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Enzyme Nomenclature
Information on EC 2.7.7.23 - UDP-N-acetylglucosamine diphosphorylase
for references in articles please use BRENDA:EC2.7.7.23
Word Map on EC 2.7.7.23
- 2.7.7.23
- peptidoglycan
- tokodaii
-
sulfolobus
- cyst
- medicine
-
alpha-phosphate
-
thymidylyltransferase
-
sugar-1-phosphate
-
nucleotidylyltransferase
- udp-galnac
- synthesis
- analysis
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
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EC NUMBER 
COMMENTARY 
2.7.7.23
-
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RECOMMENDED NAME
GeneOntology No.
UDP-N-acetylglucosamine diphosphorylase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate = diphosphate + UDP-N-acetyl-alpha-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate = diphosphate + UDP-N-acetyl-alpha-D-glucosamine
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-
-
-
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate = diphosphate + UDP-N-acetyl-alpha-D-glucosamine
catalytic mechanism for the uridyltransfer reaction in the bifunctional enzyme GlmU, overview. The enzyme has distinct roles for Mg2+A and Mg2+B in substrate stabilization, nucleophile activation and transition-state stabilization
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
nucleotidyl group transfer
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-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
UTP:N-acetyl-alpha-D-glucosamine-1-phosphate uridylyltransferase
Part of the pathway for acetamido sugar biosynthesis in bacteria and archaea. The enzyme from several bacteria (e.g., Escherichia coli, Bacillus subtilis and Haemophilus influenzae) has been shown to be bifunctional and also to possess the activity of EC 2.3.1.157, glucosamine-1-phosphate N-acetyltransferase [3,4,6]. The enzyme from plants and animals is also active toward N-acetyl-alpha-D-galactosamine 1-phosphate (cf. EC 2.7.7.83, UDP-N-acetylgalactosamine diphosphorylase) [5,7], while the bacterial enzyme shows low activity toward that substrate [4].
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CAS REGISTRY NUMBER
COMMENTARY
9023-06-7
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
; SPL29; cvs. Guangzhan63s, 10N056, Yuehui9113, and Zhonghua 11
UniProt
bifunctional UDP-N-acetylglucosamine diphosphorylase, EC 2.7.7.23, and glucosamine-1-phosphate N-acetyltransferase, EC 2.3.1.157
UniProt
bifunctional UDP-N-acetylglucosamine diphosphorylase, EC 2.7.7.23, and glucosamine-1-phosphate N-acetyltransferase, EC 2.3.1.157
UniProt
bifunctional UDP-N-acetylglucosamine diphosphorylase, EC 2.7.7.23, and glucosamine-1-phosphate N-acetyltransferase, EC 2.3.1.157
UniProt
bifunctional UDP-N-acetylglucosamine diphosphorylase, EC 2.7.7.23, and glucosamine-1-phosphate N-acetyltransferase, EC 2.3.1.157
UniProt
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
-
the N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) is a bifunctional enzyme exclusive to prokaryotes, that belongs to the family of sugar nucleotidyltransferases (SNTs)
evolution
-
the GlmU proteins encoded by Yersinia pestis and Yersinia pseudotuberculosis are identical in amino acid sequence
evolution
although Entamoeba histolytica UAP exhibits the same three-domain global architecture as other UAPs, it appears to lack three alpha-helices at the N-terminus and contains two amino acids in the allosteric pocket that make it appear more like the enzyme from the human host than that from the other parasite Trypanosoma brucei; although Entamoeba histolytica UAP exhibits the same three-domain global architecture as other UAPs, it appears to lack three alpha-helices at the N-terminus and contains two amino acids in the allosteric pocket that make it appear more like the enzyme from the human host than that from the other parasite Trypanosoma brucei
evolution
organization andexpression of the mmy gene in Drosophila species, overview
evolution
T1RR64;, T1RRG3;
UAP isozymes are encoded by two different genes, LmUAP1 and LmUAP2; UAP isozymes are encoded by two different genes, LmUAP1 and LmUAP2
evolution
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GlmU belongs to the large family of sugar nucleotidyl transferases, which can be classified into group-I, which employs the two-metal mechanism-B as in GlmU, and group-II that employs a variant one metal mechanism-B, wherein the role of Mg2+ A is substituted by a conserved lysine. Eukaryotic sugar nucleotidyl transferases appear confined to group-II, structure-based sequence comparisons of sugar nucleotidyl transferases
evolution
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the GlmU proteins encoded by Yersinia pestis and Yersinia pseudotuberculosis are identical in amino acid sequence
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malfunction
the inhibition of this enzyme results in the fungal cell death
malfunction
-
GlmUMtb depletion perturbs cell wall structure and affects the bacterial survival in normoxia, overview
malfunction
independently-derived mmy mutants exhibit a variety of highly penetrant phenotypes, ranging from cuticle defects associated with a failure to synthesize chitin to cuticle defects associated with well-characterized Dpp-dependent closure abnormalities (dorsal closure and head involution). In particular, the mmy-associated cuticle defects are identical to those resulting from loss-of-function mutations in raw and anterior-open
malfunction
KT282116;, KT282117;
knockdown of LdUAP1 reduces chitin contents in whole larvae and integument samples, thins tracheal taenidia, impairs larval-larval molt, larval-pupal ecdysis and adult emergence. Combined knockdown of LdUAP1 and LdUAP2 causes an additive negative effect. Phenotypes, overview; silencing of LdUAP2 significantly reduces foliage consumption, decreases chitin content in midgut samples, damages PM, and retards larval growth. The resulting larvae have lighter fresh weights, smaller body sizes and depleted fat body. As a result, the development is arrested. Combined knockdown of LdUAP1 and LdUAP2 causes an additive negative effect. Phenotypes, overview
malfunction
the lesion mimic spl29 mutant exhibits spotted leaves and rapid leaf senescence from the seedling stage throughout the rest of its life cycle, leaf phenotype of wild-type and spl29 mutant plants, overview. The phenotype of spl29 is controlled by a single recessive nuclear gene, functional complementation with LOC_Os08g10600 in the spl29 mutant. Irreversible degradation of chloroplasts occurs in early senescent leaves of spl29 mutants. The early senescence phenotype involves upregulated expression levels of senescence-associated transcription factors and senescence-associated genes, and downregulated expression levels of photosynthesis-related genes, overview. Reactive oxygen species and malondialdehyde, as well as abscisic acid and jasmonic acid accumulate in the spl29 mutant accompanied by increased superoxide dismutase activity and normal catalase activity
malfunction
-
GlmUMtb depletion perturbs cell wall structure and affects the bacterial survival in normoxia, overview
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malfunction
-
GlmUMtb depletion perturbs cell wall structure and affects the bacterial survival in normoxia, overview
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malfunction
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the lesion mimic spl29 mutant exhibits spotted leaves and rapid leaf senescence from the seedling stage throughout the rest of its life cycle, leaf phenotype of wild-type and spl29 mutant plants, overview. The phenotype of spl29 is controlled by a single recessive nuclear gene, functional complementation with LOC_Os08g10600 in the spl29 mutant. Irreversible degradation of chloroplasts occurs in early senescent leaves of spl29 mutants. The early senescence phenotype involves upregulated expression levels of senescence-associated transcription factors and senescence-associated genes, and downregulated expression levels of photosynthesis-related genes, overview. Reactive oxygen species and malondialdehyde, as well as abscisic acid and jasmonic acid accumulate in the spl29 mutant accompanied by increased superoxide dismutase activity and normal catalase activity
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metabolism
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the enzymeis involved in the UDP-N-acetylglucosamine synthesis pathway, overview
metabolism
uridine diphosphate N-acetylglucosamine pyrophosphorylase catalyzes the final step in the synthesis of UDP-GlcNAc, which is involved in cell-wall biogenesis in plants and fungi and in protein glycosylation; uridine diphosphate N-acetylglucosamine pyrophosphorylase catalyzes the final step in the synthesis of UDP-GlcNAc, which is involved in cell-wall biogenesis in plants and fungi and in protein glycosylation
metabolism
the mmy-encoded N-acetylglucosamine pyrophosphorylase impacts multiple Drosophila developmental events via the action of several different downstream transferases, some of which modify proteins and lipids with GlcNAc
metabolism
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N-acetylglucosamine-1-phosphate uridyltransferase is a bifunctional enzyme that catalyzes both acetyltransfer and uridyltransfer reactions in the prokaryotic UDP-GlcNAc biosynthesis pathway
metabolism
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the first committed step in the biosynthesis of peptidoglycan involves the formation of uridine diphosphate-N-acetylglucosamine (UDP-GlcNAc) from uridine triphosphate (UTP) and GlcNAc-1-phosphate. This reactionis catalysed by N-acetylglucosamine-1-phosphate uridyltransferase (GlmU), a bifunctional enzyme with two independent active sites that possess acetyltransferase and uridyltransferase activities
metabolism
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the enzymeis involved in the UDP-N-acetylglucosamine synthesis pathway, overview; the first committed step in the biosynthesis of peptidoglycan involves the formation of uridine diphosphate-N-acetylglucosamine (UDP-GlcNAc) from uridine triphosphate (UTP) and GlcNAc-1-phosphate. This reactionis catalysed by N-acetylglucosamine-1-phosphate uridyltransferase (GlmU), a bifunctional enzyme with two independent active sites that possess acetyltransferase and uridyltransferase activities
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physiological function
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N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU) is a bifunctional enzyme involved in bacterial cell wall synthesis and is exclusive to prokaryotes
physiological function
UDP-N-acetylglucosamine pyrophosphorylase (UNAcP) is a key enzyme to construct the fungal cell wall
physiological function
down-regulation of transcripts by RNA interference prevents larval growth or results in pupal paralysis, depending on time of injection of double-stranded RNAs. Down-regulation of transcripts at the mature adult stage results in cessation of oviposition in females, as well as fat body depletion and eventual death in both sexes; down-regulation of transcripts by RNA interference results for isoform UAP1 in specific arrest at the larval-larval, larval-pupal or pupal-adult molts, depending on time of injection of double-stranded RNAs, loss of structural integrity and chitin staining and loss of peritrophic matrix-associated chitin. Down-regulation of transcripts at the mature adult stage results in cessation of oviposition in females, as well as fat body depletion and eventual death in both sexes
physiological function
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because the multifunctional ST0452 protein is capable of catalyzing the last two reactions (Ec 2.3.1.157 and EC 2.7.7.23 (UDP-N-acetylglucosamine diphosphorylase)) of the bacteria-type four-step biosynthesis pathway of UDP-GlcNAc from fructose 6-phosphate, the ST0452 protein plays an important role for the bacteria-type UDP-GlcNAc biosynthesis pathway in this archaeon
physiological function
-
the enzyme is involved in biosynthesis of UDP-N-acetyl-alpha-D-glucosamine, an activated and essential form of N-acetyl-alpha-D-glucosamine that is an important component in the polysaccharide structure of most organisms
physiological function
-
the enzyme binds N-acetylglucosamine-1-phosphate and UTP, and catalyzes an uridyltransfer reaction to synthesize UDP-GlcNAc, an important precursor for cell-wall biosynthesis
physiological function
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the product of the GlmU catalyzed reactions, UDP-N-acetylglucosamine, is a significant precursor for the peptidoglycan and LPS biosynthesis in Gram-positive and Gram-negative bacteria, respectively
physiological function
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the bifunctional UDP-N-acetylglucosamine pyrophosphorylase/glucosamine-1-phosphate N-acetyltransferase enzyme GlmU is an essential gene in Yersinia
physiological function
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the enzyme is one of the pathogen proteins that bind to human interleukin-8, IL-8. The binding interaction of mycobacterial proteins AtsG, GlmU and SahH with human IL-8 may indicate that these proteins participate in the modulation of the early events of infection with tubercle bacilli and could affect pathogen attachment to target cells. Interleukin-8 belongs to the family of CXC chemokines and functions as a chemoattractant and activator of different subsets of leukocytes
physiological function
-
the acetyl- and uridyltransferase activities of GlmUMtb are independently essential for bacterial survival in vitro, and GlmUMtb is also essential for mycobacterial survival in THP-1 cells as well as in guinea pigs. The administration of Oxa33, a novel oxazolidine derivative that specifically inhibits GlmUMtb, to infected mice results in significant decrease in the bacillary load. The synthesis of the two metabolic intermediates N-acetylglucosamine-1-phosphate (GlcNAc-1-P) and UDP-GlcNAc is catalyzed by the C- and N-terminal domains, respectively
physiological function
-
N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) is a pivotal bifunctional enzyme, its N- and C-terminal domains catalyze uridyltransferase, EC 2.7.7.23, and acetyltransferase, EC 2.3.1.157, activities, respectively. Final product of GlmU catalyzed reaction, uridine-diphospho-N-acetylglucosamine (UDP-GlcNAc), acts as sugar donor providing GlcNAc residues in the synthesis of peptidoglycan and a disaccharide linker (D-N-GlcNAc-1-rhamnose), the key structural components of Mycobacterium tuberculosis cell wall
physiological function
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the enzyme catalyzes the final reaction in the biosynthesis of UDP-GlcNAc, an essential metabolite in many organisms including Trypanosoma brucei,
physiological function
the JNK/AP-1 signaling cascade transcriptionally activates BMP signaling in leading edge epidermal cells, while the mummy (mmy) gene product is required for dorsal closure, and functions as a BMP signaling antagonist. The evolutionarily conserved JNK/AP-1 (Jun N-terminal kinase/activator protein 1) and BMP (bone morphogenetic protein) signaling cascades are deployed hierarchically to regulate dorsal closure in the fruit fly Drosophila melanogaster. The mmy gene product is a type of epidermal BMP regulator that transforms a BMP ligand from a long to a short range signal. Gene mmy codes for the single UDP-N-acetylglucosamine pyrophosphorylase in Drosophila, and its requirement for attenuating epidermal BMP signaling during dorsal closure points to another role for glycosylation in defining a highly restricted BMP activity field in the fly. In addition to being the building block of chitin, UDP-GlcNAc is an essential precursor for the synthesis of heparin and chondroitin sulfate proteoglycans, the former having been shown to play an essential role in modulating the effects of Dpp/BMP, Wingless (Wg)/WNT, and Hedgehog (Hh) morphogen signaling in Drosophila and other eukaryotes, usually as a facilitator of long-range signaling. Crucial role for Mmy in regulating embryonic Dpp signaling. Mmy modulation of Dpp signaling is Dpp-dependent and AP-1-independent; the mmy gene product isoform RA is an orthologue of the yeast N-acetylglucosamine diphosphorylase QRI1. In Drosophila melanogaster, mmy mutants exhibit a variety of highly penetrant phenotypes, ranging from cuticle defects associated with a failure to synthesize chitin to cuticle defects associated with well-characterized decapentaplegic-dependent closure abnormalities. UDP-N-acetylglucosamine diphosphorylase activity is required to spatially limit decapentaplegic, the Drosophila melanogaster BMP homolog, activity in a JNK/AP-1-independent fashion
physiological function
KT282116;, KT282117;
knockdown of UAP1 reduces chitin contents in whole larvae and integument samples, thinned tracheal taenidia, impairs larval-larval molt, larval-pupal ecdysis and adult emergence. Combined knockdown of UAP1 and UAP2 causes an additive negative effect; silencing of LdUAP2 significantly reduces foliage consumption, decreases chitin content in midgut samples, damages peritrophic matrix, and retards larval growth; the enzyme is involved in the biosynthesis of chitin, an essential component of the epidermal cuticle and midgut peritrophic matrix in insects; the enzyme is involved in the biosynthesis of chitin, an essential component of the epidermal cuticle and midgut peritrophic matrix in insects
physiological function
spl29 mutants display early leaf senescence, chloroplast degradation and both upregulation of senescence transcription factors and senescence-associated genes, and downregulation of photosynthesis-related genes. Defence responses are induced in the spl29 mutant. Reactive oxygen species, including O2 – and H2O2, accumulate in spl29 plants, there is also increased malondialdehyde content. The plant hormones jasmonic acid and abscisic acid also accumulate in spl29 plants; SPL29 or UAP1 is probably involved in regulating leaf senescence and defence responses in rice. Leaf senescence is a complex process controlled by a large number of different genes
physiological function
T1RR64;, T1RRG3;
injection of early second- and fifth-instar nymphs (1-day-old) or middle second- and fifth-instar nymphs (3- to 4-day-old) with UAP2 RNAi does not interfere with normal development and molting of insects; injection of early second- and fifth-instar nymphs (1-day-old) with UAP1 RNAi results in 100% mortality 2 days after the injection. Injection of middle second- and fifth-instar nymphs (3- to 4-day-old) with UAP1 RNAi results in 100% mortality during their next molting process; the enzyme functions in the formation of extracellular matrix by producing N-acetylglucosamine (GlcNAc) residues needed for chitin biosynthesis and protein glycosylation; the enzyme functions in the formation of extracellular matrix by producing N-acetylglucosamine (GlcNAc) residues needed for chitin biosynthesis and protein glycosylation
physiological function
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N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) is a bifunctional enzyme, its N- and C-terminal domains catalyze uridyltransferase, EC 2.7.7.23, and acetyltransferase, EC 2.3.1.157, activities, respectively. Final product of GlmU catalyzed reaction
physiological function
-
N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) is exclusive to prokaryotes and a bifunctional enzyme that synthesizes UDP-GlcNAc, an important component of the cell wall of many microorganisms
physiological function
-
the product of the GlmU catalyzed reactions, UDP-N-acetylglucosamine, is a significant precursor for the peptidoglycan and LPS biosynthesis in Gram-positive and Gram-negative bacteria, respectively
-
physiological function
-
the acetyl- and uridyltransferase activities of GlmUMtb are independently essential for bacterial survival in vitro, and GlmUMtb is also essential for mycobacterial survival in THP-1 cells as well as in guinea pigs. The administration of Oxa33, a novel oxazolidine derivative that specifically inhibits GlmUMtb, to infected mice results in significant decrease in the bacillary load. The synthesis of the two metabolic intermediates N-acetylglucosamine-1-phosphate (GlcNAc-1-P) and UDP-GlcNAc is catalyzed by the C- and N-terminal domains, respectively; the enzyme is one of the pathogen proteins that bind to human interleukin-8, IL-8. The binding interaction of mycobacterial proteins AtsG, GlmU and SahH with human IL-8 may indicate that these proteins participate in the modulation of the early events of infection with tubercle bacilli and could affect pathogen attachment to target cells. Interleukin-8 belongs to the family of CXC chemokines and functions as a chemoattractant and activator of different subsets of leukocytes
-
physiological function
-
N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) is a pivotal bifunctional enzyme, its N- and C-terminal domains catalyze uridyltransferase, EC 2.7.7.23, and acetyltransferase, EC 2.3.1.157, activities, respectively. Final product of GlmU catalyzed reaction, uridine-diphospho-N-acetylglucosamine (UDP-GlcNAc), acts as sugar donor providing GlcNAc residues in the synthesis of peptidoglycan and a disaccharide linker (D-N-GlcNAc-1-rhamnose), the key structural components of Mycobacterium tuberculosis cell wall; the acetyl- and uridyltransferase activities of GlmUMtb are independently essential for bacterial survival in vitro, and GlmUMtb is also essential for mycobacterial survival in THP-1 cells as well as in guinea pigs. The administration of Oxa33, a novel oxazolidine derivative that specifically inhibits GlmUMtb, to infected mice results in significant decrease in the bacillary load. The synthesis of the two metabolic intermediates N-acetylglucosamine-1-phosphate (GlcNAc-1-P) and UDP-GlcNAc is catalyzed by the C- and N-terminal domains, respectively; the enzyme is one of the pathogen proteins that bind to human interleukin-8, IL-8. The binding interaction of mycobacterial proteins AtsG, GlmU and SahH with human IL-8 may indicate that these proteins participate in the modulation of the early events of infection with tubercle bacilli and could affect pathogen attachment to target cells. Interleukin-8 belongs to the family of CXC chemokines and functions as a chemoattractant and activator of different subsets of leukocytes
-
physiological function
-
spl29 mutants display early leaf senescence, chloroplast degradation and both upregulation of senescence transcription factors and senescence-associated genes, and downregulation of photosynthesis-related genes. Defence responses are induced in the spl29 mutant. Reactive oxygen species, including O2 – and H2O2, accumulate in spl29 plants, there is also increased malondialdehyde content. The plant hormones jasmonic acid and abscisic acid also accumulate in spl29 plants; SPL29 or UAP1 is probably involved in regulating leaf senescence and defence responses in rice. Leaf senescence is a complex process controlled by a large number of different genes
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physiological function
-
because the multifunctional ST0452 protein is capable of catalyzing the last two reactions (Ec 2.3.1.157 and EC 2.7.7.23 (UDP-N-acetylglucosamine diphosphorylase)) of the bacteria-type four-step biosynthesis pathway of UDP-GlcNAc from fructose 6-phosphate, the ST0452 protein plays an important role for the bacteria-type UDP-GlcNAc biosynthesis pathway in this archaeon; the enzyme is involved in biosynthesis of UDP-N-acetyl-alpha-D-glucosamine, an activated and essential form of N-acetyl-alpha-D-glucosamine that is an important component in the polysaccharide structure of most organisms
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physiological function
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the bifunctional UDP-N-acetylglucosamine pyrophosphorylase/glucosamine-1-phosphate N-acetyltransferase enzyme GlmU is an essential gene in Yersinia
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additional information
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GlmU from Mycobacterium tuberculosis possesses a unique 30-residue extension at the C-terminus
additional information
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the ST0452 protein contains only two Cys residues, it is unlikely that Cys–Cys bonds contribute to its thermostability
additional information
the EhUAP binding pocket largely appears consistent with other UAPs and is likely to follow the common UAP mechanism; the EhUAP binding pocket largely appears consistent with other UAPs and is likely to follow the common UAP mechanism
additional information
the EhUAP binding pocket largely appears consistent with other UAPs and is likely to follow the common UAP mechanism; the EhUAP binding pocket largely appears consistent with other UAPs and is likely to follow the common UAP mechanism
additional information
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the Tyr103-Asp105 segment is located at the floor of the uridyltransferase active pocket and is involved in interactions with UTP and GlcNAc-1-P substrates
additional information
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GlmU forms a biological trimer, and two independent domains in each monomer catalyze two independent reactions in the protein. The enzyme uses a two-metal ion mechanism (mechanism-B). In contrast to well-established two-metal mechanism (mechanism-A) for enzymes acting on nucleic acids, mechanism-B is distinct in the way the two Mg2+ ions (Mg2+A and Mg2+B) are positioned and stabilized. Analysis of the catalytic mechanism for the uridyltransfer reaction in GlmU, role of metal ions in substrate binding, overview
additional information
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the ST0452 protein contains only two Cys residues, it is unlikely that Cys–Cys bonds contribute to its thermostability
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additional information
Sulfolobus tokodaii DSM 16993 / JCM 10545 / NBRC 100140 / 7
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the ST0452 protein contains only two Cys residues, it is unlikely that Cys–Cys bonds contribute to its thermostability
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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
CTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + CDP-N-acetyl-alpha-D-glucosamine
-
-
-
-
?
diphosphate + UDP-N-acetyl-D-galactosamine
UTP + N-acetyl-alpha-D-galactosamine 1-phosphate
N-acetyl-4-deoxy-alpha-D-glucosamine 1-phosphate + UTP
UDP-N-acetyl-4-deoxy-alpha-D-glucosamine + diphosphate
-
-
yield: 59%
-
?
N-acetyl-6-deoxy-6-azido-alpha-D-glucosamine 1-phosphate + UTP
UDP-N-acetyl-6-deoxy-6-azido-alpha-D-glucosamine + diphosphate
-
-
yield: 20%
-
?
N-acetyl-6-deoxy-alpha-D-galactosamine 1-phosphate + UTP
UDP-N-acetyl-6-deoxy-alpha-D-galactosamine + diphosphate
-
-
yield: 55%
-
?
N-acetyl-6-deoxy-alpha-D-glucosamine 1-phosphate + UTP
UDP-N-acetyl-6-deoxy-alpha-D-glucosamine + diphosphate
-
-
yield: 50%
-
?
N-acetyl-alpha-D-allopyranosylamine 1-phosphate + UTP
UDP-N-acetyl-alpha-D-allopyranosylamine + diphosphate
-
-
yield: 20%
-
?
N-acetyl-alpha-D-galactosamine 1-phosphate + UTP
UDP-N-acetyl-alpha-D-galactosamine + diphosphate
-
-
yield: 65%
-
?
N-acetyl-alpha-D-glucosamine 1-phosphate + UTP
UDP-N-acetyl-alpha-D-glucosamine + diphosphate
N-acetylglucosamine 1-phosphate + uridine 5'-triphosphate
uridine-diphospho-N-acetylglucosamine + diphosphate
-
-
-
-
r
N-azidoacetyl-alpha-D-glucosamine 1-phosphate + UTP
UDP-N-azidoacetyl-alpha-D-glucosamine + diphosphate
-
-
yield: 44%
-
?
N-butanoyl-alpha-D-glucosamine 1-phosphate + UTP
UDP-N-butanoyl-alpha-D-glucosamine + diphosphate
-
-
yield: 27%
-
?
N-propanoyl-alpha-D-galactosamine 1-phosphate + UTP
UDP-N-propanoyl-alpha-D-galactosamine + diphosphate
-
-
yield: 10%
-
?
N-propanoyl-alpha-D-glucosamine 1-phosphate + UTP
UDP-N-propanoyl-alpha-D-glucosamine + diphosphate
-
-
yield: 57%
-
?
UDP-N-acetyl-D-galactosamine + diphosphate
N-acetyl-D-galactosamine 1-phosphate + UTP
-
-
-
r
UDP-N-acetyl-D-glucosamine + diphosphate
N-acetyl-D-glucosamine 1-phosphate + UTP
-
-
-
r
UTP + N-acetyl-alpha-D-galactosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-galactosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
UTP + N-acetylglucosamine 1-phosphate
diphosphate + UDP-N-acetyl-D-glucosamine
-
-
-
?
diphosphate + UDP-glucose
UTP + D-glucose 1-phosphate
-
30% of the activity with UDP-N-acetylglucosamine
-
-
?
diphosphate + UDP-N-acetyl-D-galactosamine
UTP + N-acetyl-alpha-D-galactosamine 1-phosphate
-
-
-
-
?
diphosphate + UDP-N-acetyl-D-galactosamine
UTP + N-acetyl-alpha-D-galactosamine 1-phosphate
-
2-3 times more active with N-acetyl-D-galactosamine 1-phosphate than with N-acetyl-D-glucosamine 1-phosphate, AGX2 8 times less active with N-acetyl-D-galactosamine 1-phosphate than with N-acetyl-D-glucosamine 1-phosphate
-
-
-
diphosphate + UDP-N-acetyl-D-galactosamine
UTP + N-acetyl-alpha-D-galactosamine 1-phosphate
-
2.8% of the activity with UDP-N-acetylglucosamine
-
-
?
diphosphate + UDP-N-acetyl-D-galactosamine
UTP + N-acetyl-alpha-D-galactosamine 1-phosphate
-
-
-
r
diphosphate + UDP-N-acetyl-D-galactosamine
UTP + N-acetyl-alpha-D-galactosamine 1-phosphate
-
-
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
involved in the interconversion of various amino sugars and in the synthesis of mucopolysaccharides, glycopeptides, chitin
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
the reaction proceeds as an SN2 reaction
-
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
involved in synthesis of peptidoglycan and lipopolysaccharide
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
involved in synthesis of peptidoglycan and lipopolysaccharide
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
involved in synthesis of peptidoglycan and lipopolysaccharide
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
involved in synthesis of peptidoglycan and lipopolysaccharide
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
enzyme of the Leloir pathway
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
key enzyme of encystment
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
involved in the interconversion of various amino sugars and in the synthesis of mucopolysaccharides, glycopeptides, chitin
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
involved in the interconversion of various amino sugars and in the synthesis of mucopolysaccharides, glycopeptides, chitin
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
involved in the interconversion of various amino sugars and in the synthesis of mucopolysaccharides, glycopeptides, chitin
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
highly specific, no activity with any other sugar nucloetide tested
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
involved in synthesis of peptidoglycan and teichoic acid
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
involved in the interconversion of various amino sugars and in the synthesis of mucopolysaccharides, glycopeptides, chitin
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
highly specific, no activity with any other sugar nucloetide tested
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
involved in the interconversion of various amino sugars and in the synthesis of mucopolysaccharides, glycopeptides, chitin
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
highly specific, no activity with any other sugar nucloetide tested
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
involved in synthesis of peptidoglycan and teichoic acid
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
involved in the interconversion of various amino sugars and in the synthesis of mucopolysaccharides, glycopeptides, chitin
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
involved in the interconversion of various amino sugars and in the synthesis of mucopolysaccharides, glycopeptides, chitin
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
deficiency mutant fully swollen and some are lysed
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
involved in synthesis of peptidoglycan and lipopolysaccharide
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
involved in synthesis of peptidoglycan and lipopolysaccharide
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
involved in formation of N-linked oligosaccharides
-
r
N-acetyl-alpha-D-glucosamine 1-phosphate + UTP
UDP-N-acetyl-alpha-D-glucosamine + diphosphate
-
-
yield: 40%
-
?
N-acetyl-alpha-D-glucosamine 1-phosphate + UTP
UDP-N-acetyl-alpha-D-glucosamine + diphosphate
-
-
-
?
N-acetyl-alpha-D-glucosamine 1-phosphate + UTP
UDP-N-acetyl-alpha-D-glucosamine + diphosphate
-
-
-
?
N-acetyl-D-glucosamine 1-phosphate + UTP
UDP-N-acetyl-D-glucosamine + diphosphate
-
-
-
r
N-acetyl-D-glucosamine 1-phosphate + UTP
UDP-N-acetyl-D-glucosamine + diphosphate
-
-
-
-
?
N-acetyl-D-glucosamine 1-phosphate + UTP
UDP-N-acetyl-D-glucosamine + diphosphate
-
-
-
?
N-acetyl-D-glucosamine 1-phosphate + UTP
UDP-N-acetyl-D-glucosamine + diphosphate
-
-
-
?
UTP + N-acetyl-alpha-D-galactosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-galactosamine
-
-
-
r
UTP + N-acetyl-alpha-D-galactosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-galactosamine
-
-
-
r
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
KT282116;, KT282117;
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
T1RR64;, T1RRG3;
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
-
r
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
because the multifunctional ST0452 protein is capable of catalyzing the last two reactions (Ec 2.3.1.157 and EC 2.7.7.23 (UDP-N-acetylglucosamine diphosphorylase)) of the bacteria-type four-step biosynthesis pathway of UDP-GlcNAc from fructose 6-phosphate, the ST0452 protein plays an important role for the bacteria-type UDP-GlcNAc biosynthesis pathway in this archaeon
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
the enzyme is involved in biosynthesis of UDP-N-acetyl-alpha-D-glucosamine, an activated and essential form of N-acetyl-alpha-D-glucosamine that is an important component in the polysaccharide structure of most organisms
-
-
r
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
the enzyme also shows activity of EC 2.7.7.24, glucose-1-phosphate thymidylyltransferase
-
-
r
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
the multifunctional enzyme also shows activity with UTP + alpha-D-glucose 1-phosphate (EC 2.7.7.9, UTP-glucose-1-phosphate uridylyltransferase), UTP + N-acetylglucosamine 1-phosphate (EC 2.7.7.24, glucose-1-phosphate thymidylyltransferase), dTTP + N-acetylglucosamine 1-phosphate (N-acetylglucosamine 1-phosphate thymidylyltransferase), dCTP + alpha-D-glucose 1-phosphate (glucose-1-phosphate cytidylyltransferase), dGTP + alpha-D-glucose 1-phosphate (glucose-1-phosphate guanylyltransferase), dATP + alpha-D-glucose 1-phosphate (glucose-1-phosphate adenylyltransferase). No activity with: alpha-D-glucose 1-phosphate + dATP, alpha-D-glucose 1-phosphate + dCTP, alpha-D-glucose 1-phosphate + dGTP, UTP + alpha-D-mannose1-phosphate, UTP + alpha-D-galactose 1-phosphate, UTP + alpha-D-glucosamine 1-phosphate
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
because the multifunctional ST0452 protein is capable of catalyzing the last two reactions (Ec 2.3.1.157 and EC 2.7.7.23 (UDP-N-acetylglucosamine diphosphorylase)) of the bacteria-type four-step biosynthesis pathway of UDP-GlcNAc from fructose 6-phosphate, the ST0452 protein plays an important role for the bacteria-type UDP-GlcNAc biosynthesis pathway in this archaeon
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
the multifunctional enzyme also shows activity with UTP + alpha-D-glucose 1-phosphate (EC 2.7.7.9, UTP-glucose-1-phosphate uridylyltransferase), UTP + N-acetylglucosamine 1-phosphate (EC 2.7.7.24, glucose-1-phosphate thymidylyltransferase), dTTP + N-acetylglucosamine 1-phosphate (N-acetylglucosamine 1-phosphate thymidylyltransferase), dCTP + alpha-D-glucose 1-phosphate (glucose-1-phosphate cytidylyltransferase), dGTP + alpha-D-glucose 1-phosphate (glucose-1-phosphate guanylyltransferase), dATP + alpha-D-glucose 1-phosphate (glucose-1-phosphate adenylyltransferase). No activity with: alpha-D-glucose 1-phosphate + dATP, alpha-D-glucose 1-phosphate + dCTP, alpha-D-glucose 1-phosphate + dGTP, UTP + alpha-D-mannose1-phosphate, UTP + alpha-D-galactose 1-phosphate, UTP + alpha-D-glucosamine 1-phosphate
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
the enzyme is involved in biosynthesis of UDP-N-acetyl-alpha-D-glucosamine, an activated and essential form of N-acetyl-alpha-D-glucosamine that is an important component in the polysaccharide structure of most organisms
-
-
r
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
the enzyme also shows activity of EC 2.7.7.24, glucose-1-phosphate thymidylyltransferase
-
-
r
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
Sulfolobus tokodaii DSM 16993 / JCM 10545 / NBRC 100140 / 7
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
-
r
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-D-glucosamine
-
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-D-glucosamine
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-D-glucosamine
-
involved in the synthesis of UDP-N-acetyl-galactoseamine, which is important for cyst wall synthesis
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-D-glucosamine
involved in the synthesis of UDP-N-acetyl-galactoseamine, which is required for cyst wall synthesis
-
-
?
additional information
?
-
enzyme additionally shows the activity of UTP-glucose-1-phosphate uridylyltransferase, EC 2.7.7.9
-
-
-
additional information
?
-
enzyme additionally shows the activity of UTP-glucose-1-phosphate uridylyltransferase, EC 2.7.7.9
-
-
-
additional information
?
-
no substrates: CTP, GTP, ITP or ATP, glucose 1-phosphate, glucosamine 1-phosphate, xylose 1-phosphate, galactose 1-phosphate, galactosamin 1-phosphate, fucose 1-phosphate, mannose 1-phosphate, galactosamine 1-phosphate, fructose 1-phosphate, or glucose 6-phosphate
-
-
-
additional information
?
-
no substrates: CTP, GTP, ITP or ATP, glucose 1-phosphate, glucosamine 1-phosphate, xylose 1-phosphate, galactose 1-phosphate, galactosamin 1-phosphate, fucose 1-phosphate, mannose 1-phosphate, galactosamine 1-phosphate, fructose 1-phosphate, or glucose 6-phosphate
-
-
-
additional information
?
-
-
enzyme shows relaxed tolerance for modifications at N-acyl, C-3, C-4, and C-6 positions, with a preference for small substituent groups. The yields are low to moderate (10-65%) and some sugar-1-Ps fail to generate the corresponding UDP-sugars due to the steric problem
-
-
-
additional information
?
-
the N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase (GlmU) enzyme is a bifunctional enzyme with both acetyltransferase and uridylyltransferase (pyrophosphorylase) activities, catalyzing the reactions of EC 2.3.1.157, N-acetylglucosamine-1-phosphate uridyltransferase, and 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase. Acetyltransfer precedes uridyltransfer with both the acetyltransferase and uridyltransferase reactions taking place in two separable active sites in bifunctional GlmU where the acetyltransferase domain of GlmU does not show homology with its eukaryotic counterpart
-
-
-
additional information
?
-
-
the uridyltransferase domain of GlmU exhibits a flexible substrate specificity, roles of several highly conserved amino acid residues involved in substrate binding and recognition, overview. Besides UTP, the enzyme also shows activity with CTP, ATP, and slightly with dATP
-
-
-
additional information
?
-
the N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase (GlmU) enzyme is a bifunctional enzyme with both acetyltransferase and uridylyltransferase (pyrophosphorylase) activities, catalyzing the reactions of EC 2.3.1.157, N-acetylglucosamine-1-phosphate uridyltransferase, and 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase. Acetyltransfer precedes uridyltransfer with both the acetyltransferase and uridyltransferase reactions taking place in two separable active sites in bifunctional GlmU where the acetyltransferase domain of GlmU does not show homology with its eukaryotic counterpart
-
-
-
additional information
?
-
-
the human and trypanosome enzymes both display a strictly ordered bi-bi mechanism, but with the order of substrate binding reversed. Human UAP does not bind UTP alone, and although it does show significant binding to GlcNAc-1-P, it is not possible to calculate an affinity due to complex binding kinetics
-
-
-
additional information
?
-
the human and trypanosome enzymes both display a strictly ordered bi-bi mechanism, but with the order of substrate binding reversed. Human UAP does not bind UTP alone, and although it does show significant binding to GlcNAc-1-P, it is not possible to calculate an affinity due to complex binding kinetics
-
-
-
additional information
?
-
the molecular recognition of the enzyme with the substrates occurs mainly by hydrogen bonds between ligands and Arg116, Arg383, Gly381, and Lys408 amino acids, and few hydrophobic interactions with Tyr382 and Lys123 residues
-
-
-
additional information
?
-
-
the molecular recognition of the enzyme with the substrates occurs mainly by hydrogen bonds between ligands and Arg116, Arg383, Gly381, and Lys408 amino acids, and few hydrophobic interactions with Tyr382 and Lys123 residues
-
-
-
additional information
?
-
-
bifunctional enzyme that catalyzes two consecutive reactions leading to the biosynthesis of UDP-N-acetylglucosamine, in the first reaction, GlmU catalyzes the CoA-dependent acetylation of glucosamine-1-phosphate to afford N-acetylglucosamine-1-phosphate, in the second reaction, the UMP moiety from a UTP molecule is transferred to N-acetyl-alpha-D-glucosamine 1-phosphate to give the final product UDP-GlcNAc
-
-
-
additional information
?
-
-
N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) is a bifunctional enzyme catalyzing the reactions of EC 2.3.1.157, N-acetylglucosamine-1-phosphate uridyltransferase, and 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase, the enzyme catalyzes the two reactions, acetyl transfer and uridyl transfer, at two independent domains, regulation, overview
-
-
-
additional information
?
-
N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) is a bifunctional enzyme catalyzing the reactions of EC 2.3.1.157, N-acetylglucosamine-1-phosphate uridyltransferase, and 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase, the enzyme catalyzes the two reactions, acetyl transfer and uridyl transfer, at two independent domains, regulation, overview
-
-
-
additional information
?
-
-
N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) is a pivotal bifunctional enzyme, its N- and C-terminal domains catalyzes uridyltransferase, EC 2.7.7.23, and acetyltransferase, EC 2.3.1.157, activities, respectively
-
-
-
additional information
?
-
-
the bifunctional role of GlmU arises from two independent domains of the enzyme which possess acetyltransferase, EC 2.3.1.157, and uridyltransferase, EC 2.7.7.23, activities. The acetyltransferase domain, found in the C-terminus of the protein, is responsible for the first step of the reaction, in which an acetyl group is transferred from AcCoA to GlcN-1-P forming GlcNAc-1-P. GlcNAc-1-P then serves as a substrate for the uridyltransferase active site in the N-terminus of the enzyme which forms UDP-GlcNAc
-
-
-
additional information
?
-
-
the N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase (GlmU) enzyme is a bifunctional enzyme with both acetyltransferase and uridylyltransferase (pyrophosphorylase) activities, catalyzing the reactions of EC 2.3.1.157, N-acetylglucosamine-1-phosphate uridyltransferase, and 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase. The synthesis of the two metabolic intermediates N-acetylglucosamine-1-phosphate (GlcNAc-1-P) and UDP-GlcNAc is catalyzed by the C- and N-terminal domains, respectively. UDP-GlcNAc is a key metabolite essential for the synthesis of peptidoglycan, disaccharide linker, arabinogalactan and mycothiols
-
-
-
additional information
?
-
-
coupled assay method: coupling of the two enzyme reactions via N-acetyl-alpha-D-glucosamine 1-phosphate for determination of the acetyl transferase activity of the enzyme
-
-
-
additional information
?
-
coupled assay method: coupling of the two enzyme reactions via N-acetyl-alpha-D-glucosamine 1-phosphate for determination of the acetyl transferase activity of the enzyme
-
-
-
additional information
?
-
-
development of a double-enzyme-coupled continuous assay for Mycobacterium tuberculosis GlmU uridyltransferase. The assay used excess amounts of two coupling enzymes, namely inorganic pyrophosphatase (IPP) (EC 3.6.1.1) and purine nucleoside phosphorylase (PNPase) (EC 2.4.2.1) in the presence of 2-amino-6-mercapto-7-methylpurine ribonucleoside. the pyrophosphate produced by GlmU uridyltransferase is subsequently hydrolysed to phosphate by IPP. The phosphate then serves as a substrate for PNPase which catalyses the phosphorolytic cleavage of the glycosidic bond in 2-amino-6-mercapto-7-methylpurine ribonucleoside, resulting in the formation of 2-amino-6-mercapto-7-methylpurine that can be detected spectroscopically
-
-
-
additional information
?
-
-
enzyme GlmU is specific for its natural substrates UTP and N-acetyl-alpha-D-glucosamine 1-phosphate, substrate specificity, overview. No activity with ATP and TTP as well as glucose-1-phosphate and mannose-1-phosphate, very poor activity with GTP, low activity with CTP
-
-
-
additional information
?
-
-
the recombinant enzyme binds to human interleukin-8, interaction analysis with human neutrophils, overview
-
-
-
additional information
?
-
-
the recombinant enzyme binds to human interleukin-8, interaction analysis with human neutrophils, overview
-
-
-
additional information
?
-
-
the N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase (GlmU) enzyme is a bifunctional enzyme with both acetyltransferase and uridylyltransferase (pyrophosphorylase) activities, catalyzing the reactions of EC 2.3.1.157, N-acetylglucosamine-1-phosphate uridyltransferase, and 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase. The synthesis of the two metabolic intermediates N-acetylglucosamine-1-phosphate (GlcNAc-1-P) and UDP-GlcNAc is catalyzed by the C- and N-terminal domains, respectively. UDP-GlcNAc is a key metabolite essential for the synthesis of peptidoglycan, disaccharide linker, arabinogalactan and mycothiols
-
-
-
additional information
?
-
-
bifunctional enzyme that catalyzes two consecutive reactions leading to the biosynthesis of UDP-N-acetylglucosamine, in the first reaction, GlmU catalyzes the CoA-dependent acetylation of glucosamine-1-phosphate to afford N-acetylglucosamine-1-phosphate, in the second reaction, the UMP moiety from a UTP molecule is transferred to N-acetyl-alpha-D-glucosamine 1-phosphate to give the final product UDP-GlcNAc
-
-
-
additional information
?
-
the recombinant enzyme binds to human interleukin-8, interaction analysis with human neutrophils, overview
-
-
-
additional information
?
-
-
the N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase (GlmU) enzyme is a bifunctional enzyme with both acetyltransferase and uridylyltransferase (pyrophosphorylase) activities, catalyzing the reactions of EC 2.3.1.157, N-acetylglucosamine-1-phosphate uridyltransferase, and 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase. The synthesis of the two metabolic intermediates N-acetylglucosamine-1-phosphate (GlcNAc-1-P) and UDP-GlcNAc is catalyzed by the C- and N-terminal domains, respectively. UDP-GlcNAc is a key metabolite essential for the synthesis of peptidoglycan, disaccharide linker, arabinogalactan and mycothiols
-
-
-
additional information
?
-
-
N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) is a pivotal bifunctional enzyme, its N- and C-terminal domains catalyzes uridyltransferase, EC 2.7.7.23, and acetyltransferase, EC 2.3.1.157, activities, respectively
-
-
-
additional information
?
-
-
the bifunctional role of GlmU arises from two independent domains of the enzyme which possess acetyltransferase, EC 2.3.1.157, and uridyltransferase, EC 2.7.7.23, activities. The acetyltransferase domain, found in the C-terminus of the protein, is responsible for the first step of the reaction, in which an acetyl group is transferred from AcCoA to GlcN-1-P forming GlcNAc-1-P. GlcNAc-1-P then serves as a substrate for the uridyltransferase active site in the N-terminus of the enzyme which forms UDP-GlcNAc
-
-
-
additional information
?
-
-
development of a double-enzyme-coupled continuous assay for Mycobacterium tuberculosis GlmU uridyltransferase. The assay used excess amounts of two coupling enzymes, namely inorganic pyrophosphatase (IPP) (EC 3.6.1.1) and purine nucleoside phosphorylase (PNPase) (EC 2.4.2.1) in the presence of 2-amino-6-mercapto-7-methylpurine ribonucleoside. the pyrophosphate produced by GlmU uridyltransferase is subsequently hydrolysed to phosphate by IPP. The phosphate then serves as a substrate for PNPase which catalyses the phosphorolytic cleavage of the glycosidic bond in 2-amino-6-mercapto-7-methylpurine ribonucleoside, resulting in the formation of 2-amino-6-mercapto-7-methylpurine that can be detected spectroscopically
-
-
-
additional information
?
-
-
the enzyme has multiple sugar-1-phosphate nucleotidylyltransferase, EC 2.7.7.37, and amino-sugar-1-phosphate acetyltransferase, EC 2.3.1.157, activities, overview. In addition to glucosamine-1-phosphate acetyltransferase activity, it possesses unique galactosamine-1-phosphate acetyltransferase activity. Also, the enzyme possesses GlcNAc-1-phosphate nucleotidylyltransferase, EC 2.7.7.23, and N-acetyl-D-galactosamine-1-phosphate uridyltransferase, EC 2.7.7.83, activities, as well as the expected glucose-1-phosphate thymidylyltransferase, EC 2.7.7.24, activity
-
-
-
additional information
?
-
-
the enzyme has multiple sugar-1-phosphate nucleotidylyltransferase, EC 2.7.7.37, and amino-sugar-1-phosphate acetyltransferase, EC 2.3.1.157, activities, overview. In addition to glucosamine-1-phosphate acetyltransferase activity, it possesses unique galactosamine-1-phosphate acetyltransferase activity. Also, the enzyme possesses GlcNAc-1-phosphate nucleotidylyltransferase, EC 2.7.7.23, and N-acetyl-D-galactosamine-1-phosphate uridyltransferase, EC 2.7.7.83, activities, as well as the expected glucose-1-phosphate thymidylyltransferase, EC 2.7.7.24, activity
-
-
-
additional information
?
-
Sulfolobus tokodaii DSM 16993 / JCM 10545 / NBRC 100140 / 7
the enzyme has multiple sugar-1-phosphate nucleotidylyltransferase, EC 2.7.7.37, and amino-sugar-1-phosphate acetyltransferase, EC 2.3.1.157, activities, overview. In addition to glucosamine-1-phosphate acetyltransferase activity, it possesses unique galactosamine-1-phosphate acetyltransferase activity. Also, the enzyme possesses GlcNAc-1-phosphate nucleotidylyltransferase, EC 2.7.7.23, and N-acetyl-D-galactosamine-1-phosphate uridyltransferase, EC 2.7.7.83, activities, as well as the expected glucose-1-phosphate thymidylyltransferase, EC 2.7.7.24, activity
-
-
-
additional information
?
-
Q386Q8;
the human and trypanosome enzymes both display a strictly ordered bi-bi mechanism, but with the order of substrate binding reversed. Trypanosoma brucei UAP binds UTP alone with a KD of 83.1 microM, but does not bind GlcNAc-1-P alone
-
-
-
additional information
?
-
Trypanosoma brucei brucei 927 / 4 GUTat10.1 / TREU927
Q386Q8;
the human and trypanosome enzymes both display a strictly ordered bi-bi mechanism, but with the order of substrate binding reversed. Trypanosoma brucei UAP binds UTP alone with a KD of 83.1 microM, but does not bind GlcNAc-1-P alone
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATES
NATURAL PRODUCTS
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
N-acetyl-D-glucosamine 1-phosphate + UTP
UDP-N-acetyl-D-glucosamine + diphosphate
-
-
-
-
?
N-acetylglucosamine 1-phosphate + uridine 5'-triphosphate
uridine-diphospho-N-acetylglucosamine + diphosphate
-
-
-
-
r
UTP + N-acetyl-alpha-D-galactosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-galactosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
O74933
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
O74933
involved in the interconversion of various amino sugars and in the synthesis of mucopolysaccharides, glycopeptides, chitin
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
P0ACC7
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
involved in synthesis of peptidoglycan and lipopolysaccharide
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
involved in synthesis of peptidoglycan and lipopolysaccharide
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
P0ACC7
involved in synthesis of peptidoglycan and lipopolysaccharide
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
involved in synthesis of peptidoglycan and lipopolysaccharide
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
enzyme of the Leloir pathway
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
key enzyme of encystment
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
involved in the interconversion of various amino sugars and in the synthesis of mucopolysaccharides, glycopeptides, chitin
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
involved in the interconversion of various amino sugars and in the synthesis of mucopolysaccharides, glycopeptides, chitin
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
involved in the interconversion of various amino sugars and in the synthesis of mucopolysaccharides, glycopeptides, chitin
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
Q50986
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
involved in synthesis of peptidoglycan and teichoic acid
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
involved in the interconversion of various amino sugars and in the synthesis of mucopolysaccharides, glycopeptides, chitin
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
involved in the interconversion of various amino sugars and in the synthesis of mucopolysaccharides, glycopeptides, chitin
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
P43123
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
involved in synthesis of peptidoglycan and teichoic acid
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
involved in the interconversion of various amino sugars and in the synthesis of mucopolysaccharides, glycopeptides, chitin
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
P43123
involved in the interconversion of various amino sugars and in the synthesis of mucopolysaccharides, glycopeptides, chitin
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
P43123
deficiency mutant fully swollen and some are lysed
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
Q97R46
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
Q97R46
involved in synthesis of peptidoglycan and lipopolysaccharide
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
involved in synthesis of peptidoglycan and lipopolysaccharide
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
involved in formation of N-linked oligosaccharides
-
r
UTP + N-acetyl-alpha-D-galactosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-galactosamine
Q6ZJ97
-
-
-
r
UTP + N-acetyl-alpha-D-galactosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-galactosamine
Q6ZJ97
-
-
-
r
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
Q9Y0Z0
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
C4M036, C4MA87
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
P0ACC7
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
P0ACC7
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
KT282116, KT282117
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
T1RR64, T1RRG3
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
E2LRY8
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
P9WMN3
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
-
r
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
P9WMN3
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
Q6ZJ97
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
Q6ZJ97
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
because the multifunctional ST0452 protein is capable of catalyzing the last two reactions (Ec 2.3.1.157 and EC 2.7.7.23 (UDP-N-acetylglucosamine diphosphorylase)) of the bacteria-type four-step biosynthesis pathway of UDP-GlcNAc from fructose 6-phosphate, the ST0452 protein plays an important role for the bacteria-type UDP-GlcNAc biosynthesis pathway in this archaeon
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
the enzyme is involved in biosynthesis of UDP-N-acetyl-alpha-D-glucosamine, an activated and essential form of N-acetyl-alpha-D-glucosamine that is an important component in the polysaccharide structure of most organisms
-
-
r
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
because the multifunctional ST0452 protein is capable of catalyzing the last two reactions (Ec 2.3.1.157 and EC 2.7.7.23 (UDP-N-acetylglucosamine diphosphorylase)) of the bacteria-type four-step biosynthesis pathway of UDP-GlcNAc from fructose 6-phosphate, the ST0452 protein plays an important role for the bacteria-type UDP-GlcNAc biosynthesis pathway in this archaeon
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
the enzyme is involved in biosynthesis of UDP-N-acetyl-alpha-D-glucosamine, an activated and essential form of N-acetyl-alpha-D-glucosamine that is an important component in the polysaccharide structure of most organisms
-
-
r
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
Sulfolobus tokodaii DSM 16993 / JCM 10545 / NBRC 100140 / 7
Q975F9
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
-
r
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-D-glucosamine
-
involved in the synthesis of UDP-N-acetyl-galactoseamine, which is important for cyst wall synthesis
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-D-glucosamine
Q8MUP8
involved in the synthesis of UDP-N-acetyl-galactoseamine, which is required for cyst wall synthesis
-
-
?
additional information
?
-
P0ACC7
the N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase (GlmU) enzyme is a bifunctional enzyme with both acetyltransferase and uridylyltransferase (pyrophosphorylase) activities, catalyzing the reactions of EC 2.3.1.157, N-acetylglucosamine-1-phosphate uridyltransferase, and 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase. Acetyltransfer precedes uridyltransfer with both the acetyltransferase and uridyltransferase reactions taking place in two separable active sites in bifunctional GlmU where the acetyltransferase domain of GlmU does not show homology with its eukaryotic counterpart
-
-
-
additional information
?
-
P0ACC7
the N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase (GlmU) enzyme is a bifunctional enzyme with both acetyltransferase and uridylyltransferase (pyrophosphorylase) activities, catalyzing the reactions of EC 2.3.1.157, N-acetylglucosamine-1-phosphate uridyltransferase, and 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase. Acetyltransfer precedes uridyltransfer with both the acetyltransferase and uridyltransferase reactions taking place in two separable active sites in bifunctional GlmU where the acetyltransferase domain of GlmU does not show homology with its eukaryotic counterpart
-
-
-
additional information
?
-
-
bifunctional enzyme that catalyzes two consecutive reactions leading to the biosynthesis of UDP-N-acetylglucosamine, in the first reaction, GlmU catalyzes the CoA-dependent acetylation of glucosamine-1-phosphate to afford N-acetylglucosamine-1-phosphate, in the second reaction, the UMP moiety from a UTP molecule is transferred to N-acetyl-alpha-D-glucosamine 1-phosphate to give the final product UDP-GlcNAc
-
-
-
additional information
?
-
-
N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) is a bifunctional enzyme catalyzing the reactions of EC 2.3.1.157, N-acetylglucosamine-1-phosphate uridyltransferase, and 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase, the enzyme catalyzes the two reactions, acetyl transfer and uridyl transfer, at two independent domains, regulation, overview
-
-
-
additional information
?
-
P9WMN3
N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) is a bifunctional enzyme catalyzing the reactions of EC 2.3.1.157, N-acetylglucosamine-1-phosphate uridyltransferase, and 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase, the enzyme catalyzes the two reactions, acetyl transfer and uridyl transfer, at two independent domains, regulation, overview
-
-
-
additional information
?
-
-
N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) is a pivotal bifunctional enzyme, its N- and C-terminal domains catalyzes uridyltransferase, EC 2.7.7.23, and acetyltransferase, EC 2.3.1.157, activities, respectively
-
-
-
additional information
?
-
-
the bifunctional role of GlmU arises from two independent domains of the enzyme which possess acetyltransferase, EC 2.3.1.157, and uridyltransferase, EC 2.7.7.23, activities. The acetyltransferase domain, found in the C-terminus of the protein, is responsible for the first step of the reaction, in which an acetyl group is transferred from AcCoA to GlcN-1-P forming GlcNAc-1-P. GlcNAc-1-P then serves as a substrate for the uridyltransferase active site in the N-terminus of the enzyme which forms UDP-GlcNAc
-
-
-
additional information
?
-
-
the N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase (GlmU) enzyme is a bifunctional enzyme with both acetyltransferase and uridylyltransferase (pyrophosphorylase) activities, catalyzing the reactions of EC 2.3.1.157, N-acetylglucosamine-1-phosphate uridyltransferase, and 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase. The synthesis of the two metabolic intermediates N-acetylglucosamine-1-phosphate (GlcNAc-1-P) and UDP-GlcNAc is catalyzed by the C- and N-terminal domains, respectively. UDP-GlcNAc is a key metabolite essential for the synthesis of peptidoglycan, disaccharide linker, arabinogalactan and mycothiols
-
-
-
additional information
?
-
-
the N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase (GlmU) enzyme is a bifunctional enzyme with both acetyltransferase and uridylyltransferase (pyrophosphorylase) activities, catalyzing the reactions of EC 2.3.1.157, N-acetylglucosamine-1-phosphate uridyltransferase, and 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase. The synthesis of the two metabolic intermediates N-acetylglucosamine-1-phosphate (GlcNAc-1-P) and UDP-GlcNAc is catalyzed by the C- and N-terminal domains, respectively. UDP-GlcNAc is a key metabolite essential for the synthesis of peptidoglycan, disaccharide linker, arabinogalactan and mycothiols
-
-
-
additional information
?
-
-
bifunctional enzyme that catalyzes two consecutive reactions leading to the biosynthesis of UDP-N-acetylglucosamine, in the first reaction, GlmU catalyzes the CoA-dependent acetylation of glucosamine-1-phosphate to afford N-acetylglucosamine-1-phosphate, in the second reaction, the UMP moiety from a UTP molecule is transferred to N-acetyl-alpha-D-glucosamine 1-phosphate to give the final product UDP-GlcNAc
-
-
-
additional information
?
-
-
the N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase (GlmU) enzyme is a bifunctional enzyme with both acetyltransferase and uridylyltransferase (pyrophosphorylase) activities, catalyzing the reactions of EC 2.3.1.157, N-acetylglucosamine-1-phosphate uridyltransferase, and 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase. The synthesis of the two metabolic intermediates N-acetylglucosamine-1-phosphate (GlcNAc-1-P) and UDP-GlcNAc is catalyzed by the C- and N-terminal domains, respectively. UDP-GlcNAc is a key metabolite essential for the synthesis of peptidoglycan, disaccharide linker, arabinogalactan and mycothiols
-
-
-
additional information
?
-
-
N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) is a pivotal bifunctional enzyme, its N- and C-terminal domains catalyzes uridyltransferase, EC 2.7.7.23, and acetyltransferase, EC 2.3.1.157, activities, respectively
-
-
-
additional information
?
-
-
the bifunctional role of GlmU arises from two independent domains of the enzyme which possess acetyltransferase, EC 2.3.1.157, and uridyltransferase, EC 2.7.7.23, activities. The acetyltransferase domain, found in the C-terminus of the protein, is responsible for the first step of the reaction, in which an acetyl group is transferred from AcCoA to GlcN-1-P forming GlcNAc-1-P. GlcNAc-1-P then serves as a substrate for the uridyltransferase active site in the N-terminus of the enzyme which forms UDP-GlcNAc
-
-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Co2+
Mg2+
Mn2+
Ni2+
Zn2+
Ca2+
-
2 mM. Activation of UDP-N-acetylglucosamine diphosphorylase activity in the order of decreasing effectiveness: Mg2+, Zn2+, Ca2+, Co2+, Mn2+. No activity is detectable without a divalent cation
Co2+
-
a cobalt ion substitutes for Mg2+A in the crystal structure
Co2+
-
2 mM. Activation of UDP-N-acetylglucosamine diphosphorylase activity in the order of decreasing effectiveness: Mg2+, Zn2+, Ca2+, Co2+, Mn2+. No activity is detectable without a divalent cation
Mg2+
-
; Mg2+ enhances the enzymatic activity by increasing the affinity between UTP and the enzyme
Mg2+
-
required, the enzyme utilizes two metal ions, MgA 2+ and MgB 2+, to catalyze the uridyltransfer reaction. The enzyme binds three magnesium ions and ATP at the active site. Displacement of MgB2+ from its usual catalytically competent position, as noted in the crystal structure of RNA polymerase in an inactive state, is considered to be a key factor inhibiting the reaction. In GlmUMtb[GlcNAc-1-P:ATP], the third metal ion, MgC2+ is also stabilized by one coordination interaction with Palpha and five coordination interactions with water molecules. Its coordination by Palpha results in the stabilization of an inactive conformation of ATP. Structure-function analysis, overview. The entire metal-substrate complex renders the enzyme catalytically inactive
Mg2+
-
required, two metal binding sites, site-A and site-B. The enzyme uses a two-metal ion mechanism (mechanism-B). Roles of the metal ions in substrate stabilization, nucleophile activation and transition-state stabilization, detailed overview. Mg2+A interacts with Asp114 and Asn239 and oxygens O1B and O2A of UDP-GlcNAc in addition to two water molecules. Mg2+B is coordinated with three water molecules and the oxygen atoms are contributed by UDP-GlcNAc and diphosphate. Mg2+A enables nucleophile activation and Mg2+B stabilizes the transition state
Mg2+
-
inhibitory at high concentrations; required for maximum activity
Mg2+
-
highest activity when ratio Mg2+/diphosphate is 1/10 - 1/20; required for maximum activity
Mg2+
-
2 mM. Activation of UDP-N-acetylglucosamine diphosphorylase activity in the order of decreasing effectiveness: Mg2+, Zn2+, Ca2+, Co2+, Mn2+. No activity is detectable without a divalent cation
Mn2+
or Mg2+, required; or Mg2+, required. At 5 mM, 126% of the activity with Mg2+
Mn2+
-
2 mM. Activation of UDP-N-acetylglucosamine diphosphorylase activity in the order of decreasing effectiveness: Mg2+, Zn2+, Ca2+, Co2+, Mn2+. No activity is detectable without a divalent cation
Zn2+
-
2 mM. Activation of UDP-N-acetylglucosamine diphosphorylase activity in the order of decreasing effectiveness: Mg2+, Zn2+, Ca2+, Co2+, Mn2+. No activity is detectable without a divalent cation
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2S,4R)-N-(4-((6,7-dimethoxyquinazolin-4-yl)amino)phenyl)-4-hydroxypyrrolidine-2-carboxamide
-
-
(3-hydroxyphenyl)[4-(5,6,7,8-tetrahydroquinazolin-4-ylamino)phenyl]methanone
-
30% inhibition at 0.05 mM
(4-(6,7-dimethoxyquinazolin-4-yl)piperazin-1-yl)(phenyl)-methanone
-
-
-
(S)-N-(4-((6,7-dimethoxyquinazolin-4-yl)amino)phenyl)pyrrolidine-2-carboxamide
-
-
1-(3-hydroxybenzoyl)-4-(thieno[3,2-d]pyrimidin-4-ylamino)pyridinium
-
38% inhibition at 0.05 mM
1-[(2S,3S,4R,5S)-3,4-dihydroxy-5-(hydroxymethyl)tetrahydrofuran-2-yl]dihydropyrimidine-2,4(1H,3H)-dione
2,3-dihydroxy-5-nitrophenyl 2-acetamido-2-deoxy-alpha-D-xylo-hexopyranoside
forms with UNAcP hydrogen bonds, Pi-cation and hydrophobic interactions
2-(3-((4-((6,7-dimethoxyquinazolin-4-yl)amino)phenyl)carbamoyl)phenoxy)acetic acid
-
34% inhibition at 0.05 mM
2-amino-N-(4-((6,7-dimethoxyquinazolin-4-yl)amino)phenyl)-benzamide
-
16% inhibition at 0.05 mM
2-hydroxy-5-nitrophenyl 2-acetamido-2-deoxy-alpha-D-xylo-hexopyranoside
-
2-hydroxyphenyl 2-acetamido-2-deoxy-alpha-D-xylo-hexopyranoside
-
3,4-dihydroxyphenyl 2-acetamido-2-deoxy-alpha-D-xylo-hexopyranoside
-
3-(cyanomethoxy)-N-(4-((6,7-dimethoxyquinazolin-4-yl)amino)-phenyl)benzamide
-
-
3-amino-N-(4-((6,7-dimethoxyquinazolin-4-yl)amino)phenyl)-benzamide
-
17% inhibition at 0.05 mM
3-hydroxyphenyl 2-acetamido-2-deoxy-alpha-D-xylo-hexopyranoside
-
3-nitrophenyl 2-acetamido-2-deoxy-alpha-D-xylo-hexopyranoside
-
3-[(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)oxy]-2-hydroxy-N-[2-[(3-hydroxypropyl)carbamoyl]phenyl]benzamide
-
3-[2-(1,3-benzodioxol-5-yl)-2-oxoethyl]-4-bromo-3-hydroxy-5-methyl-1,3-dihydro-2H-indol-2-one
Q386Q8;
competitive inhibitor with selectivity over the human counterpart, binds at an allosteric site absent in the human homologue that prevents the conformational rearrangement required to bind UTP
3-[2-(2,3-dihydro-1,4-benzodioxin-6-yl)-2-oxoethyl]-3-hydroxy-5-methyl-1,3-dihydro-2H-indol-2-one
-
-
3-[2-(2H-1,3-benzodioxol-5-yl)-2-oxoethyl]-3-hydroxy-6,7-dimethyl-1,3-dihydro-2H-indol-2-one
-
-
3-[2-(2H-1,3-benzodioxol-5-yl)-2-oxoethyl]-3-hydroxy-7-methyl-1,3-dihydro-2H-indol-2-one
-
-
3-[2-(2H-1,3-benzodioxol-5-yl)-2-oxoethyl]-4,6-dichloro-3-hydroxy-1,3-dihydro-2H-indol-2-one
-
-
3-[2H-(1,3-benzodioxol-5-yl)-2-oxoethyl]-4-bromo-3-hydroxy-5-methyl-1,3-dihydro-2H-indol-2-one
-
UTP-competitive inhibitor with selectivity over the human counterpart despite the high level of conservation of active site residues. The inhibitor binds at an allosteric site
-
3-[[2-acetamido-2-deoxy-alpha-D-xylo-hexopyranosyl]oxy]-2-hydroxybenzoic acid
-
3-[[2-acetamido-2-deoxy-alpha-L-xylo-hexopyranosyl]oxy]benzoic acid
-
4-(4-(benzyloxy)benzylidene-2)-(naphthalen-1-yl)oxazol-5(4H)-one
-
i.e. Oxa33, synthesis of a specific GlmU inhibitor, molecular docking study, the inhibitor binds to an allosteric site of the uridyltransferase domain, overview. Oxa33 fails to inhibit cell growth even at concentrations as high as 0.150 mM. Tyr150, Glu250 and Arg 253 are in hydrogen bonding with carbonyl oxygen over the oxazole ring, while Leu144, Pro147, Phe148, Tyr150, Ala233, Ala236 and Leu247 participate in strong hydrophobic interactions with Oxa33
-
4-chloro-N-(3-methoxypropyl)-N-[1-(2-phenylethyl)piperidin-3-yl]benzamide
a 1.9 A resolution crystal structure of this synthetic small-molecule inhibitor of GlmU is presented. The determined crystal structure indicates that the inhibitor occupies an allosteric site adjacent to the GlcNAc-1-P substrate-binding region, thus, preventing structural rearrangements that are required for the enzymatic reaction
4-chloro-N-[1-[2-(2-fluorophenyl)ethyl]piperidin-3-yl]-N-(3-methoxypropyl)benzamide
-
4-chloro-N-[1-[2-(3-fluorophenyl)ethyl]piperidin-3-yl]-N-(3-methoxypropyl)benzamide
-
4-chloro-N-[1-[2-(4-fluorophenyl)ethyl]piperidin-3-yl]-N-(3-methoxypropyl)benzamide
-
4-fluoro-N-(3-methoxypropyl)-N-[1-(2-phenylethyl)piperidin-3-yl]benzamide
-
5'-(3-[[2-acetamido-2-deoxy-alpha-L-xylo-hexopyranosyl]oxy]-2-hydroxyanilino)-5'-deoxyuridine
-
5'-deoxy-5'-[[4-(3,4-dihydroxyphenyl)-1,3-thiazol-2-yl]amino]uridine
-
37% inhibition at 2 mM
5'-[N-[2-[[2-(acetylamino)-2-deoxy-D-glucopyranosyl]oxy]acetyl]sulfamoyl]uridine
-
55% inhibition at 2 mM
5'-[[2-(cyclohexylamino)-2-oxoethyl](2,3-dihydroxybenzoyl)amino]-5'-deoxyuridine
-
10% inhibition at 2 mM
5'-[[N-[2-[[2-(acetylamino)-2-deoxy-alpha-D-glucopyranosyl]oxy]acetyl]-L-alpha-aspartyl-L-alpha-aspartyl]amino]-5'-deoxyuridine
-
60% inhibition at 2 mM
9H-fluoren-9-ylmethyl (2S)-2-([4-[(6,7-dimethoxyquinazolin-4-yl)amino]phenyl]carbamoyl)pyrrolidine-1-carboxylate
-
-
9H-fluoren-9-ylmethyl (2S)-2-[(4-aminophenyl)carbamoyl]pyrrolidine-1-carboxylate
-
-
ATP
-
the enzyme binds three magnesium ions and ATP at the active site, but shows no activity with ATP. ATP binding results in an inactive pre-catalytic enzyme–substrate complex, where it adopts an unusual conformation such that the reaction cannot be catalyzed
cyclohexyl(4-(6,7-dimethoxyquinazolin-4-yl)piperazin-1-yl)-methanone
-
-
luteolin
minimal inhibitory concentration for growth of Xanthomonas oryzae pv. oryzae, 186 microg/ml
N'-[(4-chloro-3,5-dimethylphenoxy)acetyl]-2,4-dihydroxybenzohydrazide
minimal inhibitory concentration for growth of Xanthomonas oryzae pv. oryzae, 420 microg/ml
N'1,N'6-bis[2-(naphthalen-2-yloxy)acetyl]hexanedihydrazide
minimal inhibitory concentration for growth of Xanthomonas oryzae pv. oryzae, 302 microg/ml
N-(2-((6,7-dimethoxyquinazolin-4-yl)amino)cyclohexyl)benzamide
-
-
N-(2-((6,7-dimethoxyquinazolin-4-yl)amino)cyclohexyl)cyclohexane carboxamide
-
-
N-(3,5-dimethoxyphenyl)-2,3-dihydro-4H-1,4-benzothiazine-4-carboxamide
-
-
N-(4-((6,7-dimethoxyquinazolin-4-yl)amino)phenyl)-2-hydroxybenzamide
-
14% inhibition at 0.05 mM
N-(4-((6,7-dimethoxyquinazolin-4-yl)amino)phenyl)-2-nitrobenzamide
-
13% inhibition at 0.05 mM
N-(4-((6,7-dimethoxyquinazolin-4-yl)amino)phenyl)-3-(4-fluoro-phenyl)-5-methylisoxazole-4-carboxamide
-
19% inhibition at 0.05 mM
N-(4-((6,7-dimethoxyquinazolin-4-yl)amino)phenyl)-3-hydroxybenzamide
-
35% inhibition at 0.05 mM
N-(4-((6,7-dimethoxyquinazolin-4-yl)amino)phenyl)-3-methoxy benzamide
-
38% inhibition at 0.05 mM
N-(4-((6,7-dimethoxyquinazolin-4-yl)amino)phenyl)-3-nitrobenzamide
-
-
N-(4-((6,7-dimethoxyquinazolin-4-yl)amino)phenyl)-4-fluorobenzamide
-
21% inhibition at 0.05 mM
N-(4-((6,7-dimethoxyquinazolin-4-yl)amino)phenyl)-4-hydroxybenzamide
-
18% inhibition at 0.05 mM
N-(4-((6,7-dimethoxyquinazolin-4-yl)amino)phenyl)cyclohexane carboxamide
-
22% inhibition at 2 mM
N-(4-((6,7-dimethoxyquinazolin-4-yl)amino)phenyl)pyrazine-2-carboxamide
-
19% inhibition at 0.05 mM
N-[(1R,2R,4R,6S)-6-(2,3-dihydroxy-5-nitrophenoxy)-2,3-dihydroxy-4-(hydroxymethyl)cyclohexyl]acetamide
inhibitor identified by strucutre-based drug design, best binding energy of ?95.2 kcal/mol among the compounds analyzed
N-[(2R,3R,4R,6R)-2-(2,3-dihydroxy-5-nitrophenoxy)-4,5-dihydroxy-6-(hydroxymethyl)tetrahydro-2H-pyran-3-yl]acetamide
most active inhibitor among compounds tested, forms a hydrogen bonding network with residues Arg116, Gly381, Arg383 and Lys408, with the distance ranging from 2.9 A to and 3.14 A. The hydrophobic interaction is observed with the aromatic ring of Tyr382 with a distance of 3.85 A. The aromatic ring of the inhibitor also interacts with the Lys123 through a pi-cation interaction, with a distance of 3.99 A
N-[4-[(6,7-dimethoxyquinazolin-4-yl)amino]phenyl]benzamide
-
44% inhibition at 2 mM
N-[4-[(7-hydroxy-6-methoxyquinazolin-4-yl)amino]phenyl]benzamide
-
36% inhibition at 2 mM
N1',N3'-bis(2-(1-bromonaphthalen naphthalen-2-yloxy)acetyl)isophthalohydrazide
-
-
N1',N3'-bis(2-(3-bromonaphthalen naphthalen-2-yloxy)acetyl)isophthalohydrazide
-
-
N1',N3'-bis(2-(6-bromonaphthalen naphthalen-2-yloxy)acetyl)isophthalohydrazide
-
-
N1',N3'-bis(2-(naphthalen-2-yloxy)acetyl) isophthalohydrazide
-
-
N1',N4'-bis(2-(1-bromonaphthalen naphthalen-2-yloxy)acetyl)succinohydrazide
-
-
N1',N4'-bis(2-(3-bromonaphthalen naphthalen-2-yloxy)acetyl)succinohydrazide
-
-
N1',N4'-bis(2-(6-bromonaphthalen naphthalen-2-yloxy)acetyl)succinohydrazide
-
-
N1',N6'-bis(2-(1-bromonaphthalen naphthalen-2-yloxy)acetyl)adipohydrazide
-
-
N1',N6'-bis(2-(3-bromonaphthalen naphthalen-2-yloxy)acetyl)adipohydrazide
-
-
N1',N6'-bis(2-(6-bromonaphthalen naphthalen-2-yloxy)acetyl)adipohydrazide
-
-
N1-(6,7-dimethoxyquinazolin-4-yl)benzene-1,4-diamine
-
14% inhibition at 2 mM
tert-butyl (2S,4S)-2-([4-[(6,7-dimethoxyquinazolin-4-yl)amino]phenyl]carbamoyl)-4-hydroxypyrrolidine-1-carboxylate
-
-
[4-[(6,7-dimethoxyquinazolin-4-yl)amino]phenyl](3-hydroxyphenyl)methanone
-
7% inhibition at 0.05 mM
1-[(2S,3S,4R,5S)-3,4-dihydroxy-5-(hydroxymethyl)tetrahydrofuran-2-yl]dihydropyrimidine-2,4(1H,3H)-dione
-
-
1-[(2S,3S,4R,5S)-3,4-dihydroxy-5-(hydroxymethyl)tetrahydrofuran-2-yl]dihydropyrimidine-2,4(1H,3H)-dione
-
-
Mercuric chloride
-
complete inactivation with 0.5 mM at 30°C, 45 min, reversible by addition of 1 mM dithiothreitol
uridine
-
competitive with diphosphate, noncompetitive with UDP-N-acetyl-D-glucosamine, activity could be restored by dialysis
additional information
-
no inhibition with terreic acid, isolated from Aspergillus terreus, the compound inhibits the acetyltransferase activity of Escherichia coli GlmU but not the uridinyltransferase activity
-
additional information
N-acetylglucosamine derivative inhibitors design and synthesis, inhibitor docking studies and simulation, RMS and binding energies, overview
-
additional information
-
N-acetylglucosamine derivative inhibitors design and synthesis, inhibitor docking studies and simulation, RMS and binding energies, overview
-
additional information
-
displacement of MgB 2+ from its usual catalytically competent position, as noted in the crystal structure of RNA polymerase in an inactive state, is considered to be a key factor inhibiting the reaction. The entire metal-substrate complex renders the enzyme catalytically inactive
-
additional information
-
no inhibition by 6624116, 5655606, 5810599, and 6012954
-
additional information
-
design of bisubstrate and transition-state based inhibitors of GlmU uridyltransferase, the potential inhibitors against GlmU are initially prepared leading to the discovery of active minoquinazoline-based compounds with inhibitory potential against the uridyltransferase activity, compound synthesis, overview. No inhibition by 10, 11, 15, 16, 17, 32, and 34
-
additional information
-
TbUAP inhibitor by high-throughput screening, and structure-activity relationships, overview. No inhibition by 3
-
additional information
-
for development of potent and selective inhibitors of the uridyltransferase activity of Xanthomonas oryzae pv. oryzae GlmU, three types of target compounds are optimized and synthesized based on the Xo-GlmU structure, docking stud, and biological activity evaluation, overview
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
D-glucosamine 6-phosphate
-
allosteric, 0.003 mM, 5fold increase of activity, reversible by dialysis
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.03
N-acetyl-alpha-D-glucosamine 1-phosphate
-
purified recombinant native enzyme, pH 7.5, 37°C
0.041
N-acetyl-alpha-D-glucosamine 1-phosphate
-
pH 7.5, 37°C, recombinant enzyme
0.061
N-acetyl-alpha-D-glucosamine 1-phosphate
-
pH 8.2, 37°C, recombinant His6-tagged enzyme
0.011
N-acetyl-D-glucosamine 1-phosphate
R116A mutant, 30°C, pH 8.3
0.012
N-acetyl-D-glucosamine 1-phosphate
P122A mutant, 30°C, pH 8.3
0.014
N-acetyl-D-glucosamine 1-phosphate
wild type enzyme, 30°C, pH 8.3
0.015
N-acetyl-D-glucosamine 1-phosphate
T115A mutant, 30°C, pH 8.3
0.018
N-acetyl-D-glucosamine 1-phosphate
K123A mutant, 30°C, pH 8.3
0.019
N-acetyl-D-glucosamine 1-phosphate
G114A mutant, 30°C, pH 8.3
0.029
N-acetyl-D-glucosamine 1-phosphate
L117A mutant, 30°C, pH 8.3
0.034
N-acetyl-D-glucosamine 1-phosphate
G111A mutant, 30°C, pH 8.3
0.124
N-acetyl-D-glucosamine 1-phosphate
G112A mutant, 30°C, pH 8.3
additional information
additional information
-
Km values are 3.54 microM/l, 13.9 microM/l, 4.22 microM/l, 13.3 microM/l for isoforms MP I, MP II, MP III, MP IV, respcetively
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
the UAP enzyme kinetics display a strictly ordered bi.bi mechanism
-
additional information
additional information
-
Michaelis-Menten kinetics
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.95
N-acetyl-alpha-D-glucosamine 1-phosphate
-
pH 8.2, 37°C, recombinant His6-tagged enzyme
0.015
N-acetyl-D-glucosamine 1-phosphate
R116A mutant, 30°C, pH 8.3
0.0177
N-acetyl-D-glucosamine 1-phosphate
G112A mutant, 30°C, pH 8.3
0.0848
N-acetyl-D-glucosamine 1-phosphate
K123A mutant, 30°C, pH 8.3
1.33
N-acetyl-D-glucosamine 1-phosphate
G111A mutant, 30°C, pH 8.3
2.27
N-acetyl-D-glucosamine 1-phosphate
L117A mutant, 30°C, pH 8.3
4.4
N-acetyl-D-glucosamine 1-phosphate
P122A mutant, 30°C, pH 8.3
5.31
N-acetyl-D-glucosamine 1-phosphate
G114A mutant, 30°C, pH 8.3
8.78
N-acetyl-D-glucosamine 1-phosphate
T115A mutant, 30°C, pH 8.3
15.4
N-acetyl-D-glucosamine 1-phosphate
wild type enzyme, 30°C, pH 8.3
330
N-acetyl-D-glucosamine 1-phosphate
-
purified full length enzyme, pH 7.4
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0081
N'1,N'6-bis[2-(naphthalen-2-yloxy)acetyl]hexanedihydrazide
substrate N-acetyl-alpha-D-glucosamine 1-phosphate, pH 7.5, 37°C; substrate UTP, pH 7.5, 37°C
0.00044
luteolin
substrate N-acetyl-alpha-D-glucosamine 1-phosphate, pH 7.5, 37°C
0.0089
N'-[(4-chloro-3,5-dimethylphenoxy)acetyl]-2,4-dihydroxybenzohydrazide
substrate UTP, pH 7.5, 37°C
0.0194
N'-[(4-chloro-3,5-dimethylphenoxy)acetyl]-2,4-dihydroxybenzohydrazide
substrate N-acetyl-alpha-D-glucosamine 1-phosphate, pH 7.5, 37°C
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.037
3-[2-(1,3-benzodioxol-5-yl)-2-oxoethyl]-4-bromo-3-hydroxy-5-methyl-1,3-dihydro-2H-indol-2-one
Trypanosoma brucei brucei;
Q386Q8
pH not specified in the publication, temperature not specified in the publication
0.037
3-[2H-(1,3-benzodioxol-5-yl)-2-oxoethyl]-4-bromo-3-hydroxy-5-methyl-1,3-dihydro-2H-indol-2-one
Trypanosoma brucei;
-
pH 7.5, temperature not specified in the publication
-
0.00996
4-(4-(benzyloxy)benzylidene-2)-(naphthalen-1-yl)oxazol-5(4H)-one
Mycobacterium tuberculosis;
-
pH 7.4, 37°C
-
0.018
4-chloro-N-(3-methoxypropyl)-N-[1-(2-phenylethyl)piperidin-3-yl]benzamide
Haemophilus influenzae;
P43889
-
0.1
4-chloro-N-[1-[2-(2-fluorophenyl)ethyl]piperidin-3-yl]-N-(3-methoxypropyl)benzamide
Haemophilus influenzae;
P43889
value above
0.1
4-chloro-N-[1-[2-(3-fluorophenyl)ethyl]piperidin-3-yl]-N-(3-methoxypropyl)benzamide
Haemophilus influenzae;
P43889
value above
0.089
4-chloro-N-[1-[2-(4-fluorophenyl)ethyl]piperidin-3-yl]-N-(3-methoxypropyl)benzamide
Haemophilus influenzae;
P43889
-
0.02
4-fluoro-N-(3-methoxypropyl)-N-[1-(2-phenylethyl)piperidin-3-yl]benzamide
Haemophilus influenzae;
P43889
-
0.023
N'-[(4-chloro-3,5-dimethylphenoxy)acetyl]-2,4-dihydroxybenzohydrazide
Xanthomonas oryzae pv. oryzae;
Q2P7P9
pH 7.5, 37°C
0.014
N'1,N'6-bis[2-(naphthalen-2-yloxy)acetyl]hexanedihydrazide
Xanthomonas oryzae pv. oryzae;
Q2P7P9
pH 7.5, 37°C
0.049
N-(3,5-dimethoxyphenyl)-2,3-dihydro-4H-1,4-benzothiazine-4-carboxamide
Trypanosoma brucei;
-
pH 7.5, temperature not specified in the publication
0.074
N-(4-((6,7-dimethoxyquinazolin-4-yl)amino)phenyl)-3-hydroxybenzamide
Mycobacterium tuberculosis;
-
pH 7.6, 37°C
0.0108
N1',N3'-bis(2-(1-bromonaphthalen naphthalen-2-yloxy)acetyl)isophthalohydrazide
Xanthomonas oryzae pv. oryzae;
-
pH 7.5, 37°C
0.0184
N1',N3'-bis(2-(3-bromonaphthalen naphthalen-2-yloxy)acetyl)isophthalohydrazide
Xanthomonas oryzae pv. oryzae;
-
pH 7.5, 37°C
0.0134
N1',N3'-bis(2-(6-bromonaphthalen naphthalen-2-yloxy)acetyl)isophthalohydrazide
Xanthomonas oryzae pv. oryzae;
-
pH 7.5, 37°C
0.0138
N1',N3'-bis(2-(naphthalen-2-yloxy)acetyl) isophthalohydrazide
Xanthomonas oryzae pv. oryzae;
-
pH 7.5, 37°C
0.0154
N1',N4'-bis(2-(1-bromonaphthalen naphthalen-2-yloxy)acetyl)succinohydrazide
Xanthomonas oryzae pv. oryzae;
-
pH 7.5, 37°C
0.0194
N1',N4'-bis(2-(3-bromonaphthalen naphthalen-2-yloxy)acetyl)succinohydrazide
Xanthomonas oryzae pv. oryzae;
-
pH 7.5, 37°C
0.0112
N1',N4'-bis(2-(6-bromonaphthalen naphthalen-2-yloxy)acetyl)succinohydrazide
Xanthomonas oryzae pv. oryzae;
-
pH 7.5, 37°C
0.0171
N1',N4'-bis(2-(naphthalen-2-yloxy)acetyl) succinohydrazide
Xanthomonas oryzae pv. oryzae;
-
pH 7.5, 37°C
0.0233
N1',N6'-bis(2-(1-bromonaphthalen naphthalen-2-yloxy)acetyl)adipohydrazide
Xanthomonas oryzae pv. oryzae;
-
pH 7.5, 37°C
0.022
N1',N6'-bis(2-(3-bromonaphthalen naphthalen-2-yloxy)acetyl)adipohydrazide
Xanthomonas oryzae pv. oryzae;
-
pH 7.5, 37°C
0.0125
N1',N6'-bis(2-(6-bromonaphthalen naphthalen-2-yloxy)acetyl)adipohydrazide
Xanthomonas oryzae pv. oryzae;
-
pH 7.5, 37°C
0.0332
N1',N6'-bis(2-(naphthalen-2-yloxy)acetyl)adipohydrazide
Xanthomonas oryzae pv. oryzae;
-
pH 7.5, 37°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2
-
N-acetyl-alpha-D-glucosamine 1-phosphate substrate, pH 7.5, 80°C, recombinant mutant D005 protein
2.2
-
N-acetyl-alpha-D-glucosamine 1-phosphate substrate, pH 7.5, 80°C, recombinant wild-type ST0452 protein
2.6
-
N-acetyl-alpha-D-glucosamine 1-phosphate substrate, pH 7.5, 80°C, recombinant mutant D011 protein
6.42
-
pH 7.5, 80°C, substrates: UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
15.1
16.34
-
pH 7.5, 80°C, substrates: diphosphate + UDP-N-acetyl-alpha-D-glucosamine
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
7.5
7.6
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
expression early in embryogenesis, expression occurs ubiquitously and uniformly in the cellular blastoderm and accumulates in the developing mesoderm, gut primordia, and trachea; temporal profile of mmy transcription in early embryogenesis, overview
additional information
additional information
KT282116;
developmental expression pattern of enzyme LdUAP1, tissue and temporal expression profiles of LdUAP1 and LdUAP2, overview; developmental expression pattern of enzyme LdUAP2, tissue and temporal expression profiles of LdUAP1 and LdUAP2, overview
additional information
KT282117;
developmental expression pattern of enzyme LdUAP1, tissue and temporal expression profiles of LdUAP1 and LdUAP2, overview; developmental expression pattern of enzyme LdUAP2, tissue and temporal expression profiles of LdUAP1 and LdUAP2, overview
additional information
-
developmental expression pattern of LmUAP1, overview. The expression of LmUAP1 is significantly higher during the early embryogenesis (days 2-4) than the rest of the embryogenetic stages, highest expression is found just after fourth-instar nymph molting, but the expression gradually declined; developmental expression pattern of LmUAP2, overview. The expression of LmUAP2 is relatively consistent during the embryogenesis except for the 5-day-old eggs, in which the expression is 1.5 to 3fold higher than those in other days. The expression level of LmUAP2 is relatively consistent during the stages of after fourth-instar nymph molting and fifth-instar nymphs molted to adults; widely expressed in all the major tissues besides chitin-containing tissues and consistently expressed throughout early embryogenesis, egg hatch and nymphal development; widely expressed in all the major tissues besides chitin-containing tissues. High expression of UAP1 is detected during early embryogenesis, then decreases greatly, and slowly increases before egg hatch. During nymphal development, the highest expression of LmUAP1 appears just after molting but declines in each intermolting period and then increases before molting to the next stage
additional information
T1RR64;
developmental expression pattern of LmUAP1, overview. The expression of LmUAP1 is significantly higher during the early embryogenesis (days 2-4) than the rest of the embryogenetic stages, highest expression is found just after fourth-instar nymph molting, but the expression gradually declined; developmental expression pattern of LmUAP2, overview. The expression of LmUAP2 is relatively consistent during the embryogenesis except for the 5-day-old eggs, in which the expression is 1.5 to 3fold higher than those in other days. The expression level of LmUAP2 is relatively consistent during the stages of after fourth-instar nymph molting and fifth-instar nymphs molted to adults; widely expressed in all the major tissues besides chitin-containing tissues and consistently expressed throughout early embryogenesis, egg hatch and nymphal development; widely expressed in all the major tissues besides chitin-containing tissues. High expression of UAP1 is detected during early embryogenesis, then decreases greatly, and slowly increases before egg hatch. During nymphal development, the highest expression of LmUAP1 appears just after molting but declines in each intermolting period and then increases before molting to the next stage
additional information
T1RRG3;
developmental expression pattern of LmUAP1, overview. The expression of LmUAP1 is significantly higher during the early embryogenesis (days 2-4) than the rest of the embryogenetic stages, highest expression is found just after fourth-instar nymph molting, but the expression gradually declined; developmental expression pattern of LmUAP2, overview. The expression of LmUAP2 is relatively consistent during the embryogenesis except for the 5-day-old eggs, in which the expression is 1.5 to 3fold higher than those in other days. The expression level of LmUAP2 is relatively consistent during the stages of after fourth-instar nymph molting and fifth-instar nymphs molted to adults; widely expressed in all the major tissues besides chitin-containing tissues and consistently expressed throughout early embryogenesis, egg hatch and nymphal development; widely expressed in all the major tissues besides chitin-containing tissues. High expression of UAP1 is detected during early embryogenesis, then decreases greatly, and slowly increases before egg hatch. During nymphal development, the highest expression of LmUAP1 appears just after molting but declines in each intermolting period and then increases before molting to the next stage
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
additional information
-
the enzyme sequence cotains no signal peptide and transmembrane regions; the enzyme sequence cotains no signal peptide and transmembrane regions
-
additional information
T1RR64;
the enzyme sequence cotains no signal peptide and transmembrane regions; the enzyme sequence cotains no signal peptide and transmembrane regions
-
additional information
T1RRG3;
the enzyme sequence cotains no signal peptide and transmembrane regions; the enzyme sequence cotains no signal peptide and transmembrane regions
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Candida albicans;
Escherichia coli (strain K12);
Homo sapiens;
Q4WAR0
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100);
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4);
Q386Q8
Trypanosoma brucei brucei (strain 927/4 GUTat10.1);
Q97R46
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4);
Q97R46
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4);
Q97R46
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4);
Q97R46
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4);
Q97R46
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4);
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37000
49000
-
SDS-PAGE, corresponds very well with molecular weight expected from DNA sequence
49624
50000
57000
64000
49624
-
x * 49624, calculated from the deduced amino acid sequence of the His-tagged protein
49624
-
1 * 50000, SDS-PAGE, 1 * 49624, calculated from the deduced amino acid sequence, native mass by gel filtration
50000
-
1 * 50000, SDS-PAGE, 1 * 49624, calculated from the deduced amino acid sequence, native mass by gel filtration
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
hexamer
-
trimer/hexamer equilibrium, sedimentation equilibrium analytical ultracentrifugation. Two trimers assemble through their N-terminal domains. The interaction is mediated by a loop that undergoes a large conformational change in the uridyl transferase reaction
monomer
trimer
additional information
?
-
x * 49624, calculated from the deduced amino acid sequence of the His-tagged protein
?
T1RR64;, T1RRG3;
x * 55100, approximately, sequence calculation; x * 55800, approximately, sequence calculation