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Literature summary extracted from

  • Palaka, B.K.; Velmurugan Ilavarasi, A.; Sapam, T.D.; Kotapati, K.V.; Nallala, V.S.; Khan, M.B.; Ampasala, D.R.
    Molecular cloning, gene expression analysis, and in silico characterization of UDP-N-acetylglucosamine pyrophosphorylase from Bombyx mori (2019), Biotechnol. Appl. Biochem., 66, 880-899 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.7.23 expressed in Escherichia coli DH5alpha and BL21 (DE3) cells Bombyx mori
2.7.7.23 gene glmU, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) Bombyx mori

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.7.23 additional information docking analysis of inhibitors, overview Bombyx mori
2.7.7.23 ZINC70672706 interaction analysis Bombyx mori
2.7.7.23 ZINC85867098 interaction analysis Bombyx mori
2.7.7.23 ZINC95098775 interaction analysis Bombyx mori
2.7.7.23 ZINC95098837 interaction analysis Bombyx mori
2.7.7.23 ZINC95098867 interaction analysis Bombyx mori

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.7.7.23 cytoplasm
-
 Bombyx mori 5737
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.7.23 UTP + N-acetyl-alpha-D-glucosamine 1-phosphate Bombyx mori
-
 diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
 ?
2.7.7.23 UTP + N-acetyl-alpha-D-glucosamine 1-phosphate Bombyx mori
-
 diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
 r

Organism

EC Number Organism UniProt Comment Textmining
2.7.7.23 Bombyx mori A0A089PRC4
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.7.23 nickel chelating affinity column chromatography Bombyx mori
2.7.7.23 recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Bombyx mori

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.7.7.23 fat body
-
 Bombyx mori
-
2.7.7.23 fat body low expression Bombyx mori
-
2.7.7.23 foregut high expression Bombyx mori
-
2.7.7.23 gut
-
 Bombyx mori
-
2.7.7.23 head
-
 Bombyx mori
-
2.7.7.23 head lowest expression Bombyx mori
-
2.7.7.23 hindgut high expression Bombyx mori
-
2.7.7.23 integument highest expression Bombyx mori
-
2.7.7.23 integument high expression Bombyx mori
-
2.7.7.23 larva
-
 Bombyx mori
-
2.7.7.23 larva glmU expression profiles are monitored during the molting and feeding stages of silkworm larvae Bombyx mori
-
2.7.7.23 malpighian tubule
-
 Bombyx mori
-
2.7.7.23 malpighian tubule low expression Bombyx mori
-
2.7.7.23 midgut high expression Bombyx mori
-
2.7.7.23 additional information expression of BmUAP mRNA was observed in all the tissues and body parts considered for the study among which, integument is observed to have higher levels of expression, followed by salivary gland and gut tissues. Expression is observed to be low in malpighian tubules and fat bodies and least in the head capsule Bombyx mori
-
2.7.7.23 salivary gland
-
 Bombyx mori
-
2.7.7.23 salivary gland high expression Bombyx mori
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.7.23 additional information GlcNAc-1-P displays hydrogen bond interactions with residues Q110, R113, K120, D209, S215, and A217. the loops moved close to UTP and narrowed the entrance. Other residues that are surrounding the UTP include L106, G108, G109, K120, P218, D219, G220, N325, I326, C327, K374, and F378, which form hydrophobic, electrostatic, and van der Waals interactions, thus increasing the stability of this complex. In UTP-bound form, the residues present in the nucleotide-binding loop of UAP does not have a major role in binding to uridine. Docking analysis of substrates and products, overview Bombyx mori ?
-
-
2.7.7.23 UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
 Bombyx mori diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
 ?
2.7.7.23 UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
 Bombyx mori diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
 r

Subunits

EC Number Subunits Comment Organism
2.7.7.23 ? x * 54500, calculated from amino acid sequence Bombyx mori
2.7.7.23 ? x * 58360, calculated from SDS-PAGE Bombyx mori
2.7.7.23 ? x * 58360, recombinant His-tagged enzyme, SDS-PAGE Bombyx mori

Synonyms

EC Number Synonyms Comment Organism
2.7.7.23 BmUAP
-
 Bombyx mori
2.7.7.23 GlmU
-
 Bombyx mori
2.7.7.23 More bifunctional enzyme, see also EC 2.3.1.157 Bombyx mori
2.7.7.23 UAP
-
 Bombyx mori
2.7.7.23 UDP-N-acetylglucosamine pyrophosphorylase
-
 Bombyx mori
2.7.7.23 UDP-N-acetylhexosamine pyrophosphorylase UniProt Bombyx mori

pI Value

EC Number Organism Comment pI Value Maximum pI Value
2.7.7.23 Bombyx mori calculated from amino acid sequence
-
 6.1

Expression

EC Number Organism Comment Expression
2.7.7.23 Bombyx mori 20-hydroxyecdysone (20E) regulates the BmUAP expression. The expression levels of BmUAP in 20E-treated larvae are analyzed at 3, 6, 12, 24, 48, and 72 h, which reveals that the expression of BmUAP is mild at 3 h and reached to a peak at 12 h and decreases thereafter. In control larvae, the expression levels of BmUAP are absent initially at 3, 6, 12 h with mild expression at 24 and 48 h, reaching to a peak at 72 h up
2.7.7.23 Bombyx mori the expression levels of the enzyme periodically increase during molting stage and decrease after ecdysis. Enzyme gene expression is strongly regulated by exogenous 20E up

General Information

EC Number General Information Comment Organism
2.7.7.23 additional information enzyme structure modeling and structure comparisons, detailed overview. Conformational changes occur in apo- and ligand-bound BmUAPs. Docking and molecular dynamics simulation studies of ligand-bound complexes of BmUAP, determination of binding mode of UTP, GlcNAc-1-P, and UDP-GlcNAc Bombyx mori
2.7.7.23 physiological function the enzyme is essential for chitin synthesis Bombyx mori
2.7.7.23 physiological function UDP-N-acetylglucosamine diphosphorylase of Bombyx mori (BmUAP) is an essential enzyme for chitin synthesis in insects. The higher levels of gene expression in integument infer that BmUAP has a significant role in cuticle formation and molting Bombyx mori