strain, overview
malfunction
-
in-frame deletion of agl3 results in a decreased molecular mass of the S-layer glycoprotein SlaA and the flagellin FlaB, indicating a change in the N-glycan composition with reduced trisaccharide structure composed of Man1GlcNAc2, missing the sulfoquinovose, a mannose and glucose. Cells lacking agl3 had a significantly lower growth rate at elevated salt concentrations compared with the background strain, overview
-
metabolism
the enzyme is critical for biosynthesis of UDP-sulfoquinovose
metabolism
-
UDP-sulfoquinovose synthase, SQD1, is important in sulfoquinovosyldiacylglycerol, SQDG, biosynthesis together with the SQDG synthase, SQD2, mechanism for SQDG biosynthesis, overview. Sulfoquinovosyldiacylglycerol is the only sulfur-containing anionic glycerolipid, a relatively minor relatively minor, and is the least prevalent component of photosynthetic membrane lipids. The function of SQDG under phosphate-limited growth conditions is highly correlated with the regulation of other plant glycerolipid biosyntheses
metabolism
-
UDP-sulfoquinovose synthase, SQD1, is important in sulfoquinovosyldiacylglycerol, SQDG, biosynthesis together with the SQDG synthase, SQD2, mechanism for SQDG biosynthesis, overview. Sulfoquinovosyldiacylglycerol is the only sulfur-containing anionic glycerolipid, a relatively minor relatively minor, and is the least prevalent component of photosynthetic membrane lipids. The function of SQDG under phosphate-limited growth conditions is highly correlated with the regulation of other plant glycerolipid biosyntheses
metabolism
-
UDP-sulfoquinovose synthase, SQD1, is important in sulfoquinovosyldiacylglycerol, SQDG, biosynthesis together with the SQDG synthase, SQD2, mechanism for SQDG biosynthesis, overview. Sulfoquinovosyldiacylglycerol is the only sulfur-containing anionic glycerolipid, a relatively minor relatively minor, and is the least prevalent component of photosynthetic membrane lipids. The function of SQDG under phosphate-limited growth conditions is highly correlated with the regulation of other plant glycerolipid biosyntheses
metabolism
-
UDP-sulfoquinovose synthase, SQD1, is important in sulfoquinovosyldiacylglycerol, SQDG, biosynthesis together with the SQDG synthase, SQD2, mechanism for SQDG biosynthesis, overview. Sulfoquinovosyldiacylglycerol is the only sulfur-containing anionic glycerolipid, a relatively minor relatively minor, and is the least prevalent component of photosynthetic membrane lipids. The function of SQDG under phosphate-limited growth conditions is highly correlated with the regulation of other plant glycerolipid biosyntheses
metabolism
key elements of the sulfite network enzymes that include adenosine-5'-phosphosulfate reductase and the sulfite scavengers sulfite oxidase (SO), sulfite reductase, UDP-sulfoquinovose synthase, and beta-mercaptopyruvate sulfurtransferases. During extended dark, sulfite oxidase is enhanced in Solanum lycopersicum wild-type leaves, while the other sulfite network components are downregulated. One pathway for sulfite utilization is its incorporation into sulfolipids, catalyzed by the chloroplast-localized UDP-sulfoquinovose synthase. In the first step, UDP-sulfoquinovase is catalyzed by SQD1, employing sulfite and UDP-Glc as substrates, while in the second step, sulfoquinovosyldiacylglycerol (SQDG) is catalyzed by SQDG synthase, employing UDP-sulfoquinovose and diacylglycerols as substrates
metabolism
-
the enzyme is critical for biosynthesis of UDP-sulfoquinovose
-
physiological function
-
UDP-sulfoquinovose synthase, SqdB, is crucial for sulfolipid synthesis in the purple bacterium
physiological function
the enzyme is a member of the sulfite network, one pathway for sulfite utilization is its incorporation into sulfolipids, catalyzed by the chloroplast-localized UDP-sulfoquinovose synthase. The degradation of sulfolipids is an essential step in chloroplast degradation
additional information
-
ferredoxin-dependent glutamate synthase, FdGOGAT, co-purifies with the native SQD1 from chloroplast stroma and is tightly associated with the enzyme. FdGOGAT is a flavincontaining protein that can reversibly bind sulfite, suggesting that the protein efficiently delivers sulfite to the SQD1 active site
additional information
-
the enzyme forms a complex with ferredoxin-dependent glutamate synthase, FdGOGAT, tentative modeling of SQDG1 bound to FdGOGAT from Synechococcus sp. PCC 6803, the predicted SQD1 sulfite channel is directed at the FMN cofactor in the FdGOGAT FMN-binding domain. FdGOGAT interaction with SQD1 channels sulfite directly to SQD1 and is an efficient way to overcome this problem
Show AA Sequence and Transmembrane Helices (370 entries)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
250000
250000
native enzyme in a complex with accessory proteins, gel filtration
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion results in bipyramidal crystals, C-2-symmetric homodimer, the protein has a bidomain structure, catalytic site is located in the cleft formed between the two lobes
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
T145A
E147A
strongly impaired conversion of UDP-D-glucose to UDP-D-glucose-5,6-ene
K186A
impaired conversion of UDP-D-glucose to UDP-D-glucose-5,6-ene
T144A
mutant enzyme with fully retained activity, conversion of UDP-D-glucose to UDP-D-glucose-5,6-ene
Y148A
strongly impaired conversion of UDP-D-glucose to UDP-D-glucose-5,6-ene
Y182A
impaired conversion of UDP-D-glucose to UDP-D-glucose-5,6-ene
E147A
-
strongly impaired conversion of UDP-D-glucose to UDP-D-glucose-5,6-ene
-
K186A
-
impaired conversion of UDP-D-glucose to UDP-D-glucose-5,6-ene
-
T144A
-
mutant enzyme with fully retained activity, conversion of UDP-D-glucose to UDP-D-glucose-5,6-ene
-
additional information
T145A
-
greatly reduced activity, site-directed mutagenesis, plays critical role for catalytic activity
additional information
the function of different amino acids in reaction/binding process is analysed, Thr-145, Tyr-182 and Lys-186 are found to fulfill analogous mechanistic roles
additional information
-
construction of a agl3DELTA deletion mutant strain, that shows a significant change in the size of the S-layer SlaA and the flagellin FlaB glycoproteins, with a changed SlaA glycan composition, phenotype, overview. Change in the phenotype under environmental stress conditions
additional information
construction of a agl3DELTA deletion mutant strain, that shows a significant change in the size of the S-layer SlaA and the flagellin FlaB glycoproteins, with a changed SlaA glycan composition, phenotype, overview. Change in the phenotype under environmental stress conditions
additional information
-
construction of a agl3DELTA deletion mutant strain, that shows a significant change in the size of the S-layer SlaA and the flagellin FlaB glycoproteins, with a changed SlaA glycan composition, phenotype, overview. Change in the phenotype under environmental stress conditions
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme from chloroplasts, recombinant enzyme from Escherichia coli
native enzyme from the chloroplast stroma. Ferredoxin-dependent glutamate synthase, FdGOGAT, co-purifies and is tightly associated with SQD1
-
Ni2+-nitrilotriacetic acid column
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expression in Escherichia coli
gene agl3, DNA sequencing and analysis of gene agl3 as part of a gene cluster involved in the biosynthesis of sulfoquinovose and important for the assembly of the S-layer N-glycans, expression in Sulfolobus solfataricus agl3 deletion mutant under the control of a maltose inducible promoter using vector pSVA1450, the expression of agl3 leads to the restoration of the production of full-length glycan
gene dszB, DszB expression pattern in Pseudomonas putida strain CECT5279
-
gene dszB, organized in the dsz operon, DNA and amino acid sequence determination and analysis, genetic organization and expression analysis, recombinant expression in recombinant Rhodococcus erythropolis strain CGMCC 4.1491, that is dsz-deficient
-