Tropine acyltransferase (EC 2.3.1.185, tropine:acyl-CoA transferase, acetyl-CoA:tropan-3ol acyltransferase, tropine acetyltransferase, tropine tigloyltransferase, TAT) is an enzyme
with system name acyl-CoA:tropine O-acyltransferase.[1][2][3][4] This enzyme catalyses the
following chemical reaction
acyl-CoA + tropine
CoA + O-acyltropine
This enzyme exhibits absolute specificity for the endo/3alpha configuration found in tropine
as pseudotropine.
Glucokinase
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Glucokinase (hexokinase 4)
Based on PDB entry 1GLK.
Available structures
Ortholog search: PDBe, RCSB
PDB
[show]List of PDB id codes
Identifiers
Symbols
External
IDs
EC
number
GCK; FGQTL3; GK; GLK; HHF3; HK4; HKIV;
HXKP; LGLK; MODY2
OMIM: 138079 MGI: 1270854
HomoloGene: 55440 ChEMBL: 3820
GeneCards: GCK Gene
2.7.1.2
[show]Gene Ontology
RNA expression pattern
More reference expression data
Orthologs
Species Human
Mouse
Entrez 2645
103988
Ensembl ENSG00000106633 ENSMUSG00000041798
UniProt P35557
RefSeq
(mRNA)
RefSeq
(protein)
P52792
NM_000162
NM_010292
NP_000153
NP_034422
Location Chr 7:
Chr 11:
(UCSC) 44.18 – 44.24 Mb
5.9 – 5.95 Mb
PubMed
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Glucokinase
EC number
CAS number
IntEnz
BRENDA
ExPASy
KEGG
MetaCyc
Identifiers
2.7.1.2
9001-36-9
Databases
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BRENDA entry
NiceZyme view
KEGG entry
metabolic pathway
PRIAM
PDB structures
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RCSB PDB PDBe PDBsum
AmiGO / EGO
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Glucokinase (EC 2.7.1.2) is an enzyme that facilitates phosphorylation of glucose to
glucose-6-phosphate. Glucokinase occurs in cells in the liver, pancreas, gut, and brain of
humans and most other vertebrates. In each of these organs it plays an important role in the
regulation of carbohydrate metabolism by acting as a glucose sensor, triggering shifts in
metabolism or cell function in response to rising or falling levels of glucose, such as occur
after a meal or when fasting. Mutations of the gene for this enzyme can cause unusual forms
of diabetes or hypoglycemia.
Glucokinase (GK) is a hexokinase isozyme, related homologously to at least three other
hexokinases.[1] All of the hexokinases can mediate phosphorylation of glucose to glucose-6phosphate (G6P), which is the first step of both glycogen synthesis and glycolysis. However,
glucokinase is coded by a separate gene and its distinctive kinetic properties allow it to serve
a different set of functions. Glucokinase has a lower affinity for glucose than the other
hexokinases do, and its activity is localized to a few cell types, leaving the other three
hexokinases as more important preparers of glucose for glycolysis and glycogen synthesis for
most tissues and organs. Because of this reduced affinity, the activity of glucokinase, under
usual physiological conditions, varies substantially according to the concentration of
glucose.[2]
Triglyceride lipases (EC 3.1.1.3) are a family of lipolytic enzymes that hydrolyse ester
linkages of triglycerides.[1] Lipases are widely distributed in animals, plants and prokaryotes.
At least three tissue-specific isozymes exist in higher vertebrates, pancreatic, hepatic and
gastric/lingual. These lipases are closely related to each other and to lipoprotein lipase (EC
3.1.1.34), which hydrolyses triglycerides of chylomicrons and very low density lipoproteins
(VLDL).[2]
Dual specificity mitogen-activated protein kinase kinase 4 is an enzyme that in humans is
encoded by the MAP2K4 gene.[1]
This gene encodes a dual specificity protein kinase that belongs to the Ser/Thr protein kinase
family. This kinase is a direct activator of MAP kinases in response to various environmental
stresses or mitogenic stimuli. It has been shown to activate MAPK8/JNK1, MAPK9/JNK2,
and MAPK14/p38, but not MAPK1/ERK2 or MAPK3/ERK1. This kinase is phosphorylated,
and thus activated by MAP3K1/MEKK. The knockout studies in mice suggested the roles of
this kinase in mediating survival signal in T cell development, as well as in the organogenesis
of liver.[2]
Low-specificity L-threonine aldolase
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Low-specificity L-threonine aldolase
EC number
IntEnz
BRENDA
ExPASy
KEGG
MetaCyc
PRIAM
PDB structures
Identifiers
4.1.2.48
Databases
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BRENDA entry
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Low-specificity L-threonine aldolase (EC 4.1.2.48, LtaE) is an enzyme with system name
L-threonine/L-allo-threonine acetaldehyde-lyase (glycine-forming).[1][2][3][4][5] This enzyme
catalyses the following chemical reaction
(1) L-threonine
glycine + acetaldehyde
(2) L-allo-threonine
glycine + acetaldehyde
This enzyme requires pyridoxal phosphate.