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Information on EC 2.4.99.15 - (KDO)3-lipid IVA (2-4) 3-deoxy-D-manno-octulosonic acid transferase

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EC Tree

2 Transferases

2.4 Glycosyltransferases

2.4.99 Transferring other glycosyl groups

2.4.99.15 (KDO)3-lipid IVA (2-4) 3-deoxy-D-manno-octulosonic acid transferase

IUBMB Comments

The enzyme from Chlamydia psittaci transfers four KDO residues to lipid A, forming a branched tetrasaccharide with the structure alpha-KDO-(2,8)-[alpha-KDO-(2,4)]-alpha-KDO-(2,4)-alpha-KDO (cf. EC 2.4.99.12 [lipid IVA 3-deoxy-D-manno-octulosonic acid transferase], EC 2.4.99.13 [(KDO)-lipid IVA 3-deoxy-D-manno-octulosonic acid transferase], and EC 2.4.99.14 [(KDO)2-lipid IVA (2-8) 3-deoxy-D-manno-octulosonic acid transferase]).

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

Reaction Schemes

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alpha-Kdo-(2->8)-alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IVA

CMP-beta-Kdo

alpha-Kdo-(2->8)-[alpha-Kdo-(2->4)]-alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IVA

CMP

Synonyms

3-deoxy-D-manno-oct-2-ulosonic acid transferases, Kdo transferase, show all synonyms

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SYNONYM

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

3-deoxy-D-manno-oct-2-ulosonic acid transferases

Kdo transferase

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REACTION

REACTION DIAGRAM

COMMENTARY

ORGANISM

UNIPROT

LITERATURE

alpha-Kdo-(2->8)-alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IVA + CMP-beta-Kdo = alpha-Kdo-(2->8)-[alpha-Kdo-(2->4)]-alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IVA + CMP

2 entries

alpha-Kdo-(2->8)-alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IVA + CMP-beta-Kdo = alpha-Kdo-(2->8)-[alpha-Kdo-(2->4)]-alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IVA + CMP

(KDO)3-lipid IV(A) = 3-deoxy-alpha-D-manno-oct-2-ulopyranosyl-(2->8)-3-deoxy-alpha-D-manno-oct-2-ulopyranosyl-(2->4)-3-deoxy-alpha-D-manno-oct-2-ulopyranosyl-(2->6)-2-deoxy-2-[[(3R)-3-hydroxypentadecanoyl]amino]-3-O[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose. (KDO)4-lipid IV(A) = 3-deoxy-alpha-D-manno-oct-2-ulopyranosyl-(2->8)-[3-deoxy-alpha-D-manno-oct-2-ulopyranosyl-(2->4)]-3-deoxy-alpha-D-manno-oct-2-ulopyranosyl-(2->4)-3-deoxy-alpha-D-manno-oct-2-ulopyranosyl-(2->6)-2-deoxy-2-[[(3R)-3-hydroxypentadecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose

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PATHWAY SOURCE

PATHWAYS

MetaCyc

Kdo transfer to lipid IVA III (Chlamydia)

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SYSTEMATIC NAME

IUBMB Comments

CMP-3-deoxy-D-manno-oct-2-ulosonate:(KDO)3-lipid IVA 3-deoxy-D-manno-oct-2-ulosonate transferase [(2->4) glycosidic bond-forming]

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SUBSTRATE

PRODUCT

REACTION DIAGRAM

ORGANISM

UNIPROT

COMMENTARY
(Substrate)

LITERATURE
(Substrate)

COMMENTARY
(Product)

LITERATURE
(Product)

Reversibility
r=reversible
ir=irreversible
?=not specified

3-deoxy-alpha-D-manno-oct-2-ulopyranosyl-(2->8)-3-deoxy-alpha-D-manno-oct-2-ulopyranosyl-(2->4)-3-deoxy-alpha-D-manno-oct-2-ulopyranosyl-(2->6)-2-deoxy-2-[[(3R)-3-hydroxytetradecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose + CMP-3-deoxy-D-manno-octulosonate

3-deoxy-alpha-D-manno-oct-2-ulopyranosyl-(2->8)-[3-deoxy-alpha-D-manno-oct-2-ulopyranosyl-(2->4)]-3-deoxy-alpha-D-manno-oct-2-ulopyranosyl-(2->4)-3-deoxy-alpha-D-manno-oct-2-ulopyranosyl-(2->6)-2-deoxy-2-[[(3R)-3-hydroxytetradecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose + CMP

chlamydial Kdo transferases can replace in Escherichia coli K-12 the host's KDO transferase and retain the product specificities described in their natural background. WaaA from Chlamydia psittaci transfers predominantly four KDO residues to lipid A, forming a branched tetrasaccharide with the structure alpha-KDO-(2,8)-[alpha-KDO-(2,4)]-alpha-KDO-(2,4)-alpha-KDO

697703

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NATURAL SUBSTRATE

NATURAL PRODUCT

REACTION DIAGRAM

ORGANISM

UNIPROT

COMMENTARY
(Substrate)

LITERATURE
(Substrate)

COMMENTARY
(Product)

LITERATURE
(Product)

REVERSIBILITY
r=reversible
ir=irreversible
?=not specified

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ORGANISM

COMMENTARY

LITERATURE

UNIPROT

SEQUENCE DB

SOURCE

Chlamydia psittaci

697697, 697703

brenda

Chlamydia psittaci 6BC

697697

brenda

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GENERAL INFORMATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

physiological function

Chlamydia psittaci

697703

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CLONED (Commentary)

ORGANISM

UNIPROT

LITERATURE

expression in Escherichia coli

Chlamydia psittaci

697697

expression in Escherichia coli. Chlamydial KDO transferases can replace in Escherichia coli K-12 the host's KDO transferase and retain the product specificities described in their natural background. WaaA from Chlamydia psittaci transfers predominantly four KDOo residues to lipid A, forming a branched tetrasaccharide with the structure alpha-KDO-(2,8)-[alpha-KDO-(2,4)]-alpha-KDO-(2,4)-alpha-KDO

Chlamydia psittaci

697703

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REF.

AUTHORS

TITLE

JOURNAL

VOL.

PAGES

YEAR

ORGANISM (UNIPROT)

PUBMED ID

SOURCE

697697

Holst, O.; Bock, K.; Brade, L.; Brade, H.

The structures of oligosaccharide bisphosphates isolated from the lipopolysaccharide of a recombinant Escherichia coli strain expressing the gene gseA [3-deoxy-D-manno-octulopyranosonic acid (Kdo) transferase] of Chlamydia psittaci 6BC

Eur. J. Biochem.

229

194-200

1995

Chlamydia psittaci 6BC, Chlamydia psittaci

7744029

brenda

697703

Brabetz, W.; Lindner, B.; Brade, H.

Comparative analyses of secondary gene products of 3-deoxy-D-manno-oct-2-ulosonic acid transferases from Chlamydiaceae in Escherichia coli K-12

Eur. J. Biochem.

267