ATP:guanido phosphotransferase catalytic domain | |||||||||
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Identifiers | |||||||||
Symbol | ATP-gua_Ptrans | ||||||||
Pfam | PF00217 | ||||||||
Pfam clan | CL0286 | ||||||||
InterPro | IPR022414 | ||||||||
PROSITE | PDOC00103 | ||||||||
SCOP2 | 1crk / SCOPe / SUPFAM | ||||||||
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ATP:guanido phosphotransferase N-terminal domain | |||||||||
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Identifiers | |||||||||
Symbol | ATP-gua_PtransN | ||||||||
Pfam | PF02807 | ||||||||
InterPro | IPR022413 | ||||||||
PROSITE | PDOC00103 | ||||||||
SCOP2 | 1crk / SCOPe / SUPFAM | ||||||||
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In molecular biology, the ATP:guanido phosphotransferase family is a family of structurally and functionally related enzymes, [1] [2] that reversibly catalyse the transfer of phosphate between ATP and various phosphagens. The enzymes belonging to this family include:
Creatine kinase plays an important role in energy metabolism of vertebrates. There are at least four different, but very closely related, forms of CK. Two isozymes, M (muscle) and B (brain), are cytosolic, while the other two are mitochondrial. In sea urchins there is a flagellar isozyme, which consists of the triplication of a CK-domain. A cysteine residue is implicated in the catalytic activity of these enzymes and the region around this active site residue is highly conserved.
ATP:guanido phosphotransferases contain a C-terminal catalytic domain which consists of a duplication where the common core consists of two beta-alpha-beta2-alpha repeats. [5] The substrate binding site is located in the cleft between N and C-terminal domains, but most of the catalytic residues are found in the larger C-terminal domain. [5] They also contain an N-terminal domain which has an all-alpha fold consisting of an irregular array of 6 short helices. [5]
Creatine kinase (CK), also known as creatine phosphokinase (CPK) or phosphocreatine kinase, is an enzyme expressed by various tissues and cell types. CK catalyses the conversion of creatine and uses adenosine triphosphate (ATP) to create phosphocreatine (PCr) and adenosine diphosphate (ADP). This CK enzyme reaction is reversible and thus ATP can be generated from PCr and ADP.
Adenylate kinase is a phosphotransferase enzyme that catalyzes the interconversion of the various adenosine phosphates. By constantly monitoring phosphate nucleotide levels inside the cell, ADK plays an important role in cellular energy homeostasis.
Phosphoglycerate kinase is an enzyme that catalyzes the reversible transfer of a phosphate group from 1,3-bisphosphoglycerate (1,3-BPG) to ADP producing 3-phosphoglycerate (3-PG) and ATP :
Carbamoyl phosphate synthetase catalyzes the ATP-dependent synthesis of carbamoyl phosphate from glutamine or ammonia and bicarbonate. This enzyme catalyzes the reaction of ATP and bicarbonate to produce carboxy phosphate and ADP. Carboxy phosphate reacts with ammonia to give carbamic acid. In turn, carbamic acid reacts with a second ATP to give carbamoyl phosphate plus ADP.
In enzymology, a [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] is an enzyme that catalyzes the chemical reaction
In enzymology, a glucosamine kinase is an enzyme that catalyzes the chemical reaction
In enzymology, a guanidinoacetate kinase is an enzyme that catalyzes the chemical reaction
In enzymology, a lombricine kinase is an enzyme that catalyzes the chemical reaction
In enzymology, a low-density-lipoprotein receptor kinase is an enzyme that catalyzes the chemical reaction
In enzymology, a mannokinase is an enzyme that catalyzes the chemical reaction
In enzymology, a myosin-heavy-chain kinase is an enzyme that catalyzes the chemical reaction
In enzymology, a nucleoside-phosphate kinase is an enzyme that catalyzes the chemical reaction
Pyruvate, phosphate dikinase, or PPDK is an enzyme in the family of transferases that catalyzes the chemical reaction
In enzymology, a riboflavin kinase is an enzyme that catalyzes the chemical reaction
In enzymology, a [RNA-polymerase]-subunit kinase is an enzyme that catalyzes the chemical reaction
In enzymology, a taurocyamine kinase is an enzyme that catalyzes the chemical reaction
Brain-type creatine kinase also known as CK-BB is a creatine kinase that in humans is encoded by the CKB gene.
In molecular biology, the ELFV dehydrogenase family of enzymes include glutamate, leucine, phenylalanine and valine dehydrogenases. These enzymes are structurally and functionally related. They contain a Gly-rich region containing a conserved Lys residue, which has been implicated in the catalytic activity, in each case a reversible oxidative deamination reaction.
The prokaryotic riboflavin biosynthesis protein is a bifunctional enzyme found in bacteria that catalyzes the phosphorylation of riboflavin into flavin mononucleotide (FMN) and the adenylylation of FMN into flavin adenine dinucleotide (FAD). It consists of a C-terminal riboflavin kinase and an N-terminal FMN-adenylyltransferase. This bacterial protein is functionally similar to the monofunctional riboflavin kinases and FMN-adenylyltransferases of eukaryotic organisms, but only the riboflavin kinases are structurally homologous.
In molecular biology, the ATCase/OTCase family is a protein family which contains two related enzymes: aspartate carbamoyltransferase EC 2.1.3.2 and ornithine carbamoyltransferase EC 2.1.3.3. It has been shown that these enzymes are evolutionary related. The predicted secondary structure of both enzymes is similar and there are some regions of sequence similarities. One of these regions includes three residues which have been shown, by crystallographic studies to be implicated in binding the phosphoryl group of carbamoyl phosphate and may also play a role in trimerisation of the molecules. The N-terminal domain is the carbamoyl phosphate binding domain. The C-terminal domain is an aspartate/ornithine-binding domain.