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Search results 201 to 235 out of 235 for Fggy

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0.024s
Type Details Score
Publication
First Author: Xavier KB
Year: 2007
Journal: ACS Chem Biol
Title: Phosphorylation and processing of the quorum-sensing molecule autoinducer-2 in enteric bacteria.
Volume: 2
Issue: 2
Pages: 128-36
Strain
Attribute String: coisogenic, mutant strain, targeted mutation
Strain
Attribute String: coisogenic, endonuclease-mediated mutation, mutant strain
Strain
Attribute String: mutant strain, coisogenic, targeted mutation
Protein Domain
Type: Family
Description: This entry is composed of a group of putative bacterial L-ribulokinases (RBK; ) and similar proteins. L-RBK catalyzes the MgATP-dependent phosphorylation of a variety of sugar substrates. Members of this subfamily belong to the FGGY family of carbohydrate kinases.
Publication
First Author: Kardon T
Year: 2008
Journal: FEBS Lett
Title: Characterization of mammalian sedoheptulokinase and mechanism of formation of erythritol in sedoheptulokinase deficiency.
Volume: 582
Issue: 23-24
Pages: 3330-4
Publication
First Author: Haschemi A
Year: 2012
Journal: Cell Metab
Title: The sedoheptulose kinase CARKL directs macrophage polarization through control of glucose metabolism.
Volume: 15
Issue: 6
Pages: 813-26
Publication  
First Author: HEATH EC
Year: 1962
Journal: J Biol Chem
Title: The metabolism of L-fucose. I. The purification and properties of L-fuculose kinase.
Volume: 237
Pages: 2423-6
Protein Domain
Type: Family
Description: Proteins in this entry are L-fuculokinases including the Escherichia coli enzyme []. They catalyse the second step in fucose catabolism and belong to the FGGY family of carbohydrate kinases. These enzymes are encoded by the kinase (K) gene of the fucose (fuc) operon.
Protein Domain
Type: Family
Description: Sedoheptulokinase (SHK, also known as D-altro-heptulose or heptulokinase, ) catalyzes the ATP-dependent phosphorylation of sedoheptulose to produce sedoheptulose 7-phosphate and ADP []. In mammals, it acts as a modulator of macrophage activation through control of glucose metabolism []. It belongs to the FGGY kinase family.
Publication
First Author: Kraft L
Year: 2001
Journal: Acta Crystallogr D Biol Crystallogr
Title: Crystallization and preliminary X-ray crystallographic studies of recombinant thermoresistant gluconate kinase GntK from Escherichia coli.
Volume: 57
Issue: Pt 8
Pages: 1159-61
Publication
First Author: Izu H
Year: 1996
Journal: FEBS Lett
Title: Purification and characterization of the Escherichia coli thermoresistant glucokinase encoded by the gntK gene.
Volume: 394
Issue: 1
Pages: 14-6
Protein Domain
Type: Conserved_site
Description: FGGY carbohydrate kinases carry out ATP-dependent phosphorylation on one out of at least nine distinct sugar substrates []. These enzymes include L-ribulokinase () (gene araB); Erythriol kinase () (gene eryA); L-fucolokinase () (gene fucK); gluconokinase () (gene gntK); glycerol kinase () (gene glpK); xylulokinase () (gene xylB); L-xylulose kinase () (gene lyxK), D-ribulokinase () (gene rbtK); and rhamnulokinase () (gene rhaB). This family also contains a divergent subfamily functioning in quorum sensing, which phosphorylates AI-2, a bacterial signaling molecule derived from 4,5-dihydroxy-2,3-pentanedione (DPD) [].This entry represents conserved regions found in the central and C-terminal regions of these enzymes.
Protein Domain
Type: Family
Description: This family of proteins includes thermoresistant and thermosensitve isozymes of gluconate kinase (gluconokinase) in E. coli and other related proteins; members of this family are often named by similarity to the thermostable isozyme. These proteins show homology to shikimate kinases and adenylate kinases but not to gluconate kinases from the FGGY family of carbohydrate kinases. The structure of the E. coli thermoresistant gluconate kinase GntK has been revealed []. GntK catalyzes the phosphoryl transfer from ATP to gluconate. The resulting product gluconate-6-phoshate is an important precursor of gluconate metabolism. GntK acts as a dimmer composed of two identical subunits [, ].
Protein Domain
Type: Domain
Description: FGGY carbohydrate kinases carry out ATP-dependent phosphorylation on one out of at least nine distinct sugar substrates []. These enzymes include L-ribulokinase () (gene araB); Erythriol kinase () (gene eryA); L-fucolokinase () (gene fucK); gluconokinase () (gene gntK); glycerol kinase () (gene glpK); xylulokinase () (gene xylB); L-xylulose kinase () (gene lyxK), D-ribulokinase () (gene rbtK); and rhamnulokinase () (gene rhaB). This family also contains a divergent subfamily functioning in quorum sensing, which phosphorylates AI-2, a bacterial signaling molecule derived from 4,5-dihydroxy-2,3-pentanedione (DPD) [].This entry represents the N-terminal domain of these proteins. It adopts a ribonuclease H-like fold and is structurally related to the C-terminal domain [, ].All described members of this enzyme family are composed of two homologous actin-like ATPase domains. A catalytic cleft is formed by the interface between these two domains, where the sugar substrate and ATP co-substrate bind.
Protein Domain
Type: Domain
Description: FGGY carbohydrate kinases carry out ATP-dependent phosphorylation on one out of at least nine distinct sugar substrates []. These enzymes include L-ribulokinase () (gene araB); Erythriol kinase () (gene eryA); L-fucolokinase () (gene fucK); gluconokinase () (gene gntK); glycerol kinase () (gene glpK); xylulokinase () (gene xylB); L-xylulose kinase () (gene lyxK), D-ribulokinase () (gene rbtK); and rhamnulokinase () (gene rhaB). This family also contains a divergent subfamily functioning in quorum sensing, which phosphorylates AI-2, a bacterial signaling molecule derived from 4,5-dihydroxy-2,3-pentanedione (DPD) [].All described members of this enzyme family are composed of two homologous actin-like ATPase domains. A catalytic cleft is formed by the interface between these two domains, where the sugar substrate and ATP co-substrate bind.This entry represents the C-terminal domain of these proteins. It adopts a ribonuclease H-like fold and is structurally related to the N-terminal domain [, ].
Protein
Organism: Mus musculus/domesticus
Length: 476  
Fragment?: false
Publication
First Author: Hurley JH
Year: 1993
Journal: Science
Title: Structure of the regulatory complex of Escherichia coli IIIGlc with glycerol kinase.
Volume: 259
Issue: 5095
Pages: 673-7
Publication
First Author: Ormö M
Year: 1998
Journal: Biochemistry
Title: Crystal structure of a complex of Escherichia coli glycerol kinase and an allosteric effector fructose 1,6-bisphosphate.
Volume: 37
Issue: 47
Pages: 16565-72
Protein
Organism: Mus musculus/domesticus
Length: 168  
Fragment?: true
Publication  
First Author: Chen Y
Year: 2017
Journal: Cell Discov
Title: Glycerol kinase-like proteins cooperate with Pld6 in regulating sperm mitochondrial sheath formation and male fertility.
Volume: 3
Pages: 17030
Publication      
First Author: Shimada K
Year: 2019
Journal: J Reprod Dev
Title: Glycerol kinase 2 is essential for proper arrangement of crescent-like mitochondria to form the mitochondrial sheath during mouse spermatogenesis.
Protein
Organism: Mus musculus/domesticus
Length: 318  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 196  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 138  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 218  
Fragment?: false
Publication
First Author: Worley KC
Year: 1995
Journal: J Comput Biol
Title: Identification of new members of a carbohydrate kinase-encoding gene family.
Volume: 2
Issue: 3
Pages: 451-8
Protein Domain
Type: Family
Description: This entry corresponds to a group of metazoan glycerol kinases (GKs), coded by X chromosome-linked GK genes, and glycerol kinase (GK)-like proteins, coded by autosomal testis-specific GK-like genes GK2, GK3 and Gykl1 (in mouse). These are thought to have arise by the transposition of Gk located on the Xchromosome []. Sequence comparison shows that metazoan GKs and GK-like proteins in this family are closely related to the bacterial GKs, which catalyze the Mg-ATP dependent phosphorylation of glycerol to yield glycerol 3-phosphate (G3P). The metazoan GKs do have GK enzymatic activity. However, the GK-like metazoan proteins do not exhibit GK activity and their biological functions are not yet clear []. Some of them lack important functional residues involved in the binding of ADP and Mg2+, which may result in the loss of GK catalytic function. Others that have conserved catalytic residues have lost their GK activity as well; the reason remains unclear. It has been suggested the conserved catalytic residues might facilitate them performing a distinct function. GK2 seem to be necessary for the formation of the mitochondrial sheath during spermatogenesis [, ].GKs belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site [].
Publication
First Author: Kraft L
Year: 2002
Journal: J Mol Biol
Title: Conformational changes during the catalytic cycle of gluconate kinase as revealed by X-ray crystallography.
Volume: 318
Issue: 4
Pages: 1057-69
Protein
Organism: Mus musculus/domesticus
Length: 184  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 75  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 84  
Fragment?: false
Publication
First Author: Gerhard DS
Year: 2004
Journal: Genome Res
Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Volume: 14
Issue: 10B
Pages: 2121-7
Publication
First Author: Huttlin EL
Year: 2010
Journal: Cell
Title: A tissue-specific atlas of mouse protein phosphorylation and expression.
Volume: 143
Issue: 7
Pages: 1174-89
Publication
First Author: Church DM
Year: 2009
Journal: PLoS Biol
Title: Lineage-specific biology revealed by a finished genome assembly of the mouse.
Volume: 7
Issue: 5
Pages: e1000112