Differential Gene Expression in Tomato Fruit and Colletotrichum
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Analysis of the Impact of Silver Ions on Creatine Amidinohydrolase
ActaBIOMATERIALIA Acta Biomaterialia 1 (2005) 183–191 www.actamat-journals.com A stable three enzyme creatinine biosensor. 2. Analysis of the impact of silver ions on creatine amidinohydrolase Jason A. Berberich b,1, Lee Wei Yang a, Ivet Bahar a, Alan J. Russell b,* a Center for Computational Biology & Bioinformatics and Department of Molecular Genetics & Biochemistry, School of Medicine, University of Pittsburgh, Pittsburgh, PA, USA b Department of Surgery, McGowan Institute for Regenerative Medicine, University of Pittsburgh, Pittsburgh, PA 15219, USA Received 11 October 2004; received in revised form 26 November 2004; accepted 28 November 2004 Abstract The enzyme creatine amidinohydrolase is a clinically important enzyme used in the determination of creatinine in blood and urine. Continuous use biosensors are becoming more important in the clinical setting; however, long-use creatinine biosensors have not been commercialized due to the complexity of the three-enzyme creatinine biosensor and the lack of stability of its components. This paper, the second in a series of three, describes the immobilization and stabilization of creatine amidinohydrolase. Creatine amidinohydrolase modified with poly(ethylene glycol) activated with isocyanate retains significant activity after modification. The enzyme was successfully immobilized into hydrophilic polyurethanes using a reactive prepolymer strategy. The immobilized enzyme retained significant activity over a 30 day period at 37 °C and was irreversibly immobilized into the polymer. Despite being stabilized in the polymer, the enzyme remained highly sensitive to silver ions which were released from the amperometric electrodes. Computational analysis of the structure of the protein using the Gaussian network model suggests that the silver ions bind tightly to a cysteine residue preventing normal enzyme dynamics and catalysis. -
Protein Identities in Evs Isolated from U87-MG GBM Cells As Determined by NG LC-MS/MS
Protein identities in EVs isolated from U87-MG GBM cells as determined by NG LC-MS/MS. No. Accession Description Σ Coverage Σ# Proteins Σ# Unique Peptides Σ# Peptides Σ# PSMs # AAs MW [kDa] calc. pI 1 A8MS94 Putative golgin subfamily A member 2-like protein 5 OS=Homo sapiens PE=5 SV=2 - [GG2L5_HUMAN] 100 1 1 7 88 110 12,03704523 5,681152344 2 P60660 Myosin light polypeptide 6 OS=Homo sapiens GN=MYL6 PE=1 SV=2 - [MYL6_HUMAN] 100 3 5 17 173 151 16,91913397 4,652832031 3 Q6ZYL4 General transcription factor IIH subunit 5 OS=Homo sapiens GN=GTF2H5 PE=1 SV=1 - [TF2H5_HUMAN] 98,59 1 1 4 13 71 8,048185945 4,652832031 4 P60709 Actin, cytoplasmic 1 OS=Homo sapiens GN=ACTB PE=1 SV=1 - [ACTB_HUMAN] 97,6 5 5 35 917 375 41,70973209 5,478027344 5 P13489 Ribonuclease inhibitor OS=Homo sapiens GN=RNH1 PE=1 SV=2 - [RINI_HUMAN] 96,75 1 12 37 173 461 49,94108966 4,817871094 6 P09382 Galectin-1 OS=Homo sapiens GN=LGALS1 PE=1 SV=2 - [LEG1_HUMAN] 96,3 1 7 14 283 135 14,70620005 5,503417969 7 P60174 Triosephosphate isomerase OS=Homo sapiens GN=TPI1 PE=1 SV=3 - [TPIS_HUMAN] 95,1 3 16 25 375 286 30,77169764 5,922363281 8 P04406 Glyceraldehyde-3-phosphate dehydrogenase OS=Homo sapiens GN=GAPDH PE=1 SV=3 - [G3P_HUMAN] 94,63 2 13 31 509 335 36,03039959 8,455566406 9 Q15185 Prostaglandin E synthase 3 OS=Homo sapiens GN=PTGES3 PE=1 SV=1 - [TEBP_HUMAN] 93,13 1 5 12 74 160 18,68541938 4,538574219 10 P09417 Dihydropteridine reductase OS=Homo sapiens GN=QDPR PE=1 SV=2 - [DHPR_HUMAN] 93,03 1 1 17 69 244 25,77302971 7,371582031 11 P01911 HLA class II histocompatibility antigen, -
Supplementary Materials
Supplementary Materials COMPARATIVE ANALYSIS OF THE TRANSCRIPTOME, PROTEOME AND miRNA PROFILE OF KUPFFER CELLS AND MONOCYTES Andrey Elchaninov1,3*, Anastasiya Lokhonina1,3, Maria Nikitina2, Polina Vishnyakova1,3, Andrey Makarov1, Irina Arutyunyan1, Anastasiya Poltavets1, Evgeniya Kananykhina2, Sergey Kovalchuk4, Evgeny Karpulevich5,6, Galina Bolshakova2, Gennady Sukhikh1, Timur Fatkhudinov2,3 1 Laboratory of Regenerative Medicine, National Medical Research Center for Obstetrics, Gynecology and Perinatology Named after Academician V.I. Kulakov of Ministry of Healthcare of Russian Federation, Moscow, Russia 2 Laboratory of Growth and Development, Scientific Research Institute of Human Morphology, Moscow, Russia 3 Histology Department, Medical Institute, Peoples' Friendship University of Russia, Moscow, Russia 4 Laboratory of Bioinformatic methods for Combinatorial Chemistry and Biology, Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry of the Russian Academy of Sciences, Moscow, Russia 5 Information Systems Department, Ivannikov Institute for System Programming of the Russian Academy of Sciences, Moscow, Russia 6 Genome Engineering Laboratory, Moscow Institute of Physics and Technology, Dolgoprudny, Moscow Region, Russia Figure S1. Flow cytometry analysis of unsorted blood sample. Representative forward, side scattering and histogram are shown. The proportions of negative cells were determined in relation to the isotype controls. The percentages of positive cells are indicated. The blue curve corresponds to the isotype control. Figure S2. Flow cytometry analysis of unsorted liver stromal cells. Representative forward, side scattering and histogram are shown. The proportions of negative cells were determined in relation to the isotype controls. The percentages of positive cells are indicated. The blue curve corresponds to the isotype control. Figure S3. MiRNAs expression analysis in monocytes and Kupffer cells. Full-length of heatmaps are presented. -
Supplementary Table S4. FGA Co-Expressed Gene List in LUAD
Supplementary Table S4. FGA co-expressed gene list in LUAD tumors Symbol R Locus Description FGG 0.919 4q28 fibrinogen gamma chain FGL1 0.635 8p22 fibrinogen-like 1 SLC7A2 0.536 8p22 solute carrier family 7 (cationic amino acid transporter, y+ system), member 2 DUSP4 0.521 8p12-p11 dual specificity phosphatase 4 HAL 0.51 12q22-q24.1histidine ammonia-lyase PDE4D 0.499 5q12 phosphodiesterase 4D, cAMP-specific FURIN 0.497 15q26.1 furin (paired basic amino acid cleaving enzyme) CPS1 0.49 2q35 carbamoyl-phosphate synthase 1, mitochondrial TESC 0.478 12q24.22 tescalcin INHA 0.465 2q35 inhibin, alpha S100P 0.461 4p16 S100 calcium binding protein P VPS37A 0.447 8p22 vacuolar protein sorting 37 homolog A (S. cerevisiae) SLC16A14 0.447 2q36.3 solute carrier family 16, member 14 PPARGC1A 0.443 4p15.1 peroxisome proliferator-activated receptor gamma, coactivator 1 alpha SIK1 0.435 21q22.3 salt-inducible kinase 1 IRS2 0.434 13q34 insulin receptor substrate 2 RND1 0.433 12q12 Rho family GTPase 1 HGD 0.433 3q13.33 homogentisate 1,2-dioxygenase PTP4A1 0.432 6q12 protein tyrosine phosphatase type IVA, member 1 C8orf4 0.428 8p11.2 chromosome 8 open reading frame 4 DDC 0.427 7p12.2 dopa decarboxylase (aromatic L-amino acid decarboxylase) TACC2 0.427 10q26 transforming, acidic coiled-coil containing protein 2 MUC13 0.422 3q21.2 mucin 13, cell surface associated C5 0.412 9q33-q34 complement component 5 NR4A2 0.412 2q22-q23 nuclear receptor subfamily 4, group A, member 2 EYS 0.411 6q12 eyes shut homolog (Drosophila) GPX2 0.406 14q24.1 glutathione peroxidase -
Phosphine Stabilizers for Oxidoreductase Enzymes
Europäisches Patentamt *EP001181356B1* (19) European Patent Office Office européen des brevets (11) EP 1 181 356 B1 (12) EUROPEAN PATENT SPECIFICATION (45) Date of publication and mention (51) Int Cl.7: C12N 9/02, C12P 7/00, of the grant of the patent: C12P 13/02, C12P 1/00 07.12.2005 Bulletin 2005/49 (86) International application number: (21) Application number: 00917839.3 PCT/US2000/006300 (22) Date of filing: 10.03.2000 (87) International publication number: WO 2000/053731 (14.09.2000 Gazette 2000/37) (54) Phosphine stabilizers for oxidoreductase enzymes Phosphine Stabilisatoren für oxidoreduktase Enzymen Phosphines stabilisateurs des enzymes ayant une activité comme oxidoreducase (84) Designated Contracting States: (56) References cited: DE FR GB NL US-A- 5 777 008 (30) Priority: 11.03.1999 US 123833 P • ABRIL O ET AL.: "Hybrid organometallic/enzymatic catalyst systems: (43) Date of publication of application: Regeneration of NADH using dihydrogen" 27.02.2002 Bulletin 2002/09 JOURNAL OF THE AMERICAN CHEMICAL SOCIETY., vol. 104, no. 6, 1982, pages 1552-1554, (60) Divisional application: XP002148357 DC US cited in the application 05021016.0 • BHADURI S ET AL: "Coupling of catalysis by carbonyl clusters and dehydrigenases: (73) Proprietor: EASTMAN CHEMICAL COMPANY Redution of pyruvate to L-lactate by dihydrogen" Kingsport, TN 37660 (US) JOURNAL OF THE AMERICAN CHEMICAL SOCIETY., vol. 120, no. 49, 11 October 1998 (72) Inventors: (1998-10-11), pages 12127-12128, XP002148358 • HEMBRE, Robert, T. DC US cited in the application Johnson City, TN 37601 (US) • OTSUKA K: "Regeneration of NADH and ketone • WAGENKNECHT, Paul, S. hydrogenation by hydrogen with the San Jose, CA 95129 (US) combination of hydrogenase and alcohol • PENNEY, Jonathan, M. -
Of Drug 45, 142, 144, 346, 414 ACE Inhibitors 1
479 Index a –– voltage-gated ion channel state Abl inhibition 359 transitions 297, 298 absorption, distribution, metabolism, and – prolongation 298 elimination (ADME), of drug 45, 142, 144, – simulated cardiac, in M cells 297, 299, 300 346, 414 – simulations 303, 304, 320 ACE inhibitors 10, 12 – stratification of AP timings 301 acetaminophen 176, 374 – supra-AP timescales 300 – inhibitors, protects against hepatotoxicity – waveform 298, 304 in vivo 376 activity-based protein profiling (ABPP) 390 – liver damage 125 acute coronary syndrome (ACS) 281, 331, – overdose 110 337 acetylation 89 acute liver injury (ALI) 88, 96, 110, 115–118, acetylators 89 120 acetylcysteine (AC) 110, 113, 115 acute lymphoblastic leukemia (ALL) 332, 333, acetylhydrazine 89 377, 401 acetyl isoniazid 89 acylcarnitines 112, 115, 116 acne 341, 342, 344, 380, 458 administration route, of drugs 52, 53 action potential 258 α2 adrenergic receptor (α2 AR) 22 – AP/QT prolongation adrenergic receptor antagonists 10 –– as a torsadogenicity biomarker 320 β-adrenergic receptors (β-ADRs) 35, 235 – duration 304 adrenocorticotropic hormone (ACTH) – estimation of proarrhythmic hERG 465 occupancy levels based on 304 ADRs. See adverse drug reactions (ADRs) –– nontrappable blockers 305 adverse drug reactions (ADRs) 3, 4, 6–8, 14, 15, –– trappable blockers 304 457 – isomorphic lengthening 298 – as a drug-induced disease 30 – normal AP and proarrhythmic – as drug-induced diseases 29 abnormalities 296 – multiscale models of 30, 31 –– abnormal calcium channel reopening – primary toxicity -
Supplementary Table S1 List of Proteins Identified with LC-MS/MS in the Exudates of Ustilaginoidea Virens Mol
Supplementary Table S1 List of proteins identified with LC-MS/MS in the exudates of Ustilaginoidea virens Mol. weight NO a Protein IDs b Protein names c Score d Cov f MS/MS Peptide sequence g [kDa] e Succinate dehydrogenase [ubiquinone] 1 KDB17818.1 6.282 30.486 4.1 TGPMILDALVR iron-sulfur subunit, mitochondrial 2 KDB18023.1 3-ketoacyl-CoA thiolase, peroxisomal 6.2998 43.626 2.1 ALDLAGISR 3 KDB12646.1 ATP phosphoribosyltransferase 25.709 34.047 17.6 AIDTVVQSTAVLVQSR EIALVMDELSR SSTNTDMVDLIASR VGASDILVLDIHNTR 4 KDB11684.1 Bifunctional purine biosynthetic protein ADE1 22.54 86.534 4.5 GLAHITGGGLIENVPR SLLPVLGEIK TVGESLLTPTR 5 KDB16707.1 Proteasomal ubiquitin receptor ADRM1 12.204 42.367 4.3 GSGSGGAGPDATGGDVR 6 KDB15928.1 Cytochrome b2, mitochondrial 34.9 58.379 9.4 EFDPVHPSDTLR GVQTVEDVLR MLTGADVAQHSDAK SGIEVLAETMPVLR 7 KDB12275.1 Aspartate 1-decarboxylase 11.724 112.62 3.6 GLILTLSEIPEASK TAAIAGLGSGNIIGIPVDNAAR 8 KDB15972.1 Glucosidase 2 subunit beta 7.3902 64.984 3.2 IDPLSPQQLLPASGLAPGR AAGLALGALDDRPLDGR AIPIEVLPLAAPDVLAR AVDDHLLPSYR GGGACLLQEK 9 KDB15004.1 Ribose-5-phosphate isomerase 70.089 32.491 32.6 GPAFHAR KLIAVADSR LIAVADSR MTFFPTGSQSK YVGIGSGSTVVHVVDAIASK 10 KDB18474.1 D-arabinitol dehydrogenase 1 19.425 25.025 19.2 ENPEAQFDQLKK ILEDAIHYVR NLNWVDATLLEPASCACHGLEK 11 KDB18473.1 D-arabinitol dehydrogenase 1 11.481 10.294 36.6 FPLIPGHETVGVIAAVGK VAADNSELCNECFYCR 12 KDB15780.1 Cyanovirin-N homolog 85.42 11.188 31.7 QVINLDER TASNVQLQGSQLTAELATLSGEPR GAATAAHEAYK IELELEK KEEGDSTEKPAEETK LGGELTVDER NATDVAQTDLTPTHPIR 13 KDB14501.1 14-3-3 -
SARCOSINE OXIDASE from Microorganism
SAO-351 ●TOYOBO ENZYMES● (Diagnostic Reagent Grade) SARCOSINE OXIDASE from Microorganism Sarcosine:oxygen oxidoreductase(demethylating) (EC 1.5.3.1) Sarcosine + O2 + H2O Glycine + Formaldehyde + H2O2 PREPARATION and SPECIFICATION Appearance : Yellowish amorphous powder, lyophilized Activity : GradeⅢ 8.0U/mg-solid or more Contaminant : Catalase ≤1.0% Stabilizers : Potassium chloride PROPERTIES Stability : Stable at −20℃ for at least one year (Fig.1) Molecular weight : approx.43,000 (by SDS-PAGE) Isoelectric point : 4.8±0.1 Michaelis constant : 2.8×10-3M Inhibitors : Cu++, Ag+, Hg++, p-chloromercuribenzoate, N-ethylmaleimide, SDS Optimum pH : 7.5−8.5 (Fig.2) Optimum temperature : 55−60℃ (Fig.3) pH Stability : 6.0−9.5 (25℃, 20hr) (Fig.4) Thermal stability : below 60℃ (pH 7.5, 30min) (Fig.5) Effect of various chemicals : (Table.1) APPLICATIONS This enzyme is useful for enzymatic determination of creatinine, creatine, and sarcosine when coupled with creatinine amidohydrolase (CNH-211, CNH-311) and creatine amidinohydrolase (CRH-211, CRH- 221, CRH-229). 237 SAO-351 ASSAY Principle: sarcosine oxidase Sarcosine+O2+H2O Glycine+Formaldehyde+H2O2 peroxidase 2H2O2+4-Aminoantipyrine+Phenol Quinoneimine dye+4H2O Unit definition: One unit causes the formation of one micromole of hydrogen peroxide (half a micromole of quinoneimine dye) per minute under the conditions described below. Method: Reagents A. Sarcosine solution : 0.2M[Weight 1.78g of sarcosine (MW=89.09), dissolve in 80ml of 0.125M Tris- HCl buffer, pH8.0 containing 0.125% of Triton X-100 and, after adjusting pH 8.0 at 25℃ with 1.0N NaOH or 1.0N HCl, fill up to 100ml with H2O.](Stable for one week if stored at 0−5℃) B. -
University of Groningen Exploring the Cofactor-Binding and Biocatalytic
University of Groningen Exploring the cofactor-binding and biocatalytic properties of flavin-containing enzymes Kopacz, Malgorzata IMPORTANT NOTE: You are advised to consult the publisher's version (publisher's PDF) if you wish to cite from it. Please check the document version below. Document Version Publisher's PDF, also known as Version of record Publication date: 2014 Link to publication in University of Groningen/UMCG research database Citation for published version (APA): Kopacz, M. (2014). Exploring the cofactor-binding and biocatalytic properties of flavin-containing enzymes. Copyright Other than for strictly personal use, it is not permitted to download or to forward/distribute the text or part of it without the consent of the author(s) and/or copyright holder(s), unless the work is under an open content license (like Creative Commons). The publication may also be distributed here under the terms of Article 25fa of the Dutch Copyright Act, indicated by the “Taverne” license. More information can be found on the University of Groningen website: https://www.rug.nl/library/open-access/self-archiving-pure/taverne- amendment. Take-down policy If you believe that this document breaches copyright please contact us providing details, and we will remove access to the work immediately and investigate your claim. Downloaded from the University of Groningen/UMCG research database (Pure): http://www.rug.nl/research/portal. For technical reasons the number of authors shown on this cover page is limited to 10 maximum. Download date: 29-09-2021 Exploring the cofactor-binding and biocatalytic properties of flavin-containing enzymes Małgorzata M. Kopacz The research described in this thesis was carried out in the research group Molecular Enzymology of the Groningen Biomolecular Sciences and Biotechnology Institute (GBB), according to the requirements of the Graduate School of Science, Faculty of Mathematics and Natural Sciences. -
(12) United States Patent (10) Patent No.: US 6,867,012 B2 Kishimoto Et Al
USOO6867O12B2 (12) United States Patent (10) Patent No.: US 6,867,012 B2 Kishimoto et al. (45) Date of Patent: Mar. 15, 2005 (54) DETERMINATION METHOD OF FOREIGN PATENT DOCUMENTS BIOLOGICAL COMPONENT AND REAGENT EP O 437 373 A 7/1991 KIT USED THEREFOR EP O 477 OO1 A 3/1992 JP P2001-17198 A 1/2001 (75) Inventors: Takahide Kishimoto, Tsuruga (JP); WO WO 99/47559 A 9/1999 Atsushi Sogabe, Tsuruga (JP); Shizuo WO WO OO/28071 A 5/2000 Hattori, Tsuruga (JP); Masanori Oka, Tsuruga (JP); Yoshihisa Kawamura, OTHER PUBLICATIONS Tsuruga (JP) van Dijken et al (Archives of microbiol, V.111(1-2), pp (73) Assignee: Toyo Boseki Kabushiki Kaisha, Osaka 77-83,(Dec. 1976)(Abstract Only).* (JP) (List continued on next page.) (*) Notice: Subject to any disclaimer, the term of this Primary Examiner Louise N. Leary patent is extended or adjusted under 35 (74) Attorney, Agent, or Firm-Kenyon & Kenyon U.S.C. 154(b) by 330 days. (57) ABSTRACT The present invention provides novel glutathione-dependent (21) Appl. No.: 09/998,130 formaldehyde dehydrogenase that makes possible quantita (22) Filed: Dec. 3, 2001 tive measurement of formaldehyde by cycling reaction, and a determination method of formaldehyde and biological (65) Prior Publication Data components, Such as creatinine, creatine, and homocysteine, US 2002/0119507 A1 Aug. 29, 2002 which produces formaldehyde as a reaction intermediate. In addition, the present invention provides a reagent kit for the (30) Foreign Application Priority Data above-mentioned determination method. The present inven tion provides a novel determination method of a homocys Dec. -
Identification of Folate Binding Protein of Mitochondria As Dimethylglycine Dehydrogenase (Flavoprotein/Sarcosine Dehydrogenase/Tetrahydrofolate) ARTHUR J
Proc. Natl. Acad. Sci. USA Vol. 77, No. 8, pp. 4484-4488, August 1980 Biochemistry Identification of folate binding protein of mitochondria as dimethylglycine dehydrogenase (flavoprotein/sarcosine dehydrogenase/tetrahydrofolate) ARTHUR J. WITTWER* AND CONRAD WAGNERt Department of Biochemistry, Vanderbilt University and Veterans Administration Medical Center, Nashville, Tennessee 37203 Communicated by Sidney P. Colowick, April 24,1980 ABSTRACT The folate-binding protein of rat liver mito- Preparation of Tetrahydro[3H]folic Acid (H4[3HJPteGIu). chondria [Zamierowski, M. & Wagner, C. (1977) J. BioL Chem. [3',5',7,9-3H]PteGlu, potassium salt (20 Ci/mmol; 1 Ci = 3.7 252,933-9381 has been purified to homogeneity by a combina- tion of gel filtration, DEAE-cellulose, and affinity chromatog- X 101' becquerels) was obtained from Amersham. Unlabeled raphy. This protein was assayed by its ability to bind tetrahv- PteGlu (Sigma) was added to adjust the specific activity to 20 dro[3H folic acid in vitro. The purified protein contains tightly ,uCi/Amol. H4[3',5',7,9-3H]PteGlu was synthesized by chemical bound flavin and has a molecular weight of about 90,000 as reduction with NaBH4 (2). To 0.70 ml of 0.066 M Tris-HCI at determined by sodium dodecyl sulfate electrophoresis. This pH 7.8 was added 0.30 ml of a solution containing 0.40 protein also displays dimethylglycine deh drogenase [NN- ,gmol dimethylglycine: (acceptor) oxidoreductase (deme ylating), EC (8 ,Ci) of [3H]PteGlu. This solution was stirred in the dark 1.5.99.21 activity which copurifies with the folatebinding ac- under nitrogen at room temperature, and 0.25 ml of NaBH4 tivity. -
Genetic Manipulation of Glycine Decarboxylation
Journal of Experimental Botany, Vol. 54, No. 387, pp. 1523±1535, June 2003 DOI: 10.1093/jxb/erg171 REVIEW ARTICLE Genetic manipulation of glycine decarboxylation Hermann Bauwe1 and UÈ ner Kolukisaoglu Abteilung P¯anzenphysiologie der UniversitaÈt Rostock, Albert-Einstein-Strasse 3, D-18051 Rostock, Germany Received 2 October 2002; Accepted 11 March 2003 Downloaded from https://academic.oup.com/jxb/article/54/387/1523/540368 by guest on 26 September 2021 Abstract complex that occurs in all organisms, prokaryotes and eukaryotes. GDC, together with serine hydroxymethyl- The glycine±serine interconversion, catalysed by gly- transferase (SHMT), is responsible for the inter-conversion cine decarboxylase and serine hydroxymethyltransfer- of glycine and serine, an essential and ubiquitous step of ase, is an important reaction of primary metabolism in primary metabolism. In Escherichia coli, 15% of all all organisms including plants, by providing one-car- carbon atoms assimilated from glucose are estimated to bon units for many biosynthetic reactions. In plants, pass through the glycine±serine pathway (Wilson et al., in addition, it is an integral part of the photorespira- 1993). In eukaryotes, GDC is present exclusively in the tory metabolic pathway and produces large amounts mitochondria, whereas isoforms of SHMT also occur in the of photorespiratory CO within mitochondria. 2 cytosol and, in plants, in plastids. The term `glycine±serine Although controversial, there is signi®cant evidence that this process, by the relocation of glycine decar- interconversion' might suggest that the central importance boxylase within the leaves from the mesophyll to the of this pathway is just the synthesis of serine from glycine and vice versa.