Topic
Creatinase
About: Creatinase is a research topic. Over the lifetime, 105 publications have been published within this topic receiving 2167 citations. The topic is also known as: creatine amidinohydrolase.
Papers published on a yearly basis
Papers
TL;DR: The structure of the proline-specific aminopeptidase from Escherichia coli has been solved and refined for crystals of the native enzyme at a 2.0-A resolution, consistent with observations from analytical ultracentrifuge studies that show that the protein is a tetramer under physiological conditions.
Abstract: The structure of the proline-specific aminopeptidase (EC 3.4.11.9) from Escherichia coli has been solved and refined for crystals of the native enzyme at a 2.0-A resolution, for a dipeptide-inhibited complex at 2.3-A resolution, and for a low-pH inactive form at 2.7-A resolution. The protein crystallizes as a tetramer, more correctly a dimer of dimers, at both high and low pH, consistent with observations from analytical ultracentrifuge studies that show that the protein is a tetramer under physiological conditions. The monomer folds into two domains. The active site, in the larger C-terminal domain, contains a dinuclear manganese center in which a bridging water molecule or hydroxide ion appears poised to act as the nucleophile in the attack on the scissile peptide bond of Xaa-Pro. The metal-binding residues are located in a single subunit, but the residues surrounding the active site are contributed by three subunits. The fold of the protein resembles that of creatine amidinohydrolase (creatinase, not a metalloenzyme). The C-terminal catalytic domain is also similar to the single-domain enzyme methionine aminopeptidase that has a dinuclear cobalt center.
177 citations
TL;DR: Amino acid sequence comparison suggests that the structure of Escherichia coli methionine aminopeptidase and the C-terminal domain of Pseudomonas putida creatinase are related, and this homology is confirmed by a detailed comparison of the three-dimensional folds of the two enzymes.
Abstract: Amino acid sequence comparison suggests that the structure of Escherichia coli methionine aminopeptidase (EC 3.4.11.18) and the C-terminal domain of Pseudomonas putida creatinase (EC 3.5.3.3) are related. A detailed comparison of the three-dimensional folds of the two enzymes confirms this homology: with an approximately 260-residue chain segment, 218 C alpha atoms of the structures superimpose within 2.5 A; only 41 of these overlapping positions (i.e., 19%) feature identical amino acids in the two protein chains. Notwithstanding this striking correspondence in structure, methionine aminopeptidase binds and is stimulated by Co2+, while creatinase is not a metal-dependent enzyme. Searches of protein data banks using sequence and structure-based profiles reveal other enzymes, including aminopeptidase P (EC 3.4.11.9), prolidase (EC 3.4.13.9), and agropine synthase, that likely share the same "pita-bread" fold common to creatinase and methionine aminopeptidase.
156 citations
TL;DR: Miniaturized, disposable amperometric biosensors for determination of creatinine in human serum are described, using a thin electropolymerized film of poly(1,3-diaminobenzene) to reduce electrochemical interferences from ascorbate, urate, acetaminophen, and other oxidizable species.
Abstract: Miniaturized, disposable amperometric biosensors for determination of creatinine in human serum are described. The base electrodes are fabricated using microelectronics techniques, to build a multilayer film structure on a polyimide foil. By using a thin electropolymerized film of poly(1,3-diaminobenzene), the electrochemical interferences from ascorbate, urate, acetaminophen, and other oxidizable species are greatly diminished. The multienzyme system (creatininase, creatinase, sarcosine oxidase) is immobilized on top of the permselective layer using cross-linking of the proteins with glutaraldehyde. The electropolymerization conditions for obtaining almost ideal permselectivity of the inner layer are defined, as well as the optimal enzyme layer preparation. A composite polymeric outer membrane [Nafion + poly-(2-hydroxyethyl methacrylate)] is used for diffusion control and to protect the enzyme layer from fouling. The reagentless planar sensors for creatinine and creatine have fast response time (t95 = 1 ...
140 citations
TL;DR: In this paper, microfabricated sensors for determination of creatine and creatinine in serum were described, based on a bienzyme sequence, involving creatine amidinohydrolase (CI) and sarcosine oxidase (SO).
110 citations
TL;DR: The fabrication and operation of a multi-analyte miniature conductance biosensor that responds to changes in the electrode double layer capacitance as the ionic strength is increased by the enzyme-catalysed generation of charged reaction products is described.
109 citations
Related Topics (5)
Performance Metrics
| Year | Papers |
|---|---|
| 2020 | 3 |
| 2019 | 4 |
| 2018 | 2 |
| 2017 | 7 |
| 2016 | 2 |
| 2015 | 2 |